WO2025229019A1

WO2025229019A1 - Neutralizing antibody constructs against hiv

Info

Publication number: WO2025229019A1
Application number: PCT/EP2025/061760
Authority: WO
Inventors: Tiancen HU; Mark R. Krystal; James SCHAWALDER; Eric Arnoult
Original assignee: ViiV Healthcare UK No 5 Ltd
Current assignee: ViiV Healthcare UK No 5 Ltd
Priority date: 2024-04-30
Filing date: 2025-04-29
Publication date: 2025-11-06
Anticipated expiration: 2026-10-30

Abstract

Antigen binding proteins of the invention bind to Human Immunodeficiency Virus (HIV) envelope protein and are useful in treating and preventing HIV infection. In particular, the antigen binding proteins of the V1/V2 apex region of glycoprotein 120 (gp120) or the gp120-gp41 interface region of gp120 and gp41 as well as having a CD4 domain that binds to the CD4bs of gp120.

Description

ANTIGEN BINDING PROTEINS FIELD OF THE INVENTION _{The invention is directed to a multimeric antigen binding protein that binds to the Human} Immunodeficiency Virus (HIV) envelope spike complex and its use in treating or preventing HIV _{infection. The antigen binding proteins of the invention bind to the V1/V2 apex region of} _{glycoprotein 120 (gp120) or the gp120-gp41 interface region of gp120 and gp41 as well as having a} _{CD4 domain that binds to the CD4bs of gp120. The antigen binding proteins of the invention may} _{also bind to at least one complex N-glycan on a gp120 or a gp41 protein as well as having a CD4} domain that binds to the CD4bs of gp120. BACKGROUND TO THE INVENTION HIV, the virus that over time may result in Acquired Immunodeficiency Syndrome (AIDS), continues to be a serious public health challenge and has claimed 40.1 million lives so far. HIV attacks the body’s immune system, targeting CD4-positive white blood cells, and leaves those infected vulnerable to opportunistic infections such as tuberculosis and fungal infections, severe bacterial infections and some cancers. Globally, 38.4 million people were living with HIV at the end of 2021, with 1.5 million people becoming newly infected (WHO, Key Facts HIV, July 2022). Whilst there is currently no cure for HIV infection, it can be treated with antiretroviral therapy (ART), which includes a number of different types of drugs that prevent the virus from multiplying (nucleoside reverse transcriptase inhibitors (NRTIs), non-nucleoside reverse transcriptase inhibitors (NNRTIs), protease inhibitors, entry inhibitors and integrase inhibitors), allowing the body’s immune system to recover sufficiently for the infected patient to be asymptomatic. 75% of people living with HIV in 2021 received some form of ART. However, ART often requires taking medication every day for life and has the risk of serious and debilitating side effects. Further, increased use of ART has also been accompanied by the emergence of drug resistance, the levels of which have steadily increased in recent years. Broadly neutralizing antibodies (bNAbs) could potentially provide longer-term HIV suppression, but individual bNAbs have only had limited success in previous studies. This is in part _{because antibody-resistant virus either already existed in the patient or emerged soon after} treatment began (NIH Research Matters, 14 June 2022). Combinations of bNAbs are currently being investigated in the presence or absence of ART (Nature, 606, 368-374, 2022). Further treatment options are needed for HIV infection, in particular drugs that are long- acting and effective against a wide spectrum of HIV strains so that patients taking them are less susceptible to drug resistance. SUMMARY OF THE INVENTION _{In a first aspect of the invention, there is provided a multimeric anti-HIV envelope spike complex-} binding protein comprising: i_{. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at least one} heavy chain or light chain, wherein the antibody binds to the V1/V2 loop of a gp120 protein or the gp120-gp41 interface region of a gp120 and a gp41 protein; and i_{i. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached} directly or by a linker to the N-terminus or C-terminus of at least one of the heavy chains or light chains of the broadly neutralizing antibody. In a second aspect of the invention, there is provided a multimeric anti-HIV envelope spike complex- binding protein comprising: i_{. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at least one} heavy chain or light chain, wherein the antibody binds to at least one complex N-glycan on a gp120 protein or a gp41 protein; and i_{i. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached} directly or by a linker to the N-terminus or C-terminus of at least one of the heavy chains or light chains of the broadly neutralizing antibody. In further aspects of the invention, pharmaceutical compositions comprising anti-HIV envelope spike complex-binding proteins of the invention, methods of preventing HIV infection and methods of treating HIV infection with anti-HIV envelope spike complex-binding proteins of the invention, uses of anti-HIV envelope spike complex-binding proteins of the invention, methods of manufacturing anti-HIV envelope spike complex-binding proteins of the invention and kits comprising anti-HIV envelope spike complex-binding proteins of the invention are also provided. DESCRIPTION OF DRAWINGS/FIGURES F_{IG. 1 shows schematic designs of example bispecific binding proteins of the invention.} Human CD4 domains or variants thereof are fused, either directly or via linkers, to the N-termini the heavy chains (A), the light chains (B) or to the N-termini of the heavy chains (C) or light chains (D) of bNAbs. Such designs facilitate concomitant binding of the human CD4 domain of the bispecific _{molecule and gp160 binding domain (or in other words, the envelope spike complex broad} neutralizing antibody or fragment) of the bispecific molecule to HIV-1 gp160 (the envelope spike complex) and prevent HIV-1 virions from binding to the cell surface receptors and fusing with the cell membrane (E-F). F_{IG. 2 shows IC50 values (nM) of soluble CD4 domains (SEQ ID NOs:4-15) against a panel} of HIV-1 envelopes in a PSV assay (ACTOne), together with the Tm for each soluble CD4 domain. The horizontal bars indicate geometric mean IC50. F_{IG. 3 shows that linker length between the CD4 domain and a similar model bNAb to the} _{invention (V3-bNAb1) heavy chain N-terminus does not particularly affect anti-viral activity in a PSV} assay (ACTOne) (A) but does change the PK of the resultant bispecific molecules in a humanized mouse model (Tg32-hFcRn strain) (B). Thermal stability of the CD4 domain also affects the PK of the bispecific molecules (B). F_{IG. 4 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} _{bNAb1-derived bispecifics (targeting the V1/V2 Apex) according to the invention summarised in} Table 1 below. Where the bispecific contains the CD4 at the HC, the HC sequence includes the linker _{and the CD4 domain (e.g. SEQ ID NOs: 74 and 421), equally where the bispecific contains the CD4} _{at the LC, the LC sequence includes the linker and the CD4 domain (e.g. 420 and 422). (A-C) shows} _{anti-viral activity of Apex-bNAb1-derived bispecifics and control molecules against a panel of HIV-1} _{envelopes in a PSV assay (ACTOne cells); (D-F) shows anti-viral activity of Apex-bNAb1-derived} _{bispecifics with CD4 domain fused at different positions against a panel of HIV-1 envelopes in a PSV} _{assay (ACTOne cells); (G-J) shows anti-viral activity of a Apex-bNAb1-derived bispecific against a} diverse panel of 119 HIV-1 envelopes (Seaman et al., J Virol. 2010 Feb;84(3):1439-52.) in a PSV assay (TZM.bl cells). (_{A), (D), and (G) shows IC50; (H) shows IC80; (B), (E) and (I) shows IC90; and (C), (F) and} (J) show MPI. _{Table 1 – Figure 4 molecule key (SEQ ID NOs:)} _{SEQ ID NO HC LC} CDR CDR CDR CDR CDR CDR H1 H2 H3 L1 L2 L3 _{VH VL} _{Bispecific1-1 (74)} (CD4 at N-terminus of HC) _{74 254 244 245 246 247 248 249 250 251} _{Bispecific1-2 (420)} (CD4 at N-terminus of LC) _{253 420 244 245 246 247 248 249 250 251} _{Bispecific1-3 (421)} (CD4 at C-terminus of HC) _{421 254 244 245 246 247 248 249 250 251} _{Bispecific1-4 (422) 253 422 244 245 246 247 248 249 250 251} (CD4 at C-terminus of LC) A_{pex-bNAb1 253 254 244 245 246 247 248 249 250 251} CD4 = D1m-K8C-G99C_Fc (SEQ ID NO: 53) Combo = mixture of Apex-bNAb1 and CD4 at 1:1 molar ratio F_{IG. 5 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} _{bNAb2-derived bispecifics (targeting the V1/V2 Apex) according to the invention summarized in} Figure 5 below. Where the bispecific contains the CD4 at the HC, the HC sequence includes the linker and the CD4 domain (e.g. SEQ ID NOs: 75 and 424), equally where the bispecific contains the _{CD4 at the LC, the LC sequence includes the linker and the CD4 domain (e.g. 423 and 425). (A-C)} _{shows anti-viral activity of Apex-bNAb2-derived bispecifics and control molecules against a panel of} _{HIV-1 envelopes in a PSV assay (ACTOne cells); (D-F) shows anti-viral activity of Apex-bNAb2-} _{derived bispecifics with CD4 domain fused at different positions against a panel of HIV-1 envelopes} _{in a PSV assay (ACTOne cells); (G-J) shows anti-viral activity of a Apex-bNAb2-derived bispecific} against a diverse panel of 119 HIV-1 envelopes (Seaman et al., J Virol. 2010 Feb;84(3):1439-52.) in _{a PSV assay (TZM.bl cells).} _{Table 2 – Figure 5 molecule key (SEQ ID NOs:)} _{SEQ ID NO HC LC} CDR CDR CDR CDR CDR CDR H1 H2 H3 L1 L2 L3 _{VH VL} _{Bispecific2-1 (75)} (CD4 at N-terminus of HC) _{75 265 255 256 257 258 259 260 261 262} _{Bispecific2-2 (423)} (CD4 at N-terminus of LC) _{264 423 255 256 257 258 259 260 261 262} _{Bispecific2-3 (424)} (CD4 at C-terminus of HC) _{424 265 255 256 257 258 259 260 261 262} _{Bispecific2-4 (425)} (CD4 at C-terminus of LC) _{264 425 255 256 257 258 259 260 261 262} _{bNAb2 264 265 255 256 257 258 259 260 261 262} CD4 = D1m-K8C-G99C_Fc (SEQ ID NO: 53) Combo = mixture of the bNAb and CD4 at 1:1 molar ratio F_{IG. 6 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} bNAb3-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC _{including a linker + CD4 domain as per SEQ ID NO: 76 and a LC according to SEQ ID NO: 276) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} _{FIG. 7 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} bNAb4-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC _{including a linker + CD4 domain as per SEQ ID NO: 77 and a LC according to SEQ ID NO: 287) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} _{FIG. 8 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} bNAb5-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC _{including a linker + CD4 domain as per SEQ ID NO: 78 and a LC according to SEQ ID NO: 298) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} _{FIG. 9 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} _{bNAb6-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC} _{including a linker + CD4 domain as per SEQ ID NO: 79 and a LC according to SEQ ID NO: 309) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} _{FIG. 10 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} bNAb7-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC _{including a linker + CD4 domain as per SEQ ID NO: 80 and a LC according to SEQ ID NO: 320) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} _{FIG. 11 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} bNAb8-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC _{including a linker + CD4 domain as per SEQ ID NO: 81 and a LC according to SEQ ID NO: 331) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} _{FIG. 12 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} bNAb9-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC _{including a linker + CD4 domain as per SEQ ID NO: 82 and a LC according to SEQ ID NO: 342) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} _{FIG. 13 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} bNAb10-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC _{including a linker + CD4 domain as per SEQ ID NO: 83 and a LC according to SEQ ID NO: 353) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} _{FIG. 14 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} bNAb11-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC _{including a linker + CD4 domain as per SEQ ID NO: 84 and a LC according to SEQ ID NO: 364) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} _{FIG. 15 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} bNAb12-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC _{including a linker + CD4 domain as per SEQ ID NO: 85 and a LC according to SEQ ID NO: 375) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} _{FIG. 16 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} bNAb13-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC _{including a linker + CD4 domain as per SEQ ID NO: 86 and a LC according to SEQ ID NO: 386) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} _{FIG. 17 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} bNAb14-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC _{including a linker + CD4 domain as per SEQ ID NO: 87 and a LC according to SEQ ID NO: 397) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} _{FIG. 18 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} bNAb15-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC _{including a linker + CD4 domain as per SEQ ID NO: 88 and a LC according to SEQ ID NO: 408) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} _{FIG. 19 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Apex-} bNAb16-derived bispecifics according to the invention (targeting the V1/V2 Apex, containing a HC _{including a linker + CD4 domain as per SEQ ID NO: 89 and a LC according to SEQ ID NO: 419) and} _{control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells).} FIG. 20 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface- bNAb17-derived bispecifics according to the invention (targeting the gp120-gp41 interface, _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 60 and a LC according to SEQ} _{ID NO: 100) and control molecules (A-C) against a panel of HIV-1 envelopes in a PSV assay} _{(ACTOne cells) and (D-G) against a diverse panel of 119 HIV-1 envelopes.} _{FIG. 21 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface} -bNAb18-derived bispecifics according to the invention (targeting the gp120-gp41 interface, _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 61 and a LC according to SEQ} _{ID NO: 111) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne} cells). F_{IG. 22 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface} -bNAb19-derived bispecifics according to the invention (targeting the gp120-gp41 interface, _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 62 and a LC according to SEQ} _{ID NO: 122) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne} cells). F_{IG. 23 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface} -bNAb20-derived bispecifics according to the invention (targeting the gp120-gp41 interface, _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 63 and a LC according to SEQ} _{ID NO: 133) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne} cells). F_{IG. 24 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface} -bNAb21-derived bispecifics according to the invention (targeting the gp120-gp41 interface, _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 64 and a LC according to SEQ} _{ID NO: 144) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne} cells). F_{IG. 25 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface} -bNAb22-derived bispecifics according to the invention (targeting the gp120-gp41 interface, _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 65 and a LC according to SEQ} ID NO: 155) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne cells). F_{IG. 26 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface} -bNAb23-derived bispecifics according to the invention (targeting the gp120-gp41 interface, _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 66 and a LC according to SEQ} _{ID NO: 166) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne} cells). F_{IG. 27 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface} -bNAb24-derived bispecifics according to the invention (targeting the gp120-gp41 interface, _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 67 and a LC according to SEQ} _{ID NO: 177) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne} cells). F_{IG. 28 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface} _{bNAb25-derived bispecifics according to the invention (targeting the gp120-gp41 interface,} _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 68 and a LC according to SEQ} _{ID NO: 188) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne} cells). F_{IG. 29 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface} bNAb26-derived bispecifics according to the invention (targeting the gp120-gp41 interface, _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 69 and a LC according to SEQ} _{ID NO: 199) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne} cells). F_{IG. 30 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface} bNAb27-derived bispecifics according to the invention (targeting the gp120-gp41 interface, _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 70 and a LC according to SEQ} _{ID NO: 210) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne} cells). F_{IG. 31 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface} bNAb29-derived bispecifics according to the invention (targeting the gp120-gp41 interface, _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 71 and a LC according to SEQ} _{ID NO: 221) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne} cells). F_{IG. 32 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface} bNAb30-derived bispecifics according to the invention (targeting the gp120-gp41 interface, _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 72 and a LC according to SEQ} _{ID NO: 232) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne} cells). F_{IG. 33 shows IC50 (nM), IC90 (nM) and MPV (%) values for anti-viral activity of Interface} _{bNAb31-derived bispecifics according to the invention (targeting the gp120-gp41 interface,} _{containing a HC including a linker + CD4 domain as per SEQ ID NO: 73 and a LC according to SEQ} _{ID NO: 243) and control molecules against a panel of HIV-1 envelopes in a PSV assay (ACTOne} cells). DETAILED DESCRIPTION OF THE INVENTION DEFINITIONS “Affinity”, also referred to as “binding affinity”, is the strength of binding at a single interaction site, i.e., of one molecule, e.g., an antigen binding protein, to another molecule, e.g., its target antigen, at a single binding site. The binding affinity of an antigen binding protein to its target may be determined by equilibrium methods (e.g., enzyme-linked immunoabsorbent assay (ELISA) or radioimmunoassay (RIA)), or kinetics (e.g., BIACORE analysis). “Alternative antibody formats” include alternative scaffolds in which one or more CDRs of the antigen binding protein can be arranged onto a suitable non-immunoglobulin protein scaffold 5 or skeleton, such as an affibody, a SpA scaffold, an LDL receptor class A domain, an avimer (see, e.g., U.S. Patent Application Publication Nos. 2005/0053973, 2005/0089932, 2005/0164301) or an EGF domain. “Antibody” is used herein to refer to a heterotetrameric glycoprotein with an approximate molecular weight of 150,000 daltons. An intact antibody is composed of two identical heavy chains (HCs) and two identical light chains (LCs) linked by covalent disulphide bonds. This H2L2 structure folds to form a ‘Y’ shape with three functional domains comprising two antigen-binding fragments, known as ‘Fab’ fragments (the ‘top’ of the ‘Y’), and a fragment 9crystallisable 99‘Fc’ (the ‘bottom’ of the ‘Y’). The Fab fragment is composed of the variable domain at the amino-terminus, variable heavy (VH) or variable light (VL), and the constant domain at the carboxyl terminus, CH1 (heavy) and CL (light). The Fc fragment is composed of two domains formed by dimerization of paired CH2 and CH3 regions. The Fc may elicit effector functions by binding to receptors on immune cells or by binding C1q, the first component of the classical complement pathway. The five classes of antibodies IgM, IgA, IgG, IgE and IgD are defined by distinct heavy chain amino acid sequences, which are called µ, α, γ, ε and δ respectively; each heavy chain can pair with either a Κ or λ light chain. The majority of antibodies in the serum belong to the IgG class, there are four isotypes of human IgG (IgG1, IgG2, IgG3 and IgG4), the sequences of which differ mainly in their hinge region. In an embodiment, an anti-CD4bs antibody, as used herein, refers to an antibody that binds to a CD4 binding site “Antigen binding antibody fragments” or “antigen binding fragments” or “antibody fragments” as used herein include Fab, F(ab’)2, Fv, disulphide linked Fv, single chain Fv (scFv), disulphide-linked scFv, diabodies, TANDABS, etc. and modified versions of any of the foregoing (for a summary of alternative “antibody” formats see Holliger and Hudson, Nature Biotechnology, 23(9), 1126-1136, 2005). “_{Antigen binding protein of the invention” and “anti-HIV envelope spike complex} binding protein” are used interchangeably herein and refer to antibodies and fragments thereof, alternative antibody formats, and other protein constructs, such as domains, that are capable of _{binding to the HIV envelope spike complex comprised of gp120 and gp41, or in other words are} capable of binding to either gp120 or gp41. The HIV env gene encodes a gene product of around _{850 amino acids. The primary env product is the protein gp160 (or envelope glycoprotein gp160)} which is gets cleaved into gp120 (about 480 amino acids) and gp41 (about 345 amino acids) in the _{endoplasmic reticulum by the cellular protease furin. Gp120 (or gp120) is a 120 kDa glycoprotein} that is part of the outer layer of HIV. It presents itself as viral membrane spikes consisting of three molecules of gp120 linked together and anchored to the membrane by gp41 protein. Gp120 is essential for viral infection as it facilitates HIV entry into the host cell through its interaction with cell _{surface receptors. Gp41 is a transmembrane protein that contains several sites within its ectodomain} that are required for infection of host cells. The amino acid sequence of an exemplary gp160 from HIV clone WITO is provided below (SEQ ID NO: 55): MKVMGTKKNYQHLWRWGIMLLGMLMMSSAAEQLWVTVYYGVPVWREANTTLFCASDAKAYDTEVHNVWAT HACVPTDPNPQEVVMGNVTEDFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLHCTNVTISSTNGSTA NVTMREEMKNCSFNTTTVIRDKIQKEYALFYKLDIVPIEGKNTNTSYRLINCNTSVITQACPKVSFEPIPIHYCAPA GFAILKCNNKTFNGKGPCRNVSTVQCTHGIKPVVSTQLLLNGSLAEEDIIIRSENFTNNGKNIIVQLKEPVKINCT RPGNNTRRSINIGPGRAFYATGAIIGDIRKAHCNISTEQWNNTLTQIVDKLREQFGNKTIIFNQSSGGDP EVVMHTFNCGGEFFYCNSTQLFNSTWFNNGTSTWNSTADNITLPCRIKQVINMWQEVGKAMYAPPIRGQIDCS SNITGLILTRDGGSNSSQNETFRPGGGNMKDNWRSELYKYKVVKIEPLGIAPTRAKRRVVQREKRAVTLGAVFLG FLGAAGSTMGAASLTLTVQARLLLSGIVQQQSNLLRAIEAQQHMLQLTVWGIKQLQARVLAIERYLKDQQLLGI WGCSGKLICTTTVPWNTSWSNKSYDYIWNNMTWMQWEREIDNYTGFIYTLIEESQNQQEKNELELLELDKWA SLWNWFNITNWLWYIKLFIMIIGGLVGLRIVCAVLSIVNRVRQGYSPLSFQTRLPNPRGPDRPEETEGEGGERDR DRSARLVNGFLAIIWDDLRSLCLFSYHRLRDLLLIVARVVEILGRRGWEILKYWWNLLKYWSQELKNSAVSLLNV TAIAVAEGTDRVIEIVQRAVRAILHIPTRIRQGFERALL The amino acid of an exemplary gp120 is provided below (SEQ ID NO: 56): AEQLWVIVYYGVPVWREANTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVMGNVTEDFNMWKNNMV EQMHEDIISLWDQSLKPCVKLTPLCVTLHCTNVTISSTNGSTANVTMREEMKNCSFNTTTVIRDKIQKEYALFYK LDIVPIEGKNTNTSYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGKGPCRNVSTVQCTHGIKP VVSTQLLLNGSLAEEDIIIRSENFTNNGKNIIVQLKEPVKINCTRPGNNTRRSINIGPGRAFYATGAIIGDIR KAHCNISTEQWNNTLTQIVDKLREQFGNKTIIFNQSSGGDPEVVMHTFNCGGEFFYCNSTQLFNSTWFNNGTS TWNSTADNITLPCRIKQVINMWQEVGKAMYAPPIRGQIDCSSNITGLILTRDGGSNSSQNETFRPGGGNMKDN WRSELYKYKVVKIEPLGIAPTRAKRRVVQREKR _{The amino acid of an exemplary gp41 is provided below (SEQ ID NO: 57):} AVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVER YLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNE QELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEG IEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQEL KNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL “Antigen binding site” and “paratope” are used interchangeably herein and refer to a particular site on an antigen binding protein that makes contact with and is capable of specifically binding to a site (i.e., epitope) on an antigen, e.g., HIV gp120. The antigen binding site may be formed by a single variable domain, or paired VH/VL domains as can be found on a standard antibody. Single-chain Fv (ScFv) domains can also provide antigen binding sites. “Avidity” also referred to as functional affinity, is the cumulative strength of binding at multiple interaction sites, e.g., the sum total of the strength of binding of two molecules (or more) to one another at multiple sites, e.g., taking into account the valency of the interaction. A “bispecific molecule” or “bispecific antigen binding protein” as used herein is an antigen binding protein that is capable of binding to two different epitopes on the same antigen, i.e., _{HIV gp160 protein/envelope spike complex. In particular, one epitope comprises part of or the} _{whole of the V1/V2 Apex region of gp120 or the interface region of gp120 and gp41, and the other} epitope comprises part of or the whole of the CD4 binding site of gp120. “Broadly neutralizing antibody” or “bNAb” as used herein, is meant an antibody that neutralizes more than one HIV-1 virus species (from diverse clades and different strains within a _{clade) in a neutralization assay. A broadly neutralizing antibody may neutralize at least 2, 3, 4, 5, 6,} 7, 8, 9 or more different strains of HIV-1, the strains belonging to the same or different clades. “CD4 binding site” or “CD4-binding site” or “CD4bs” refers to a site on the HIV envelope protein gp120 that binds to CD4. (Cluster of differentiation factor 4). CD4 is a T-cell surface protein that serves as the primary receptor site for HIV during HIV infection. The CD4 binding site on gp120 is a highly conserved, discontinuous and conformational that comprises residues on either side of the HIV V4 loop (Curr HIV/AIDS Rep, 9(1): 52-63, 2021) that binds to CD4. A “CD4 domain” as used herein is a soluble recombinant form of human CD4 (Cluster of differentiation factor 4, a transmembrane glycoprotein found on T-cells), or a fragment thereof, that mimics the activity of native membrane-anchored human CD4 in its binding interactions with the HIV envelope protein. A CD4 domain of the present invention binds to the CD4-binding site of HIV gp120 and may block the ability of HIV gp120 to bind membrane-anchored CD4, e.g., on CD4+ T cells. A CD4 domain of the invention may induce a structural rearrangement in gp120 upon _{binding, including a structural rearrangement of part or all of the V1/V2 Apex region of gp120} _{(PMID: 37993719). This structural rearrangement in gp120 results in a high affinity binding site for a} chemokine coreceptor (CXCR4 and/or CCR5) being exposed. Native CD4 comprises four domains that are exposed on the extracellular surface of the cell, D1, D2, D3 and D4; a transmembrane domain; and a cytoplasmic tail domain. D1 and D3 resemble Ig variable domains and D2 and D4 resemble Ig constant domains. CD4 domains of the invention include one or more of domains D1 to _{D4 of CD4, or variants thereof. Examples of CD4 domains of the Invention include wild-type D1} _{(SEQ ID NO:3); “mD1.22”/D1m (SEQ ID NO:4), which is a variant of D1 of CD4 (Chen et al, JVI} 88(2): 1125-39, 2014); wild-type D1D2 (SEQ ID NO:1); “mD1.22-D2” (SEQ ID NO:2), which is a variant of D1D2 (Fetzer et al., Journal of Virology, 92(12), 2018); and further variants of mD1.22 (SEQ ID NOs:5-21). “CDRs” are defined as the complementarity determining region amino acid sequences of an antigen binding protein. These are the hypervariable regions of immunoglobulin heavy and light chains. There are three heavy chain and three light chain CDRs (or CDR regions) in the variable portion of an immunoglobulin. In one embodiment, the CDRs are defined based on the Kabat definition. In another embodiment, the CDRs are defined based on the Chothia definition. In a further embodiment, the Chothia definition is from Discovery Studio which uses the definitions fromChothia and Lesk, Jmol Biol. 196(4):901-17 (1987) and Morea et al, Methods, 20:267-279 (2000). In another embodiment, the Chothia definition is based on the Chothia from Abysis definition. In a further embodiment, the CDRs are defined based on the IMGT definition. In another embodiment, the CDRs are defined based on the Honegger definition. In another embodiment, the _{CDRs are defined based on the contact definition. Thus, “CDRs” as used herein refers to all three} heavy chain CDRs, all three light chain CDRs, all heavy and light chain CDRs, or at least two CDRs. “Domain” refers to a folded polypeptide structure that retains its tertiary structure independent of the rest of the polypeptide. Generally, domains are responsible for discrete functional properties of polypeptides and in many cases may be added, removed or transferred to other polypeptides without loss of function of the remainder of the protein and/or of the domain. “Effector Function” as used herein refers to one or more of antibody-mediated effects including antibody-dependent cell-mediated cytotoxicity (ADCC), antibody-mediated complement activation including complement-dependent cytotoxicity (CDC), complement-dependent cell- mediated phagocytosis (CDCP), antibody dependent complement-mediated cell lysis (ADCML), and Fc-mediated phagocytosis or antibody-dependent cellular phagocytosis (ADCP). “_{Epitope” as used herein refers to the portion of an antigen (e.g., gp120) that makes} contact with and is capable of specifically binding to a particular site (paratope) on an antigen binding protein. An epitope may be linear or conformational/discontinuous. A conformational/ discontinuous epitope comprises amino acid residues that are separated by other sequences, i.e., it does not comprise a continuous sequence in the antigen’s primary amino acid sequence, but instead relies on the tertiary folding of the polypeptide. Although the residues within a confirmational/ discontinuous epitope may be from different regions of the polypeptide chain, they are in close proximity in the three-dimensional structure of the antigen. In the case of multimeric antigens, a conformational or discontinuous epitope may include residues from different polypeptide chains. Particular residues comprised within an epitope can be determined through computer modelling programs or via three-dimensional structures obtained through methods known in the art, such as X-ray crystallography. Epitope mapping can be carried out using various techniques known to persons skilled in the art as described in publications such as Methods in Molecular Biology ‘Epitope Mapping Protocols’, by Mike Schutkowski and Ulrich Reineke (volume 524, 2009) and Johan Rockberg and Johan Nilvebrant (volume 1785, 2018). Exemplary methods include peptide-based approaches such as pepscan whereby a series of overlapping peptides are screened for binding using techniques such as ELISA or by in vitro display of large libraries of peptides or protein mutants, e.g., on phage. Detailed epitope information can be determined by structural techniques including X-ray crystallography, solution nuclear magnetic resonance (NMR) spectroscopy and cryogenic-electron microscopy (cryo- EM). Mutagenesis, such as alanine scanning, is an effective approach whereby loss of binding analysis is used for epitope mapping. Another method is hydrogen/deuterium exchange (HDX) combined with proteolysis and liquid-chromatography mass spectrometry (LC-MS) analysis to characterize discontinuous or conformational epitopes. “Half-life” or “t1/2” refers to the time required for the serum concentration of an antigen binding protein to reach half of its original value. The serum half-life of proteins can be measured by pharmacokinetic studies according to the method described by Kim et al., 1994, Eur. J. of Immuno. 24: 542-548. According to this method, radio-labelled protein is injected intravenously into mice and its plasma concentration is periodically measured as a function of time, for example, at about 3 minutes to about 72 hours after the injection. Other methods for pharmacokinetic analysis and determination of the half-life of a molecule will be familiar to those skilled in the art. “HIV envelope spike complex” or “ENV” or “spike complex” refers to a trimeric viral _{membrane-associated glycoprotein (gp) or ‘spike’ comprised of non-covalently linked heterodimers} of surface gp120 and transmembrane gp41. It is found on both the viral membrane and the cell _{membrane of infected host cells and is encoded by the Env gene. The env gene encodes the gp160} polypeptide which forms a homotrimer and is cleaved into gp120 and gp41 polypeptides. Gp120 is a surface (SU) glycoprotein responsible for binding to receptor molecules and the transmembrane I glycoprotein, gp41, mediates fusion of the viral membrane with the plasma cell membrane. Over half of the mass of the trimeric envelope ‘spike’ is an N-linked glycan shield that hides most amino acid-based epitopes on gp120. Binding of the cell surface receptor CD4 to HIV gp120 induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor (CXCR4 and/or CCR5), on gp120. Following gp120 binding to CXCR4 or CCR5 further conformational changes are triggered which results in gp120 disengaging from gp41, allowing for the fusion peptide of gp41 to be inserted into the cell membrane, which in turn triggers a sequence of structural changes resulting in membrane fusion (Dimitrov et al., Biochemistry 44(37): 12471-12479, 2005). “Human immunodeficiency virus (HIV)” has been characterized into two types: HIV-1 and HIV-2. HIV-1 is more virulent and more infective than HIV-2 and is the cause of the majority of HIV infections globally, whereas HIV-2 is limited to a much smaller number of people, mostly in _{West Africa (Gilbert et al., Statistics in Medicine 22(4): 573-593). Thus, “HIV” may mean HIV-1 and} _{HIV-2, or just “HIV-1”. HIV virions are spherical with viral glycoprotein “spikes”, the HIV envelope} protein, protruding outwards. A conical capsid exists within the virion, enclosing a ribonucleoprotein complex comprising two copies of positive-sense single stranded RNA tightly bound to nucleocapsid _{proteins and enzymes needed for viral replication. “Symptoms” of HIV include raised temperature} (fever), sore throat, body rash, tiredness, joint pain, muscle pain, swollen glands, weight loss, chronic diarrhoea, night sweats, skin problems, recurrent infections, headaches. A_{“linker” is a suitable structure that can be used to join together the CD4 domain and} antibody or fragment of the invention. A linker may be a chemical linker such as PEG, or an amino _{acid sequence, that links one domain in a polypeptide to another domain in a polypeptide. For} example, a linker within the meaning of the invention includes an amino acid sequence that joins a CD4 domain to a bNAb heavy chain or a bNAb light chain. In an embodiment, the linker is not cleavable under intracellular conditions. “_{Multimeric antigen binding protein” or “Multispecific antigen binding protein”} refers to an antigen binding protein that comprises at least two different polypeptide chains having different antigen binding sites. Each of these antigen-binding sites is capable of binding to a different epitope, which may be present on the same antigen or different antigens. In an embodiment, the multi-specific antigen binding proteins of the invention are bispecific molecules capable of binding to two different epitopes on the HIV envelope protein. In particular, _{one epitope may comprise part of or the whole of to the V1/V2 loop of a gp120 protein or the} gp120-gp41 interface of a gp120 and a gp41 protein and the other epitope may comprise part of or _{the whole of the CD4 binding site of gp120 (through binding of the CD4 domain portion of the} molecule). Symmetric formats of MSABPs combine multiple binding specificities in a single polypeptide chain or single HL pair including Fc-fusion proteins of fragment-based formats and formats whereby antibody fragments are fused to regular antibody molecules. Examples of symmetric formats may include DVD-Ig, TVD-Ig, CODV-Ig, (scFv)4-Fc, IgG-(scFv)2, Tetravalent DART-Fc, F(ab)4CrossMab, IgG-HC-scFv, IgG-LC-scFv, mAb-dAb etc. A_{multimeric antigen binding protein described herein, for example, a bispecific antigen} _{binding protein having a broadly neutralizing anti-HIV envelope spike complex antibody and a CD4} _{domain, may be encoded by one or more isolated nucleic acid sequences. Production of a multimeric} _{antigen binding protein, such as a bispecific antigen binding protein, may be achieved in a cell or} _{living organism by delivering exogenous isolated nucleic acids encoding the multimeric antigen} _{binding protein, for example, a heavy chain and a light chain of a broadly neutralizing anti-HIV} _{envelope spike complex antibody and a CD4 domain. Production of a multimeric antigen binding} _{protein, such as a bispecific antigen binding protein, may be achieved in a cell in vitro or in vivo by} _{delivering exogenous isolated nucleic acids encoding the multimeric antigen binding protein, for} _{example, a heavy chain and a light chain of a broadly neutralizing anti-HIV envelope spike complex} _{antibody and a CD4 domain. A subject in need may be delivered one or more nucleic acids encoding} _{an multimeric antigen binding protein provided herein, such as a heavy chain and a light chain of a} _{broadly neutralizing anti-HIV envelope spike complex antibody and a CD4 domain. The heavy chain} and the light chain of the antibody may be delivered by the same or separate nucleic acids. The _{nucleic acids may be DNA or RNA. The nucleic acids encoding the multimeric antigen binding protein} may be delivered to the subject naked (i.e. without an encapsulating particle) or packaged (i.e. encapsulated in liposomes or polymer-based vehicles). The nucleic acids encoding the multimeric antigen binding protein may be delivered without a delivery vehicle (i.e., “naked”) or delivered with a viral or non-viral delivery vehicle (i.e., as a viral vector, adsorbed to or encapsulated in liposomes or polymer-based vehicles, and the like). The nucleic acid may include elements such as a poly-A tail, a 5’ and/or 3’ untranslated region (UTR). The nucleic acids may be mRNA. The mRNA may include a cap structure. The mRNA may be self-replicating RNA. T_{he nucleic acid coding for the multimeric antigen binding proteins may be modified or} _{unmodified. The nucleic acids coding for the multimeric antigen binding proteins may comprise at} least one chemical modification. Nucleic acids (e.g., mRNAs) can be modified to enhance stability by including one or more chemical modifications. Such chemical modifications include, but are not limited to, a modified nucleotide, a modified sugar backbone, and the like. Also provided herein is a _{method of producing a multimeric antigen binding protein in a cell, tissue, or organism comprising} contacting said cell, tissue, or organism with a composition comprising an isolated nucleic acid _{comprising at least one chemical modification and which encodes the multimeric antigen binding} _{protein. Also provided herein is a method of producing a multimeric antigen binding protein in a cell,} tissue or organism comprising contacting said cell, tissue or organism with a composition comprising a polynucleotide comprising at least one chemical modification and which encodes a multimeric _{antigen binding protein. Also provided herein is a method of producing a multimeric antigen binding} protein in a cell, in vitro or in vivo, comprising contacting said cell with a composition comprising a nucleic acid comprising at least one chemical modification and which encodes a multimeric antigen binding protein. “Neutralizes” as used throughout the present specification means that the biological activity of HIV is reduced in the presence of an antigen binding protein as described herein in _{comparison to the biological activity of HIV in the absence of the antigen binding protein, in vitro or} in vivo. For example, a neutralizing antigen binding protein of the invention may inhibit HIV entry into a target cell and reduce viral load in a patient infected with HIV. “Percent identity” or “% identity” between a query amino acid sequence and a subject amino acid sequence is the “Identities” value, expressed as a percentage, that is calculated using a suitable algorithm (e.g., BLASTP, FASTA, Needleman-Wunsch, Smith-Waterman, LALIGN, or GenePAST/KERR) or software (e.g., DNASTAR Lasergene, GenomeQuest, EMBOSS needle or EMBOSS infoalign), over the entire length of the query sequence after a pair-wise global sequence alignment has been performed using a suitable algorithm (e.g., Needleman-Wunsch or GenePAST/KERR) or software (e.g. DNASTAR Lasergene or GenePAST/KERR). Importantly, a query amino acid sequence may be described by an amino acid sequence disclosed herein, in particular in one or more of the claims. The query sequence may be 100% identical to the subject sequence, or it may include up to a certain integer number of amino acid alterations as compared to the subject sequence such that the % identity is less than 100%. For example, the query sequence is at least 50, 60, 70, 75, 80, 85, 90, 95, 96, 97, 98, or 99% identical to the subject sequence. In the case of amino acid sequences such alterations include at least one amino acid residue deletion, substitution (including conservative and non-conservative substitutions), or insertion, wherein said alterations may occur at the amino- or carboxy-terminal positions of the query sequence or anywhere between those terminal positions, interspersed either individually among the amino acid residues in the query sequence or in one or more contiguous groups within the query sequence. For antibody sequences, the % identity may be determined across the entire length of the query sequence, including the CDRs. Alternatively, the % identity may exclude one or more or all of the CDRs, for example all of the CDRs are 100% identical to the subject sequence and the % identity variation is in the remaining portion of the query sequence, e.g., the framework sequence, so that the CDR sequences are fixed and intact. “Protein scaffold” as used herein includes, but is not limited to, an immunoglobulin (Ig) scaffold, for example an IgG scaffold, which may be a four chain or two chain antibody, or which may comprise only the Fc region of an antibody, or which may comprise one or more constant regions from an antibody, which constant regions may be of human origin. The protein scaffold may be an Ig scaffold, for example an IgG, or IgA scaffold. The IgG scaffold may comprise some or all the domains of an intact antibody (i.e., CH1, CH2, CH3, VH, VL). The antigen binding protein may comprise an IgG scaffold selected from IgG1, IgG2, IgG3, IgG4 or IgG4PE. For example, the scaffold may be IgG1. The scaffold may consist of, or comprise, the Fc region of an antibody, or is a part thereof. The protein scaffold may be a non-Ig scaffold. The protein scaffold may be a derivative of a _{scaffold selected from one or more of CTLA-4, lipocalin, Protein A derived molecules such as Z-} domain of Protein A (Affibody, SpA), A-domain (Avimer/Maxibody); heat shock proteins such as GroEl and GroES; transferrin (trans-body); ankyrin repeat protein (DARPin); peptide aptamer; Ctype lectin domain (Tetranectin); human γ-crystallin and human ubiquitin (affilins); PDZ domains; scorpion toxin kunitz type domains of human protease inhibitors; and fibronectin/adnectin; which _{has been subjected to protein engineering in order to obtain binding to an antigen, such as gp120 or} gp41. “Single variable domain” refers to a folded polypeptide domain comprising sequences characteristic of antibody variable domains. It therefore includes complete antibody variable domains such as VH, VHH and VL and modified antibody variable domains, for example, in which one or more loops have been replaced by sequences that are not characteristic of antibody variable _{domains, or antibody variable domains that have been truncated or comprise N- or C-terminal} extensions, as well as folded fragments of variable domains that retain at least the binding activity and specificity of the full-length domain. A single variable domain as defined herein is capable of binding an antigen or epitope independently of a different variable region or domain. A “domain antibody” or “DAB” may be considered the same as a human “single variable domain”. A single variable domain may be a human single variable domain, but also includes single variable domains from other species such as rodent (for example, as disclosed in WO 00/29004), nurse shark and Camelid VHHs Camelid VHHs are immunoglobulin single variable domain polypeptides that are derived from species including camel, llama, alpaca, dromedary, and guanaco, which produce heavy _{chain only antibodies naturally devoid of light chains. Such VHH domains may be humanised} 17according to standard techniques available in the art, and such domains are considered to be “single variable domains”. “Stabilizing mutation” refers to a change of an amino acid residue in a polypeptide sequence that increases the thermal thermostability of said polypeptide. Increased thermostability may be reflected in a melting temperature (Tm) increase of, for example, between 1 and 50 ºC. CD4 domains with stabilizing mutations include SEQ ID NOs:5-21. A “variant sequence” substantially retains the biological characteristics of the unmodified protein. In the case of an antibody sequence disclosed herein, the VH or VL (or HC or LC) sequence may be a variant sequence with up to 10 amino acid substitutions, additions or deletions. For _{example, the variant sequence may have up to 9, 8, 7, 6, 5, 4, 3, 2 or 1 amino acid substitution(s),} addition(s) or deletion(s). The sequence variation may exclude one or more or all of the CDRs, for example the CDRs are the same as the VH or VL (or HC or LC) sequence and the variation is in the remaining portion of the VH or VL (or HC or LC) sequence, so that the CDR sequences are fixed and intact. “V3 loop region”, “V3/glycan” or “V3” as used herein refers to the third variable region (V3) of HIV gp120. Comparison of predicted amino acid sequences from several different isolates has shown that sequence heterogeneity of gp120 is clustered in five variable regions (designated V1, V2, V3, V4, and V5.) The V3 region contains post-translational modifications, such as glycosylation, and is essential for viral infectivity. The V3 region, although only 35 amino acids long, exhibits considerable sequence variability. Additionally, variability in potential N-linked glycosylation sites allow for further variability in the variable regions of gp120. Together, the V3 region and the N- linked glycosylation sites within and adjacent to the region are understood to comprise the “V3 loop region,” “V3/glycan” or V3” as used herein. For example, one site of glycosylation (e.g., 30 oligomannose such as Man-5 to Man-9) is centered on amino acid residue N332 of gp120. Other _{sites of potential N-linked glycosylation within and adjacent to the V3 loop region include K295,} N301, N386, N392 of gp120. The V3 loop is generally considered to be in the region between cysteine residues C296 and C331 of gp120, while some N-linked glycosylation sites are located directly adjacent to the V3 loop. The V3 loop comprises a highly conserved tetrapeptide sequence, GPGR (residues 312 to 315) (Ivanhoff et al., Virology, 187(2) 1992). HIV-1 cellular entry depends on the interaction of the V3 loop region with an HIV co-receptor, commonly CCR5 or CXCR4. The V3 loop comprises: (i) the base (residues 296–299), (ii) the stem (residues 300–303 and 321–326), and (iii) the crown (residues 304–320) (Friedrich et al., Nature Communications 12, 6705 (2021)). A consensus sequence of the V3 region of gp120 (Milich et al., J Virol., 67(9):5623-5634 (1993)) is provided below: CTRPNNNTRKSIHIGPGRAFYTTGEIIGDIRQAHC (SEQ ID NO: 54) It is understood that the consensus sequence describes the highest frequency of residues emerging on each position of this region across multiple subtypes, but that the V3 loop region of a particular strain may exhibit sequence variability. A “V3-bNAb” or “anti-V3 bNAb” is a bNAb that binds within the V3 loop region. A V3- bNAb may also be referred to herein as an anti-V3 antibody. A V3-bNAb may bind the N332 glycan in the V3 loop region and/or other N-linked glycosylation sites within and adjacent to the V3 loop region. “V1/V2 Apex”, “V1/V2 loop”, “V2 Apex” or “Apex” as used herein refers to an important region of gp120 known in the art that contains the receptor binding site which interacts _{with host cell receptors like CD4 and coreceptors like CCR5 or CXCR4. The Apex region plays a} crucial role in the initial stages of HIV infection by mediating the attachment of the virus to target _{cells and facilitating viral entry. A consensus sequence of the Apex region of gp120 is provided} below: C_{TDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSC (SEQ} ID NO: 58) It is understood that the consensus sequence describes the highest frequency of residues emerging on each position of this region across multiple subtypes, but that this region of a particular strain may exhibit sequence variability. A_{n “Apex-bNAb” or “anti-Apex bNAb” is a bNAb that binds within the V1/V2 Apex region.} _{An Apex-bNAb may also be referred to herein as an anti-Apex antibody. An Apex bNAb may bind at} _{least one complex N-glycan.} “gp120-gp41 interface” or “interface” as used herein refers to a conformational non- _{continuous epitope located across the complex of gp120 and gp41 known in the art. A consensus,} _{non-continuous sequence of the interface region of gp120-gp41 is provided below:} _{SDAKAYDTVPTDPNPQTKAKRRVVNASWSNKSLEQIWN (SEQ ID NO: 59)} It is understood that the consensus sequence describes the highest frequency of residues emerging on each position of this region across multiple subtypes, but that this region of a particular strain may exhibit sequence variability. A_{n “Interface-bNAb” or “anti-interface bNAb” is a bNAb that binds within the gp120-} _{gp41 interface region. Given that the interface epitope is a non-continuous epitope across a complex} of gp120 and gp41, it is possible that an interface-bNAb may bind gp120, gp41 or across both _{gp120 and gp41. An interface-bNAb may also be referred to herein as an anti-interface antibody. An} _{Interface bNAb may bind at least one complex N-glycan.} _{An “N-glycan” or “N-linked glycan” is an oligosaccharide (also known as a glycan)} attached to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein) via a _{process called N-glycosylation. N-glycans can be further modified by enzymes in the Golgi including} _{glycosyltransferases and glycosidases which gives rise to the three main types of N-glycans which} are known by the skilled person: high mannose N-glycans, complex N-glycans and hybrid N-glycans. _{STATEMENT OF THE INVENTION} _{A multimeric antigen binding protein of the invention binds to the Human Immunodeficiency} Virus (HIV) envelope spike complex. Multimeric antigen binding proteins of the invention that bind to _{the V1/V2 apex region of gp120 or the gp120-gp41 interface region of gp120 and gp41 as well as} having a CD4 domain that binds to the CD4bs of gp120 have been shown to effectively neutralize HIV and exhibit significantly better anti-viral activity than monospecific molecules that only bind to _{the V1/V2 apex region of gp120, the gp120-gp41 interface region of gp120 and gp41, or the CD4bs} of gp120, and mixtures of these monospecific molecules. Without being bound by any particular theory, we postulate that the bispecific molecules of the invention bind the two different epitopes in the same or neighboring HIV envelope protein trimers at the same time, such that the bispecific molecules achieve stronger binding (increased _{avidity) to the HIV envelope proteins. This may be as a result of the high local concentration of the} bispecific molecules’ binding sites (paratopes) being “pre-positioned” around their target binding sites (epitopes) on the HIV envelope compared to their monospecific counterparts, which in turn _{leads to stronger anti-viral activity. In addition, we believe that CD4-induced conformational change} _{of the envelope spike complex (also referred to as gp160) exposes new epitopes for the bNAb} portion of the binding proteins, which overcomes the low susceptibility of insensitive envelopes. This is particularly surprising in view of literature evidence. For antibodies that bind to a CD4-induced epitope, such as 17b which binds to the co- _{receptor binding site, or 7B2 that binds to the heptad repeat of gp41, soluble CD4 (sCD4) has been} shown to agonize their activity to neutralize HIV (PMID 30650070) or ability to deliver cytotoxic immunoconjugates into infected cells (PMID 34358190). Therefore, as a logical step, fusion of sCD4 to these antibodies have been made and shown further enhancement of activities (PMID 12584309, 20158904 and 34358190). But sCD4 also antagonizes bNAbs (broadly neutralizing antibodies) such as PGT128 from the V3/glycan family that binds to the high mannose patch at the V3 loop, the V1/V2 apex family which only binds to a closed trimer, and the interface family that binds the gp41/gp120 interface. Surprisingly, as disclosed herein, when CD4 is fused to representative members of these families, we observed strong anti-viral synergy: the fused CD4-bNAb bispecifics neutralized HIV with stronger potency and broader spectrum than the mixture of CD4 with these bNAbs as well as the CD4 and individual bNAbs alone. A_{ccordingly, in one aspect of the invention, there is provided a multimeric anti-HIV envelope} spike complex -binding protein comprising: i_{. a means for binding to the V1/V2 loop of a gp120 protein or the gp120-gp41} interface of a gp120 and a gp41 protein and neutralizing at least 2 different strains of HIV-1; and i_{i. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached} _{directly or by a linker to the N-terminus or C-terminus of said means for binding.} In some embodiments, the means for binding to the V1/V2 loop of a gp120 protein or the gp120- _{gp41 interface of a gp120 and a gp41 protein and neutralizing at least 2 different strains of HIV-1 is} _{a broadly neutralizing antibody or fragment thereof. For example, the means for binding to the} _{V1/V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41 protein and} _{neutralizing at least 2 different strains of HIV-1 may be any of the bispecific binding proteins} _{exemplified in Examples 6 and 7 and Figures 4-33, as well as those bispecific binding proteins with} sequences as per Tables 3 and 4. Accordingly, in one aspect of the invention there is provided a multimeric anti-HIV envelope spike complex-binding protein comprising: i_{. a broadly neutralizing anti-HIV envelope spike complex, comprising at least one} heavy chain or light chain, wherein the antibody binds to the V1/V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41 protein; and i_{i. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached} directly or by a linker to the N-terminus or C-terminus of one of the heavy chains or l_{ight chains of the broadly neutralizing antibody.} _{In some embodiments, wherein the antibody binds to the V1/V2 loop of a gp120 protein. In} _{other words the antibody is an anti-apex broad neutralizing antibody. In some embodiments the} _{antibody binds the gp120-gp41 interface of a gp120 and a gp41 protein. In other words, the} antibody is an anti-interface broad neutralizing antibody. I_{n some embodiments, the broadly neutralizing antibody binds to at least one complex N-} _{glycan at the V1/V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41} _{protein. In some embodiments, the broadly neutralizing antibody binds to at least one complex N-} _{glycan at the V1/V2 loop of a gp120. In some embodiments, the broadly neutralizing antibody binds} _{to at least one complex N-glycan at the gp120-gp41 interface of a gp120 and a gp41 protein.} _{Experiments disclosed herein demonstrate a role for complex N-glycan binding in the} _{synergistic effect seen in antigen binding proteins of the invention. In particular, when a compound} _{called kifunensine, which prevents the modification of N-glycans into complex N-glycans, is added to} a PSV assay, the synergistic effect of the bispecific proteins tested is lost. Without being bound by _{theory, it is postulated that a broadly neutralizing antibody (or fragment thereof) alone has a certain} affinity to at least one N-glycan as well as its “main” affinity to the target epitope (having a certain _{amino acid binding sequence) within the HIV envelope spike protein complex. Thus, if the target} _{epitope is not present at 100% identity, the HIV envelope spike protein complex is resistant to} binding because the affinity for the N-glycan only is too low. However, in multimeric antigen binding _{proteins of the invention, the addition of a CD4 domain allows for anchoring the antibody to the HIV} _{envelope spike protein complex. As a result, the antibody is located very closely to a small number} of N-glycans which the antibody can bind to, creating the observed synergy (e.g. greatly improved IC50 compared to the antibody alone, the CD4 domain alone or a mixture of the two components). As such, N-glycan binding also facilitates improved binding of the antibody portion of the multimeric protein to a target sequence, which allows, a greater breadth of binding across different HIV _{envelopes having sequence variation at a particular epitope and further allows for some variation in} _{the sequence of the broadly neutralizing antibody whilst retaining binding ability.} One skilled in the art can ascertain whether an antigen binding protein is binding via _{complex N-glycan binding by methods known in the art. For example, one may analyse the x-ray} _{crystal structure to visualize binding of an antigen binding protein to N-glycans. In another example,} _{one may de-glycosylate HIV virus and/or the HIV envelope spike protein complex using Endo F} _{treatment, which uses multiple enzymes that removes N-linked glycans, wherein disruption of} _{binding after such treatment suggests N-glycan binding by the antigen binding protein. In another} _{example, the kifunensine experiments disclosed herein may be used in a similar way.} In one aspect of the invention there is provided a multimeric anti-HIV envelope spike complex -binding protein comprising: i_{. a broadly neutralizing anti-HIV envelope spike complex antibody , comprising at least} one heavy chain or light chain, wherein the antibody binds to at least one complex N-glycan on a gp120 or a gp41 protein; and _{ii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached} directly or by a linker to the N-terminus or C-terminus of one of the heavy chains or l_{ight chains of the broadly neutralizing antibody.} In some embodiments, the antibody binds to the V1/V2 loop of a gp120 protein. In some embodiments the antibody binds the gp120-gp41 interface of a gp120 and a gp41 protein. A_{gain, in some embodiments, the broadly neutralizing antibody binds to at least one} complex N-glycan at the V1/V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and _{a gp41 protein. In some embodiments, the broadly neutralizing antibody binds to at least one} _{complex N-glycan at the V1/V2 loop of a gp120. In some embodiments, the broadly neutralizing} antibody binds to at least one complex N-glycan at the gp120-gp41 interface of a gp120 and a gp41 protein. In some embodiments, the binding protein is a bispecific binding protein. Such bispecific binding proteins may be any of the bispecific binding proteins exemplified in Examples 6 and 7 and Figures 4-33, as well as those bispecific binding proteins with sequences as per Tables 3 and 4. The following sections will describe particular features of the multimeric binding proteins of the invention including bispecific binding proteins. CD4 Domains CD4 domains of the invention include SEQ ID NOs: 1-21. In an embodiment of the invention, the CD4 domain is a CD4 D1 domain. In an embodiment, the CD4 domain is a human CD4 domain. CD4 D1 domains include human wild-type D1 (SEQ ID NO:3), mD1.22 (SEQ ID NO:4) also known as D1m, and further variants of mD1.22 (SEQ ID NOs: 5-21). In some embodiments, the CD4 domain has a sequence that is at least 90%, 95%, 97%, 98% or 99% identical to SEQ ID NO: 3 or 4. In an embodiment of the invention, the CD4 domain is a CD4 D1D2 domain. In an embodiment, the CD4 domain is a human CD4 D1D2 domain. CD4 D1D2 domains include human wild-type D1D2 (SEQ ID NO:1) and mD1.22-D2 (SEQ ID NO:2). In some embodiments, the CD4 domain has a sequence that is at least 90%, 95%, 97%, 98% or 99% identical to SEQ ID NO:1 or 2. I_{n an aspect of the invention, a stabilized CD4 domain is provided. In an embodiment of the} invention, a stabilized CD4 D1 domain is provided. In an embodiment, the CD4 domain is thermally stable, i.e., thermostable. In an embodiment, the CD4 domain is a thermostable CD4 D1 domain. In an embodiment of the invention, the CD4 domain comprises one or more stabilizing _{mutations compared to the wild type sequence. In an embodiment, the stabilizing mutations are in} the CD4 D1 domain. In an embodiment, the CD4 D1 domain comprises at least one mutation at position 5, 23, 55, 79, 96 and/or 98 of SEQ ID NO: 1 or 3. In an embodiment, the CD4 D1 domain comprises one or more mutations at positions 8, 11, 13, 21, 25, 27, 38, 52, 58, 61, 65, 70, 72, 87, 91 and or 99 of SEQ ID NO: 1 or 3. In an embodiment, the CD4 D1 domain comprises a mutation at position 8 or _{SEQ ID NO: 1 or 3. In an embodiment, the CD4 D1 domain comprises a mutation at positions 11} and 72 of SEQ ID NO: 1 or 3. In an embodiment, the CD4 D1 domain comprises mutation at positions 8 and 99. In an embodiment, the CD4 D1 domain comprises at least one mutation selected from: L5Y, S23N, A55V, I79P, L96V and/or F98V mutations. In an embodiment, the CD4 D1 domain comprises one or more mutations selected from: K8C, K8I, K8V, T11C, E13C, K21C, Q25E, H27C, H27D, G38C, _{N52W, R58N, R58T, R58V, L61M, G65C, I70C, K72C, E87G, E91H, E91Q, and/or G99C. In an} _{embodiment, the CD4 D1 domain comprises a K8I mutation. In an embodiment, the CD4 D1 domain} _{comprises a K8V mutation. In an embodiment, the CD4 D1 domain comprises T1C and K72C} _{mutations. In an embodiment, the CD4 D1 domain comprises K8C and G99C mutations. In all of} these embodiments, these mutations may be compared to a wild type sequence as per SEQ ID NO: 1 or 3. CD4 domains of the invention comprising novel and inventive stabilizing mutations include SEQ ID NOs:5-21. In some embodiments, the CD4 domain is a SEQ ID NOs: 5-15. In some embodiments, the CD4 domain has a sequence that is at least 90%, 95%, 97%, 98% or 99% _{identical to SEQ ID NO: 5-21. In some embodiments, the CD4 domain has a sequence that is at} least 90%, 95%, 97%, 98% or 99% identical to SEQ ID NO: 5-15. Increased thermostability may be reflected in a melting temperature (Tm) increase of, for example, between 1 and 50 ºC; in particular between 1 and 30 ºC; in particular between 1 and 25 ºC, in particular between 1 and 21 ºC, more particularly between 5 and 21 ºC. The Tm increase is determined by measuring the Tm of the CD4 domain(s) comprising one or more stabilizing mutations and subtracting the Tm of the corresponding CD4 domain(s) without said mutation(s). For example, measuring the Tm of a stabilized CD4 D1 domain and subtracting the Tm of the wild-type CD4 D1 domain. In an embodiment, the Tm increase is about 8 ºC. In an embodiment, the Tm increase is about 9 ºC. In an embodiment, the Tm increase is about 12 ºC. In an embodiment, the Tm increase is about 21 ºC. In an embodiment, the Tm of the CD4 domain is above 70 ºC. In an embodiment, the Tm of the CD4 domain is between 70 ºC and 95 ºC. In an embodiment, the Tm of the CD4 domain is between 75 ºC and 95 ºC. In an embodiment, the Tm of the CD4 domain is between 75 ºC and 91 ºC. In an embodiment, the Tm of the CD4 domain is about 76 ºC, about 77 ºC, about 78 ºC, about 79 ºC, about 80 ºC, about 81 ºC, about 82 ºC, about 83 ºC, about 84 ºC, about 85 ºC, about 86 ºC, about 87 ºC, about 88 ºC, about 89 ºC, or about 90 ºC. In an embodiment, the Tm of the CD4 domain is about 90 ºC. In an embodiment, the Tm of the CD4 domain is about 89 ºC. Tm may be determined by routine methods known in the art or as set out in the Examples. In an embodiment, Tm is determined using the Prometheus System (NanoTemper, München Germany). In some embodiments of the invention, a CD4 domain as described above may be attached _{directly to a broadly neutralizing antibody, by “directly” is meant that a CD4 domain is covalently} _{bonded to a broadly neutralizing antibody without the use of an additional linking chemical or} peptide sequence. In other embodiments, the CD4 domain as described above may be attached by a _{linker (for example a peptide linker such as those shown in SEQ ID: 30-35).} _{Anti-HIV envelope spike complex broadly neutralizing antibodies} _{An antigen binding protein of the invention may comprise a broadly neutralizing antibody} having heavy chain CDRs (CDRH1, CDRH2, and CDRH3) as set out in any row of Table 3. An antigen _{binding protein of the invention may comprise a broadly neutralizing antibody having light chain} CDRs (CDRL1, CDRL2, and CDRL3) as set out in any row of Table 3. An antigen binding protein of _{the invention may comprise a broadly neutralizing antibody having a set of six CDRs (CDRH1,} CDRH2, CDRH3, CDRL1, CDRL2 and CDRL3) as set out in any row of Table 3. A_{n antigen binding protein of the invention may comprise a broadly neutralizing antibody} having a VH domain as set out in Table 4. An antigen binding protein of the invention may comprise _{a broadly neutralizing antibody having a VL domain as set out in Table 4. An antigen binding} _{protein of the invention may comprise a broadly neutralizing antibody having a pair of variable} domains (a VH and a VL) as set out in any row of Table 4. _{Table 3: SEQ ID NOs for the complementarity determining regions (CDRs) of broadly neutralizing} antibodies C_{DRH1 CDRH2 CDRH3 CDRL1 CDRL2 CDRL3} _{Interface-bNAb17 90 91 92 93 94 95} e_ca^f _{Interface-bNAb18 101 102 103 104 105 106} _r e_t n _{Interface-bNAb19 112 113 114 115 116 117} _I _{Interface-bNAb20 123 124 125 126 127 128} _{Interface-bNAb21 134 135 136 137 138 139} _{Interface-bNAb22 145 146 147 148 149 150} _{Interface-bNAb23 156 157 158 159 160 161} _{Interface-bNAb24 167 168 169 170 171 172} _{Interface-bNAb25 178 179 180 181 182 183} _{Interface-bNAb26 189 190 191 192 193 194} _{Interface-bNAb27 200 201 202 203 204 205} _{Interface-bNAb29 211 212 213 214 215 216} _{Interface-bNAb30 222 223 224 225 226 227} _{Interface-bNAb31 233 234 235 236 237 238} _{Apex-bNAb1 244 245 246 247 248 249} _{Apex-bNAb2 255 256 257 258 259 260} _{Apex-bNAb3 266 267 268 269 270 271} _{Apex-bNAb4 277 278 279 280 281 282} _{Apex-bNAb5 288 289 290 291 292 293} _{Apex-bNAb6 299 300 301 302 303 304} _{Apex-bNAb7 310 311 312 313 314 315} x _{Apex-bNAb8 321 322 323 324 325 326} ep A _{Apex-bNAb9 332 333 334 335 336 337} _{Apex-bNAb10 343 344 345 346 347 348} _{Apex-bNAb11 354 355 356 357 358 359} _{Apex-bNAb12 365 366 367 368 369 370} _{Apex-bNAb13 376 377 378 379 380 381} _{Apex-bNAb14 387 388 389 390 391 392} _{Apex-bNAb15 398 399 400 401 402 403} _{Apex-bNAb16 409 410 411 412 413 414} _{Table 4: SEQ ID NOs for the variable heavy regions (VH) and variable light regions (VL)} variable domain pairs), and the full heavy chains (with and without LS mutations) chains (LC) broadly neutralizing antibodies. V_{ariable domain pair Full chain pair} _{VH VL Full HC} Full HC Full LC (no LS) (LS) I_{nterface-bNAb17 96 97 98 99 100} _{Interface-bNAb18 107 108 109 110 111} _{Interface-bNAb19 118 119 120 121 122} _{Interface-bNAb20 129 130 131 132 133} _{Interface-bNAb21 140 141 142 143 144} _{Interface-bNAb22 151 152 153 154 155} ^e _ca^f _{Interface-bNAb23 162 163 164 165 166} _r ^e _t ⁿ _{Interface-bNAb24 173 174 175 176 177} _I _{Interface-bNAb25 184 185 186 187 188} _{Interface-bNAb26 195 196 197 198 199} _{Interface-bNAb27 206 207 208 209 210} _{Interface-bNAb29 217 218 219 220 221} _{Interface-bNAb30 228 229 230 231 232} _{Interface-bNAb31 239 240 241 242 243} _{Apex-bNAb1 250 251 252 253 254} _{Apex-bNAb2 261 262 263 264 265} _{Apex-bNAb3 272 273 274 275 276} _{Apex-bNAb4 283 284 285 286 287} _{Apex-bNAb5 294 295 296 297 298} _{Apex-bNAb6 305 306 307 308 309} _{Apex-bNAb7 316 317 318 319 320}x _{Apex-bNAb8 327 328 329 330 331}ep A _{Apex-bNAb9 338 339 340 341 342} _{Apex-bNAb10 349 350 351 352 353} _{Apex-bNAb11 360 361 362 363 364} _{Apex-bNAb12 371 372 373 374 375} _{Apex-bNAb13 382 383 384 385 386} _{Apex-bNAb14 393 394 395 396 397} _{Apex-bNAb15 404 405 406 407 408} _{Apex-bNAb16 415 416 417 418 419} Anti-interface bNAbs I_{n particular, an antigen binding protein of the invention may comprise an anti-interface} _{bNAb or a fragment thereof (i.e. a broadly neutralizing antibody or fragment binds to the gp120-} gp41 interface of a gp120 and a gp41 protein). A fragment may include Fab, F(ab’)2, Fv, disulphide linked Fv, single chain Fv (scFv), disulphide-linked scFv, diabodies, TANDABS, etc. and modified _{versions of any of the foregoing. For example, scFv variants of anti-interface bNAbs have been} described in van Dorsten et al. 2021 (PMID: 34603312). An anti-interface bNAb or fragment thereof includes an antibody comprising a set of CDRs (CDRH1, CDRH2, CDRH3, CDRL1, CDRL2 and CDRL3) _{as set out in rows 1 to 14 of Table 3 (interface bNAbs17-31).} _{An anti-interface bNAb or fragment thereof also includes an antibody comprising a pair of} _{variable domains (a VH and VL) set out in rows 1 to 14 of Table 4 (interface bNAbs17-31).} An anti-interface bNAb may be an antibody comprising a heavy chain (HC), with or without _{M428L/N434S (EU numbering) ‘LS’ mutations, and a light chain (LC) as set out in rows 1 to 14 of} _{Table 4 (interface bNAbs17-31). In an embodiment, the HC comprises LS.} In an embodiment, the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 90, a CDRH2 of SEQ ID NO: 91, a CDRH3 of SEQ ID NO: 92, a CDRL1 of SEQ ID NO: 93, a _{CDRL2 of SEQ ID NO: 94 and a CDRL3 of SEQ ID NO: 95. In an embodiment, the anti-interface} bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 101, a CDRH2 of SEQ ID NO: 102, a _{CDRH3 of SEQ ID NO: 103, a CDRL1 of SEQ ID NO: 104, a CDRL2 of SEQ ID NO: 105 and a CDRL3} of SEQ ID NO: 106. In an embodiment, the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 112, a CDRH2 of SEQ ID NO: 113, a CDRH3 of SEQ ID NO: 114, a CDRL1 of _{SEQ ID NO: 115, a CDRL2 of SEQ ID NO: 116 and a CDRL3 of SEQ ID NO: 117. In an embodiment,} the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 123, a CDRH2 of SEQ ID NO: 124, a CDRH3 of SEQ ID NO: 125, a CDRL1 of SEQ ID NO: 126, a CDRL2 of SEQ ID _{NO: 127 and a CDRL3 of SEQ ID NO: 128. In an embodiment, the anti-interface bNAb or fragment} thereof comprises a CDRH1 of SEQ ID NO: 134, a CDRH2 of SEQ ID NO: 135, a CDRH3 of SEQ ID _{NO: 136, a CDRL1 of SEQ ID NO: 137, a CDRL2 of SEQ ID NO: 138 and a CDRL3 of SEQ ID NO:} 139. In an embodiment, the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 145, a CDRH2 of SEQ ID NO: 146, a CDRH3 of SEQ ID NO: 147, a CDRL1 of SEQ ID NO: 148, a _{CDRL2 of SEQ ID NO: 149 and a CDRL3 of SEQ ID NO: 150. In an embodiment, the anti-interface} bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 156, a CDRH2 of SEQ ID NO: 157, a _{CDRH3 of SEQ ID NO: 158, a CDRL1 of SEQ ID NO: 159, a CDRL2 of SEQ ID NO: 160 and a CDRL3} of SEQ ID NO: 161. In an embodiment, the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 167, a CDRH2 of SEQ ID NO: 168, a CDRH3 of SEQ ID NO: 169, a CDRL1 of _{SEQ ID NO: 170, a CDRL2 of SEQ ID NO: 171 and a CDRL3 of SEQ ID NO: 172. In an embodiment,} the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 178, a CDRH2 of SEQ ID NO: 179, a CDRH3 of SEQ ID NO: 180, a CDRL1 of SEQ ID NO: 181, a CDRL2 of SEQ ID _{NO: 182 and a CDRL3 of SEQ ID NO: 183. In an embodiment, the anti-interface bNAb or fragment} thereof comprises a CDRH1 of SEQ ID NO: 189, a CDRH2 of SEQ ID NO: 190, a CDRH3 of SEQ ID _{NO: 191, a CDRL1 of SEQ ID NO: 192, a CDRL2 of SEQ ID NO: 193 and a CDRL3 of SEQ ID NO:} 194. In an embodiment, the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 200, a CDRH2 of SEQ ID NO: 201, a CDRH3 of SEQ ID NO: 202, a CDRL1 of SEQ ID NO: 203, a _{CDRL2 of SEQ ID NO: 204 and a CDRL3 of SEQ ID NO: 205. In an embodiment, the anti-interface} bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 211, a CDRH2 of SEQ ID NO: 212, a _{CDRH3 of SEQ ID NO: 213, a CDRL1 of SEQ ID NO: 214, a CDRL2 of SEQ ID NO: 215 and a CDRL3} of SEQ ID NO: 216. In an embodiment, the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 222, a CDRH2 of SEQ ID NO: 223, a CDRH3 of SEQ ID NO: 224, a CDRL1 of _{SEQ ID NO: 225, a CDRL2 of SEQ ID NO: 226 and a CDRL3 of SEQ ID NO: 227. In an embodiment,} the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 233, a CDRH2 of SEQ ID NO: 234, a CDRH3 of SEQ ID NO: 235, a CDRL1 of SEQ ID NO: 236, a CDRL2 of SEQ ID _{NO: 237 and a CDRL3 of SEQ ID NO: 238.} In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain having at least 95% sequence identity to SEQ ID NO: 96 and a VL domain having at least 95% _{sequence identity to SEQ ID NO: 97, optionally wherein the anti-interface bNAb or fragment thereof} comprises a CDRH1 of SEQ ID NO: 90, a CDRH2 of SEQ ID NO: 91, a CDRH3 of SEQ ID NO: 92, a _{CDRL1 of SEQ ID NO: 93, a CDRL2 of SEQ ID NO: 94 and a CDRL3 of SEQ ID NO: 95.} _{In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain} having at least 95% sequence identity to SEQ ID NO: 107 and a VL domain having at least 95% sequence identity to SEQ ID NO: 108, optionally wherein the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 101, a CDRH2 of SEQ ID NO: 102, a CDRH3 of SEQ ID _{NO: 103, a CDRL1 of SEQ ID NO: 104, a CDRL2 of SEQ ID NO: 105 and a CDRL3 of SEQ ID NO:} 106. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain having at least 95% sequence identity to SEQ ID NO: 118 and a VL domain having at least 95% sequence identity to SEQ ID NO: 119, optionally wherein the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 112, a CDRH2 of SEQ ID NO: 113, a CDRH3 of SEQ ID _{NO: 114, a CDRL1 of SEQ ID NO: 115, a CDRL2 of SEQ ID NO: 116 and a CDRL3 of SEQ ID NO:} 117. I_{n an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain} _{having at least 95% sequence identity to SEQ ID NO: 129 and a VL domain having at least 95%} _{sequence identity to SEQ ID NO: 130, optionally wherein the anti-interface bNAb or fragment} thereof comprises a CDRH1 of SEQ ID NO: 123, a CDRH2 of SEQ ID NO: 124, a CDRH3 of SEQ ID _{NO: 125, a CDRL1 of SEQ ID NO: 126, a CDRL2 of SEQ ID NO: 127 and a CDRL3 of SEQ ID NO:} 128. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain having at least 95% sequence identity to SEQ ID NO: 140 and a VL domain having at least 95% _{sequence identity to SEQ ID NO: 141, optionally wherein the anti-interface bNAb or fragment} thereof comprises a CDRH1 of SEQ ID NO: 134, a CDRH2 of SEQ ID NO: 135, a CDRH3 of SEQ ID _{NO: 136, a CDRL1 of SEQ ID NO: 137, a CDRL2 of SEQ ID NO: 138 and a CDRL3 of SEQ ID NO:} 139. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain _{having at least 95% sequence identity to SEQ ID NO: 151 and a VL domain having at least 95%} _{sequence identity to SEQ ID NO: 152, optionally wherein the anti-interface bNAb or fragment} thereof comprises a CDRH1 of SEQ ID NO: 145, a CDRH2 of SEQ ID NO: 146, a CDRH3 of SEQ ID _{NO: 147, a CDRL1 of SEQ ID NO: 148, a CDRL2 of SEQ ID NO: 149 and a CDRL3 of SEQ ID NO:} 150. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain _{having at least 95% sequence identity to SEQ ID NO: 162 and a VL domain having at least 95%} _{sequence identity to SEQ ID NO: 163, optionally wherein the anti-interface bNAb or fragment} thereof comprises a CDRH1 of SEQ ID NO: 156, a CDRH2 of SEQ ID NO: 157, a CDRH3 of SEQ ID _{NO: 158, a CDRL1 of SEQ ID NO: 159, a CDRL2 of SEQ ID NO: 160 and a CDRL3 of SEQ ID NO:} 161. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain _{having at least 95% sequence identity to SEQ ID NO: 173 and a VL domain having at least 95%} sequence identity to SEQ ID NO: 174, optionally wherein the anti-interface bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 167, a CDRH2 of SEQ ID NO: 168, a CDRH3 of SEQ ID _{NO: 169, a CDRL1 of SEQ ID NO: 170, a CDRL2 of SEQ ID NO: 171 and a CDRL3 of SEQ ID NO:} 172. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain having at least 95% sequence identity to SEQ ID NO: 184 and a VL domain having at least 95% _{sequence identity to SEQ ID NO: 185, optionally wherein the anti-interface bNAb or fragment} thereof comprises a CDRH1 of SEQ ID NO: 178, a CDRH2 of SEQ ID NO: 179, a CDRH3 of SEQ ID _{NO: 180, a CDRL1 of SEQ ID NO: 181, a CDRL2 of SEQ ID NO: 182 and a CDRL3 of SEQ ID NO:} 183. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain _{having at least 95% sequence identity to SEQ ID NO: 195 and a VL domain having at least 95%} _{sequence identity to SEQ ID NO: 196, optionally wherein the anti-interface bNAb or fragment} thereof comprises a CDRH1 of SEQ ID NO: 189, a CDRH2 of SEQ ID NO: 190, a CDRH3 of SEQ ID _{NO: 191, a CDRL1 of SEQ ID NO: 192, a CDRL2 of SEQ ID NO: 193 and a CDRL3 of SEQ ID NO:} 194. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain _{having at least 95% sequence identity to SEQ ID NO: 206 and a VL domain having at least 95%} _{sequence identity to SEQ ID NO: 207, optionally wherein the anti-interface bNAb or fragment} thereof comprises a CDRH1 of SEQ ID NO: 200, a CDRH2 of SEQ ID NO: 201, a CDRH3 of SEQ ID _{NO: 202, a CDRL1 of SEQ ID NO: 203, a CDRL2 of SEQ ID NO: 204 and a CDRL3 of SEQ ID NO:} 205. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain _{having at least 95% sequence identity to SEQ ID NO: 217 and a VL domain having at least 95%} _{sequence identity to SEQ ID NO: 218, optionally wherein the anti-interface bNAb or fragment} thereof comprises a CDRH1 of SEQ ID NO: 211, a CDRH2 of SEQ ID NO: 212, a CDRH3 of SEQ ID _{NO: 213, a CDRL1 of SEQ ID NO: 214, a CDRL2 of SEQ ID NO: 215 and a CDRL3 of SEQ ID NO:} 216. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain _{having at least 95% sequence identity to SEQ ID NO: 228 and a VL domain having at least 95%} _{sequence identity to SEQ ID NO: 229, optionally wherein the anti-interface bNAb or fragment} thereof comprises a CDRH1 of SEQ ID NO: 222, a CDRH2 of SEQ ID NO: 223, a CDRH3 of SEQ ID _{NO: 224, a CDRL1 of SEQ ID NO: 225, a CDRL2 of SEQ ID NO: 226 and a CDRL3 of SEQ ID NO:} 227. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain _{having at least 95% sequence identity to SEQ ID NO: 239 and a VL domain having at least 95%} _{sequence identity to SEQ ID NO: 240, optionally wherein the anti-interface bNAb or fragment} thereof comprises a CDRH1 of SEQ ID NO: 233, a CDRH2 of SEQ ID NO: 234, a CDRH3 of SEQ ID _{NO: 235, a CDRL1 of SEQ ID NO: 236, a CDRL2 of SEQ ID NO: 237 and a CDRL3 of SEQ ID NO:} 238. _{In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain of} _{SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97. In an embodiment, the anti-interface bNAb or} _{fragment thereof, comprises a VH domain of SEQ ID NO: 107 and a VL domain of SEQ ID NO: 108.} _{In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain of SEQ ID} _{NO: 118 and a VL domain of SEQ ID NO: 119. In an embodiment, the anti-interface bNAb or} _{fragment thereof, comprises a VH domain of SEQ ID NO: 129 and a VL domain of SEQ ID NO: 130.} _{In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain of SEQ ID} _{NO: 140 and a VL domain of SEQ ID NO: 141. In an embodiment, the anti-interface bNAb or} _{fragment thereof, comprises a VH domain of SEQ ID NO: 151 and a VL domain of SEQ ID NO: 152.} _{In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain of SEQ ID} _{NO: 162 and a VL domain of SEQ ID NO: 163. In an embodiment, the anti-interface bNAb or} _{fragment thereof, comprises a VH domain of SEQ ID NO: 173 and a VL domain of SEQ ID NO: 174.} _{In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain of SEQ ID} _{NO: 184 and a VL domain of SEQ ID NO: 185. In an embodiment, the anti-interface bNAb or} _{fragment thereof, comprises a VH domain of SEQ ID NO: 195 and a VL domain of SEQ ID NO: 196.} _{In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain of SEQ ID} _{NO: 206 and a VL domain of SEQ ID NO: 207. In an embodiment, the anti-interface bNAb or} _{fragment thereof, comprises a VH domain of SEQ ID NO: 217 and a VL domain of SEQ ID NO: 218.} _{In an embodiment, the anti-interface bNAb or fragment thereof, comprises a VH domain of SEQ ID} _{NO: 228 and a VL domain of SEQ ID NO: 229. In an embodiment, the anti-interface bNAb or} _{fragment thereof, comprises a VH domain of SEQ ID NO: 239 and a VL domain of SEQ ID NO: 240.} _{In an embodiment, the anti-interface bNAb or fragment thereof, comprises a heavy chain} _{(HC) having at least 95% sequence identity to SEQ ID NO: 98 or 99 and a light chain (LC) having at} _{least 95% sequence identity to SEQ ID NO: 100. In an embodiment, the anti-interface bNAb or} _{fragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID NO: 109 or 110} _{and a LC having at least 95% sequence identity to SEQ ID NO: 111. In an embodiment, the anti-} _{interface bNAb or fragment thereof, comprises a HC having at least 95% sequence identity to SEQ} _{ID NO: 120 or 121 and a LC having at least 95% sequence identity to SEQ ID NO: 122. In an} _{embodiment, the anti-interface bNAb or fragment thereof, comprises a HC having at least 95%} _{sequence identity to SEQ ID NO: 131 or 132 and a LC having at least 95% sequence identity to SEQ} _{ID NO: 133. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC having} _{at least 95% sequence identity to SEQ ID NO: 142 or 143 and a LC having at least 95% sequence} _{identity to SEQ ID NO: 144. In an embodiment, the anti-interface bNAb or fragment thereof,} _{comprises a HC having at least 95% sequence identity to SEQ ID NO: 153 or 154 and a LC having at} _{least 95% sequence identity to SEQ ID NO: 155. In an embodiment, the anti-interface bNAb or} _{fragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID NO: 164 or 165} _{and a LC having at least 95% sequence identity to SEQ ID NO: 166. In an embodiment, the anti-} _{interface bNAb or fragment thereof, comprises a HC having at least 95% sequence identity to SEQ} _{ID NO: 175 or 176 and a LC having at least 95% sequence identity to SEQ ID NO: 177. In an} _{embodiment, the anti-interface bNAb or fragment thereof, comprises a HC having at least 95%} _{sequence identity to SEQ ID NO: 186 or 187 and a LC having at least 95% sequence identity to SEQ} _{ID NO: 188. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC having} _{at least 95% sequence identity to SEQ ID NO: 197 or 198 and a LC having at least 95% sequence} _{identity to SEQ ID NO: 199. In an embodiment, the anti-interface bNAb or fragment thereof,} _{comprises a HC having at least 95% sequence identity to SEQ ID NO: 208 or 209 and a LC having at} _{least 95% sequence identity to SEQ ID NO: 210. In an embodiment, the anti-interface bNAb or} _{fragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID NO: 219 or 220} _{and a LC having at least 95% sequence identity to SEQ ID NO: 221. In an embodiment, the anti-} _{interface bNAb or fragment thereof, comprises a HC having at least 95% sequence identity to SEQ} _{ID NO: 230 or 231 and a LC having at least 95% sequence identity to SEQ ID NO: 232. In an} _{embodiment, the anti-interface bNAb or fragment thereof, comprises a HC having at least 95%} _{sequence identity to SEQ ID NO: 241 or 242 and a LC having at least 95% sequence identity to SEQ} ID NO: 243. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a heavy chain _{(HC) of SEQ ID NO: 98 or 99 and a light chain (LC) of SEQ ID NO: 100. In an embodiment, the anti-} _{interface bNAb or fragment thereof, comprises a HC of SEQ ID NO: 109 or 110 and a LC of SEQ ID} NO: 111. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC of SEQ ID _{NO: 120 or 121 and a LC of SEQ ID NO: 122. In an embodiment, the anti-interface bNAb or} _{fragment thereof, comprises a HC of SEQ ID NO: 131 or 132 and a LC of SEQ ID NO: 133. In an} _{embodiment, the anti-interface bNAb or fragment thereof, comprises a HC of SEQ ID NO: 142 or} _{143 and a LC of SEQ ID NO: 144. In an embodiment, the anti-interface bNAb or fragment thereof,} _{comprises a HC of SEQ ID NO: 153 or 154 and a LC of SEQ ID NO: 155. In an embodiment, the} _{anti-interface bNAb or fragment thereof, comprises a HC of SEQ ID NO: 164 or 165 and a LC of SEQ} ID NO: 166. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC of SEQ _{ID NO: 175 or 176 and a LC of SEQ ID NO: 178. In an embodiment, the anti-interface bNAb or} _{fragment thereof, comprises a HC of SEQ ID NO: 186 or 187 and a LC of SEQ ID NO: 188. In an} _{embodiment, the anti-interface bNAb or fragment thereof, comprises a HC of SEQ ID NO: 197 or} _{198 and a LC of SEQ ID NO: 199. In an embodiment, the anti-interface bNAb or fragment thereof,} _{comprises a HC of SEQ ID NO: 208 or 209 and a LC of SEQ ID NO: 210. In an embodiment, the} _{anti-interface bNAb or fragment thereof, comprises a HC of SEQ ID NO: 219 or 220 and a LC of SEQ} ID NO: 221. In an embodiment, the anti-interface bNAb or fragment thereof, comprises a HC of SEQ _{ID NO: 230 or 231 and a LC of SEQ ID NO: 232. In an embodiment, the anti-interface bNAb or} _{fragment thereof, comprises a HC of SEQ ID NO: 241 or 242 and a LC of SEQ ID NO: 243.} Anti-apex bNAbs I_{n particular, an antigen binding protein of the invention may comprise an anti-apex bNAb or} _{a fragment thereof (i.e. a broadly neutralizing antibody or fragment binds to the V1/V2 loop of a} gp120 protein)). A fragment may include Fab, F(ab’)2, Fv, disulphide linked Fv, single chain Fv (scFv), disulphide-linked scFv, diabodies, TANDABS, etc. and modified versions of any of the foregoing. For example, scFv variants of anti-apex bNAbs have been described in van Dorsten et al. _{2022 (PMID: 34935437). An anti-apex bNAb or fragment thereof includes an antibody comprising a} _{set of CDRs (CDRH1, CDRH2, CDRH3, CDRL1, CDRL2 and CDRL3) as set out in rows 15 to 30 of} _{Table 3 (Apex bNAb1-16).} An anti-apex bNAb or fragment thereof also includes an antibody comprising a pair of _{variable domains (a VH and VL) set out in rows 15 to 30 of Table 4 (Apex-bNAb1-16).} _{An anti- apex bNAb may be an antibody comprising a heavy chain (HC), with or without} _{M428L/N434S (EU numbering) ‘LS’ mutations, and a light chain (LC) as set out in rows 15 to 30 of} _{Table 4 (Apex bNAb1-16). In an embodiment, the HC comprises LS.} In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 244, a CDRH2 of SEQ ID NO: 245, a CDRH3 of SEQ ID NO: 246, a CDRL1 of SEQ ID NO: 247, a _{CDRL2 of SEQ ID NO: 248 and a CDRL3 of SEQ ID NO: 249. In an embodiment, the anti-apex bNAb} or fragment thereof comprises a CDRH1 of SEQ ID NO: 255, a CDRH2 of SEQ ID NO: 256, a CDRH3 of SEQ ID NO: 257, a CDRL1 of SEQ ID NO: 258, a CDRL2 of SEQ ID NO: 259 and a CDRL3 of SEQ ID NO: 260. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 266, a CDRH2 of SEQ ID NO: 267, a CDRH3 of SEQ ID NO: 268, a CDRL1 of SEQ ID NO: _{269, a CDRL2 of SEQ ID NO: 270 and a CDRL3 of SEQ ID NO: 271. In an embodiment, the anti-} apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 277, a CDRH2 of SEQ ID NO: _{278, a CDRH3 of SEQ ID NO: 279, a CDRL1 of SEQ ID NO: 280, a CDRL2 of SEQ ID NO: 281 and a} CDRL3 of SEQ ID NO: 282. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 288, a CDRH2 of SEQ ID NO: 289, a CDRH3 of SEQ ID NO: 290, a CDRL1 of _{SEQ ID NO: 291, a CDRL2 of SEQ ID NO: 292 and a CDRL3 of SEQ ID NO: 293. In an embodiment,} the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 299, a CDRH2 of SEQ ID NO: 300, a CDRH3 of SEQ ID NO: 301, a CDRL1 of SEQ ID NO: 302, a CDRL2 of SEQ ID NO: 303 and a CDRL3 of SEQ ID NO: 304. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 310, a CDRH2 of SEQ ID NO: 311, a CDRH3 of SEQ ID NO: 312, _{a CDRL1 of SEQ ID NO: 313, a CDRL2 of SEQ ID NO: 314 and a CDRL3 of SEQ ID NO: 315. In an} embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 321, a CDRH2 of SEQ ID NO: 322, a CDRH3 of SEQ ID NO: 323, a CDRL1 of SEQ ID NO: 324, a CDRL2 of _{SEQ ID NO: 325 and a CDRL3 of SEQ ID NO: 326. In an embodiment, the anti-apex bNAb or} fragment thereof comprises a CDRH1 of SEQ ID NO: 332, a CDRH2 of SEQ ID NO: 333, a CDRH3 of _{SEQ ID NO: 334, a CDRL1 of SEQ ID NO: 335, a CDRL2 of SEQ ID NO: 336 and a CDRL3 of SEQ ID} _{NO: 337. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID} NO: 343, a CDRH2 of SEQ ID NO: 344, a CDRH3 of SEQ ID NO: 345, a CDRL1 of SEQ ID NO: 346, a _{CDRL2 of SEQ ID NO: 347 and a CDRL3 of SEQ ID NO: 348. In an embodiment, the anti-apex bNAb} or fragment thereof comprises a CDRH1 of SEQ ID NO: 354, a CDRH2 of SEQ ID NO: 355, a CDRH3 _{of SEQ ID NO: 356, a CDRL1 of SEQ ID NO: 357, a CDRL2 of SEQ ID NO: 358 and a CDRL3 of SEQ} ID NO: 359. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 365, a CDRH2 of SEQ ID NO: 366, a CDRH3 of SEQ ID NO: 367, a CDRL1 of SEQ ID NO: _{368, a CDRL2 of SEQ ID NO: 369 and a CDRL3 of SEQ ID NO: 370. In an embodiment, the anti-} apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 376, a CDRH2 of SEQ ID NO: _{377, a CDRH3 of SEQ ID NO: 378, a CDRL1 of SEQ ID NO: 379, a CDRL2 of SEQ ID NO: 380 and a} CDRL3 of SEQ ID NO: 381. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 387, a CDRH2 of SEQ ID NO: 388, a CDRH3 of SEQ ID NO: 389, a CDRL1 of _{SEQ ID NO: 390, a CDRL2 of SEQ ID NO: 391 and a CDRL3 of SEQ ID NO: 392. In an embodiment,} the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 398, a CDRH2 of SEQ ID NO: 399, a CDRH3 of SEQ ID NO: 400, a CDRL1 of SEQ ID NO: 401, a CDRL2 of SEQ ID NO: 402 and a CDRL3 of SEQ ID NO: 403. In an embodiment, the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 409, a CDRH2 of SEQ ID NO: 410, a CDRH3 of SEQ ID NO: 411, _{a CDRL1 of SEQ ID NO: 412, a CDRL2 of SEQ ID NO: 413 and a CDRL3 of SEQ ID NO: 414.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having _{at least 95% sequence identity to SEQ ID NO: 250 and a VL domain having at least 95% sequence} identity to SEQ ID NO: 251, optionally wherein the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 244, a CDRH2 of SEQ ID NO: 245, a CDRH3 of SEQ ID NO: 246, a CDRL1 of _{SEQ ID NO: 247, a CDRL2 of SEQ ID NO: 248 and a CDRL3 of SEQ ID NO: 249.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having at least 95% sequence identity to SEQ ID NO: 261 and a VL domain having at least 95% sequence identity to SEQ ID NO: 262, optionally wherein the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 255, a CDRH2 of SEQ ID NO: 256, a CDRH3 of SEQ ID NO: 257, a CDRL1 of _{SEQ ID NO: 258, a CDRL2 of SEQ ID NO: 259 and a CDRL3 of SEQ ID NO: 260.} _{In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having} _{at least 95% sequence identity to SEQ ID NO: 272 and a VL domain having at least 95% sequence} identity to SEQ ID NO: 273, optionally wherein the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 266, a CDRH2 of SEQ ID NO: 267, a CDRH3 of SEQ ID NO: 268, a CDRL1 of _{SEQ ID NO: 269, a CDRL2 of SEQ ID NO: 270 and a CDRL3 of SEQ ID NO: 271.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having _{at least 95% sequence identity to SEQ ID NO: 283 and a VL domain having at least 95% sequence} identity to SEQ ID NO: 284, optionally wherein the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 277, a CDRH2 of SEQ ID NO: 278, a CDRH3 of SEQ ID NO: 279, a CDRL1 of _{SEQ ID NO: 280, a CDRL2 of SEQ ID NO: 281 and a CDRL3 of SEQ ID NO: 282.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having _{at least 95% sequence identity to SEQ ID NO: 294 and a VL domain having at least 95% sequence} identity to SEQ ID NO: 295, optionally wherein the anti-apex bNAb or fragment thereof comprises a CDRH1 of SEQ ID NO: 288, a CDRH2 of SEQ ID NO: 289, a CDRH3 of SEQ ID NO: 290, a CDRL1 of _{SEQ ID NO: 291, a CDRL2 of SEQ ID NO: 292 and a CDRL3 of SEQ ID NO: 293.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having _{at least 95% sequence identity to SEQ ID NO: 305 and a VL domain having at least 95% sequence} _{identity to SEQ ID NO: 306 optionally wherein the anti-apex bNAb or fragment thereof comprises a} CDRH1 of SEQ ID NO: 299, a CDRH2 of SEQ ID NO: 300, a CDRH3 of SEQ ID NO: 301, a CDRL1 of _{SEQ ID NO: 302, a CDRL2 of SEQ ID NO: 303 and a CDRL3 of SEQ ID NO: 304.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having _{at least 95% sequence identity to SEQ ID NO: 316 and a VL domain having at least 95% sequence} _{identity to SEQ ID NO: 317 optionally wherein the anti-apex bNAb or fragment thereof comprises a} CDRH1 of SEQ ID NO: 310, a CDRH2 of SEQ ID NO: 311, a CDRH3 of SEQ ID NO: 312, a CDRL1 of _{SEQ ID NO: 313, a CDRL2 of SEQ ID NO: 314 and a CDRL3 of SEQ ID NO: 315.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having _{at least 95% sequence identity to SEQ ID NO: 327 and a VL domain having at least 95% sequence} _{identity to SEQ ID NO: 328 optionally wherein the anti-apex bNAb or fragment thereof comprises a} CDRH1 of SEQ ID NO: 321, a CDRH2 of SEQ ID NO: 322, a CDRH3 of SEQ ID NO: 323, a CDRL1 of _{SEQ ID NO: 324, a CDRL2 of SEQ ID NO: 325 and a CDRL3 of SEQ ID NO: 326.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having _{at least 95% sequence identity to SEQ ID NO: 338 and a VL domain having at least 95% sequence} _{identity to SEQ ID NO: 339 optionally wherein the anti-apex bNAb or fragment thereof comprises a} comprises a CDRH1 of SEQ ID NO: 332, a CDRH2 of SEQ ID NO: 333, a CDRH3 of SEQ ID NO: 334, _{a CDRL1 of SEQ ID NO: 335, a CDRL2 of SEQ ID NO: 336 and a CDRL3 of SEQ ID NO: 337.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having _{at least 95% sequence identity to SEQ ID NO: 349 and a VL domain having at least 95% sequence} _{identity to SEQ ID NO: 350 optionally wherein the anti-apex bNAb or fragment thereof comprises a} CDRH1 of SEQ ID NO: 343, a CDRH2 of SEQ ID NO: 344, a CDRH3 of SEQ ID NO: 345, a CDRL1 of _{SEQ ID NO: 346, a CDRL2 of SEQ ID NO: 347 and a CDRL3 of SEQ ID NO: 348.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having _{at least 95% sequence identity to SEQ ID NO: 360 and a VL domain having at least 95% sequence} _{identity to SEQ ID NO: 361 optionally wherein the anti-apex bNAb or fragment thereof comprises a} CDRH1 of SEQ ID NO: 354, a CDRH2 of SEQ ID NO: 355, a CDRH3 of SEQ ID NO: 356, a CDRL1 of _{SEQ ID NO: 357, a CDRL2 of SEQ ID NO: 358 and a CDRL3 of SEQ ID NO: 359.} _{In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having} _{at least 95% sequence identity to SEQ ID NO: 371 and a VL domain having at least 95% sequence} _{identity to SEQ ID NO: 372 optionally wherein the anti-apex bNAb or fragment thereof comprises a} _{CDRH1 of SEQ ID NO: 365, a CDRH2 of SEQ ID NO: 366, a CDRH3 of SEQ ID NO: 367, a CDRL1 of} _{SEQ ID NO: 368, a CDRL2 of SEQ ID NO: 369 and a CDRL3 of SEQ ID NO: 370.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having _{at least 95% sequence identity to SEQ ID NO: 382 and a VL domain having at least 95% sequence} _{identity to SEQ ID NO: 383 optionally wherein the anti-apex bNAb or fragment thereof comprises a} CDRH1 of SEQ ID NO: 376, a CDRH2 of SEQ ID NO: 377, a CDRH3 of SEQ ID NO: 378, a CDRL1 of _{SEQ ID NO: 379, a CDRL2 of SEQ ID NO: 380 and a CDRL3 of SEQ ID NO: 381.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having _{at least 95% sequence identity to SEQ ID NO: 393 and a VL domain having at least 95% sequence} _{identity to SEQ ID NO: 394 optionally wherein the anti-apex bNAb or fragment thereof comprises a} CDRH1 of SEQ ID NO: 387, a CDRH2 of SEQ ID NO: 388, a CDRH3 of SEQ ID NO: 389, a CDRL1 of _{SEQ ID NO: 390, a CDRL2 of SEQ ID NO: 391 and a CDRL3 of SEQ ID NO: 392.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having _{at least 95% sequence identity to SEQ ID NO: 404 and a VL domain having at least 95% sequence} _{identity to SEQ ID NO: 405 optionally wherein the anti-apex bNAb or fragment thereof comprises a} CDRH1 of SEQ ID NO: 398, a CDRH2 of SEQ ID NO: 399, a CDRH3 of SEQ ID NO: 400, a CDRL1 of _{SEQ ID NO: 401, a CDRL2 of SEQ ID NO: 402 and a CDRL3 of SEQ ID NO: 403.} In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain having _{at least 95% sequence identity to SEQ ID NO: 415 and a VL domain having at least 95% sequence} _{identity to SEQ ID NO: 416 optionally wherein the anti-apex bNAb or fragment thereof comprises a} CDRH1 of SEQ ID NO: 409, a CDRH2 of SEQ ID NO: 410, a CDRH3 of SEQ ID NO: 411, a CDRL1 of _{SEQ ID NO: 412, a CDRL2 of SEQ ID NO: 413 and a CDRL3 of SEQ ID NO: 414.} _{In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ} _{ID NO: 250 and a VL domain of SEQ ID NO: 251. In an embodiment, the anti-apex bNAb or} _{fragment thereof, comprises a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262.} _{In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO:} _{272 and a VL domain of SEQ ID NO: 273. In an embodiment, the anti-apex bNAb or fragment} _{thereof, comprises a VH domain of SEQ ID NO: 283 and a VL domain of SEQ ID NO: 284. In an} _{embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO: 294} _{and a VL domain of SEQ ID NO: 295. In an embodiment, the anti-apex bNAb or fragment thereof,} _{comprises a VH domain of SEQ ID NO: 305 and a VL domain of SEQ ID NO: 306. In an embodiment,} _{the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO: 316 and a VL} _{domain of SEQ ID NO: 317. In an embodiment, the anti-apex bNAb or fragment thereof, comprises} _{a VH domain of SEQ ID NO: 327 and a VL domain of SEQ ID NO: 328. In an embodiment, the anti-} _{apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO: 338 and a VL domain of SEQ} _{ID NO: 339. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain of} _{SEQ ID NO: 349 and a VL domain of SEQ ID NO: 350. In an embodiment, the anti-apex bNAb or} _{fragment thereof, comprises a VH domain of SEQ ID NO: 360 and a VL domain of SEQ ID NO: 361.} _{In an embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO:} _{371 and a VL domain of SEQ ID NO: 372. In an embodiment, the anti-apex bNAb or fragment} _{thereof, comprises a VH domain of SEQ ID NO: 382 and a VL domain of SEQ ID NO: 383. In an} _{embodiment, the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO: 393} _{and a VL domain of SEQ ID NO: 394. In an embodiment, the anti-apex bNAb or fragment thereof,} _{comprises a VH domain of SEQ ID NO: 404 and a VL domain of SEQ ID NO: 405. In an embodiment,} _{the anti-apex bNAb or fragment thereof, comprises a VH domain of SEQ ID NO: 415 and a VL} domain of SEQ ID NO: 416. I_{n an embodiment, the anti-apex bNAb or fragment thereof, comprises a heavy chain (HC)} _{having at least 95% sequence identity to SEQ ID NO: 252 or 253 and a light chain (LC) having at} _{least 95% sequence identity to SEQ ID NO: 254. In an embodiment, the anti-apex bNAb or} _{fragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID NO: 263 or 264} _{and a LC having at least 95% sequence identity to SEQ ID NO: 265. In an embodiment, the anti-} _{apex bNAb or fragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID} _{NO: 274 or 275 and a LC having at least 95% sequence identity to SEQ ID NO: 276. In an} _{embodiment, the anti-apex bNAb or fragment thereof, comprises a HC having at least 95%} _{sequence identity to SEQ ID NO: 285 or 286 and a LC having at least 95% sequence identity to SEQ} _{ID NO: 287. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC having at} _{least 95% sequence identity to SEQ ID NO: 296 or 297 and a LC having at least 95% sequence} _{identity to SEQ ID NO: 298. In an embodiment, the anti-apex bNAb or fragment thereof, comprises} _{a HC having at least 95% sequence identity to SEQ ID NO: 307 or 308 and a LC having at least 95%} _{sequence identity to SEQ ID NO: 309. In an embodiment, the anti-apex bNAb or fragment thereof,} _{comprises a HC having at least 95% sequence identity to SEQ ID NO: 318 or 319 and a LC having at} _{least 95% sequence identity to SEQ ID NO: 320. In an embodiment, the anti-apex bNAb or} _{fragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID NO: 329 or 330} _{and a LC having at least 95% sequence identity to SEQ ID NO: 331. In an embodiment, the anti-} _{apex bNAb or fragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID} _{NO: 340 or 341 and a LC having at least 95% sequence identity to SEQ ID NO: 342. In an} _{embodiment, the anti-apex bNAb or fragment thereof, comprises a HC having at least 95%} _{sequence identity to SEQ ID NO: 351 or 352 and a LC having at least 95% sequence identity to SEQ} _{ID NO: 353. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC having at} _{least 95% sequence identity to SEQ ID NO: 362 or 363 and a LC having at least 95% sequence} _{identity to SEQ ID NO: 364. In an embodiment, the anti-apex bNAb or fragment thereof, comprises} _{a HC having at least 95% sequence identity to SEQ ID NO: 373 or 374 and a LC having at least 95%} _{sequence identity to SEQ ID NO: 375. In an embodiment, the anti-apex bNAb or fragment thereof,} _{comprises a HC having at least 95% sequence identity to SEQ ID NO: 384 or 385 and a LC having at} _{least 95% sequence identity to SEQ ID NO: 386. In an embodiment, the anti-apex bNAb or} _{fragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID NO: 395 or 396} _{and a LC having at least 95% sequence identity to SEQ ID NO: 397. In an embodiment, the anti-} _{apex bNAb or fragment thereof, comprises a HC having at least 95% sequence identity to SEQ ID} _{NO: 406 or 407 and a LC having at least 95% sequence identity to SEQ ID NO: 408. In an} _{embodiment, the anti-apex bNAb or fragment thereof, comprises a HC having at least 95%} _{sequence identity to SEQ ID NO: 417 or 418 and a LC having at least 95% sequence identity to SEQ} ID NO: 419. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a heavy chain (HC) _{of SEQ ID NO: 252 or 253 and a light chain (LC) of SEQ ID NO: 254. In an embodiment, the anti-} _{apex bNAb or fragment thereof, comprises a HC of SEQ ID NO: 263 or 264 and a LC of SEQ ID NO:} 265. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID NO: _{274 or 275 and a LC of SEQ ID NO: 276. In an embodiment, the anti-apex bNAb or fragment} _{thereof, comprises a HC of SEQ ID NO: 285 or 286 and a LC of SEQ ID NO: 287. In an embodiment,} _{the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID NO: 296 or 297 and a LC of SEQ} ID NO: 298. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID _{NO: 307 or 308 and a LC of SEQ ID NO: 309. In an embodiment, the anti-apex bNAb or fragment} _{thereof, comprises a HC of SEQ ID NO: 318 or 319 and a LC of SEQ ID NO: 320. In an embodiment,} _{the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID NO: 329 or 330 and a LC of SEQ} ID NO: 331. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID _{NO: 340 or 341 and a LC of SEQ ID NO: 342. In an embodiment, the anti-apex bNAb or fragment} _{thereof, comprises a HC of SEQ ID NO: 351 or 352 and a LC of SEQ ID NO: 353. In an embodiment,} _{the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID NO: 362 or 363 and a LC of SEQ} ID NO: 364. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID _{NO: 373 or 374 and a LC of SEQ ID NO: 375. In an embodiment, the anti-apex bNAb or fragment} _{thereof, comprises a HC of SEQ ID NO: 384 or 385 and a LC of SEQ ID NO: 386. In an embodiment,} _{the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID NO: 395 or 396 and a LC of SEQ} ID NO: 397. In an embodiment, the anti-apex bNAb or fragment thereof, comprises a HC of SEQ ID _{NO: 406 or 407 and a LC of SEQ ID NO: 408. In an embodiment, the anti-apex bNAb or fragment} _{thereof, comprises a HC of SEQ ID NO: 417 or 418 and a LC of SEQ ID NO: 419.} Linkers Examples of suitable linkers include amino acid sequences that are from 1 amino acid to 150 amino acids in length. In particular, from 1 to 140 amino acids, from 1 to 130 amino acids, from 1 to 120 amino acids, from 1 to 110 amino acids, from 1 to 100 amino acids, from 1 to 90 amino acids, from 1 to 80 amino acids, from 1 to 70 amino acids, from 1 to 60 amino acids, from 1 to 50 amino acids, from 1 to 40 amino acids, from 1 to 30 amino acids, from 1 to 20 amino acids, from 1 to 10 amino _{acids, from 5 to 30 amino acids. In an embodiment, the linker is an amino acid sequence from 5 to} 30 amino acids in length. In an embodiment, the linker is an amino acid sequence as set forth in any one of SEQ ID _{NOs: 30 to 35. In an embodiment, the linker is an amino acid sequence as set forth in SEQ ID} NO:30. In an embodiment, the linker is a multimer of the amino acid sequence as set forth in SEQ _{ID NO: 30. In an embodiment, the linker is [SEQ ID NO:30]n, wherein n is an integer from 1 to 6. In} an embodiment, the linker is an amino acid sequence as set forth in SEQ ID NO:31. In an embodiment, the linker is an amino acid sequence as set forth in SEQ ID NO:32. In an embodiment, the linker is an amino acid sequence as set forth in SEQ ID NO:33. In an embodiment, the linker is an amino acid sequence as set forth in SEQ ID NO:34. In an embodiment, the linker is an amino acid sequence as set forth in SEQ ID NO:35. Any of the aforementioned linkers may be incorporated into an antigen binding protein of the invention. In particular, any of the aforementioned linkers may be used to join a domain within the antigen binding protein to another domain within the antigen binding protein. In particular, any of the aforementioned linkers may be used to join a CD4 domain within the antigen binding protein _{to a broadly neutralizing antibody or fragment thereof that binds to the V1/V2 apex of the gp120} protein or the gp120-gp41 interface of a gp120 and gp41 protein of HIV. Further, any of the aforementioned linkers may be used to join a CD4 domain as disclosed herein to a bNAb as disclosed herein. In an embodiment, the linker is an amino acid sequence as set forth in any one of _{SEQ ID NOs: 30 to 35. In an embodiment, the linker is an amino acid sequence as set forth in SEQ} _{ID NO: 30.} In an embodiment, a linker is used to join the C-terminus of a CD4 domain to the N- terminus of a bNAb heavy chain variable domain. In an embodiment, a linker is used to join the C- terminus of a CD4 domain to the N-terminus of a bNAb light chain variable domain. In an embodiment, a linker is used to join the C-terminus of a CD4 domain to the N-terminus of a bNAb heavy chain variable domain and a linker is used to join the C-terminus of a CD4 domain to the N- terminus of a bNAb light chain variable domain. In an embodiment, a linker is used to join the C- terminus of a CD4 domain to the N-terminus of a bNAb heavy chain variable domain and an identical linker is used to join the C-terminus of a CD4 domain to the N-terminus of a bNAb light chain variable domain. In an embodiment, the linker is an amino acid sequence as set forth in any one of _{SEQ ID NOs: 30 to 35. In an embodiment, the linker is an amino acid sequence as set forth in SEQ} _{ID NO: 30.} In an embodiment, a linker is used to join the N-terminus of a CD4 domain to the C- terminus of a bNAb heavy chain. In an embodiment, a linker is used to join the N-terminus of a CD4 domain to the C-terminus of a bNAb heavy chain variable domain. In an embodiment, a linker is used to join the N-terminus of a CD4 domain to the C-terminus of a bNAb light chain. In an embodiment, a linker is used to join the N-terminus of a CD4 domain to the C-terminus of a bNAb light chain variable domain. In an embodiment, a linker is used to join the N-terminus of a CD4 domain to the C-terminus of an Fc domain. In an embodiment, the linker is an amino acid sequence _{as set forth in any one of SEQ ID NOs: 30 to 35. In an embodiment, the linker is an amino acid} _{sequence as set forth in SEQ ID NO: 30.} Any of the aforementioned linkers may be used to join a VH and VL pair as disclosed herein to form a scFv. In an embodiment, the linker between the VH domain and the VL domain of the scFv _{is selected from one of SEQ ID NOs: 30-35. In a particular embodiment, the linker between the VH} _{domain and the VL domain of the scFv is SEQ ID NO: 33.} Any of the aforementioned linkers may be used to join a scFv as disclosed herein to an Fc domain. In an embodiment, the scFv is fused to a human Fc via a linker selected from one of SEQ _{ID NO: 30-35. In an embodiment, the scFv is fused to a human Fc via a linker of SEQ ID NO: 31.} Bispecific proteins In an embodiment, the multimeric binding protein of the invention is a bispecific binding _{protein. Examples of such bispecific binding protein are embodiments are disclosed in the below} _{Table 5.}

Table 5: Discloses bispecific proteins under the scope of the invention with reference to the _{sequences provided in Tables 3 and 4. For example, the cell containing an “X” in the table includes a} bispecific binding protein of the invention comprising a CD4 domain having a sequence of SEQ ID _{NO: 11 and a bNAb or fragment thereof comprising a VH domain having at least 95% sequence} identity to SEQ ID NO: 96 and a VL domain having at least 95% sequence identity of SEQ ID NO: 97 (first row of Table 4) and CDRs according to SEQ ID NOs: 90-95 (first row of Table 3). CD4 domain comprises… (e.g. joined by a linker at the N-terminus of the heavy or light chain of the bnAb) B_{road to narrow >>>>>} Comprises a sequence according to SEQ ID NO: 3_{1 4 5-21 5-15 11} HC/LC according to any of pair disclosed in a row of Table 4 HC/LC having 95% sequence identity to any of pair of HC/LC disclosed in a row of Table 4 with > > > CDRs according to the equivalent row in Table wo 3 r_ra n HC/LC having 95% sequence identity to any of o ^t d pair of HC/LC disclosed in a row of Table 4 a o_r b VH/VL according to any of pair disclosed in a row of Table 4 …se VH/VL having 95% sequence identity to any of sⁱ _r p pair of VH/VL disclosed in a row of Table 4 with m X o c CDRs according to the equivalent row in Table b A 3 N b VH/VL having 95% sequence identity to any of pair of VH/VL disclosed in a row of Table 4 C_{DRs according to any of pair disclosed in a} row of Table 3 In an embodiment, the bispecific binding protein comprises a CD4 domain and a broadly neutralizing antibody or fragment thereof comprising a pair of variable domains (a VH and a VL) as set out in any row of Table 4. In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of any one of SEQ ID NOs: 1-21 and a broadly neutralizing antibody or fragment thereof} comprising a pair of variable domains (a VH and a VL) as set out in any row of Table 4. In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and a broadly neutralizing antibody or fragment thereof comprising a} pair of variable domains (a VH and a VL) as set out in any row of Table 4. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 107 and a VL domain of SEQ ID NO: 108. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 118 and a VL domain of SEQ ID NO: 119. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 129 and a VL domain of SEQ ID NO: 130. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 140 and a VL domain of SEQ ID NO: 141. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 151 and a VL domain of SEQ ID NO: 152. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 162 and a VL domain of SEQ ID NO: 163. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 173 and a VL domain of SEQ ID NO: 174. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 184 and a VL domain of SEQ ID NO: 185. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain of SEQ ID NO: 195 and a VL domain of SEQ ID NO: 196. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain _{of SEQ ID NO: 206 and a VL domain of SEQ ID NO: 207.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain _{of SEQ ID NO: 217 and a VL domain of SEQ ID NO: 218.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain _{of SEQ ID NO: 228 and a VL domain of SEQ ID NO: 229.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-interface bNAb or fragment thereof comprising a VH domain _{of SEQ ID NO: 239 and a VL domain of SEQ ID NO: 240.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} _{SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} _{SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} _{SEQ ID NO: 272 and a VL domain of SEQ ID NO: 273.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} _{SEQ ID NO: 283 and a VL domain of SEQ ID NO: 284.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} _{SEQ ID NO: 294 and a VL domain of SEQ ID NO: 295.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} _{SEQ ID NO: 305 and a VL domain of SEQ ID NO: 306.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} _{SEQ ID NO: 316 and a VL domain of SEQ ID NO: 317.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} _{SEQ ID NO: 327 and a VL domain of SEQ ID NO: 328.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} _{SEQ ID NO: 338 and a VL domain of SEQ ID NO: 339.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} _{SEQ ID NO: 349 and a VL domain of SEQ ID NO: 350.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} SEQ ID NO: 360 and a VL domain of SEQ ID NO: 361. In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} _{SEQ ID NO: 371 and a VL domain of SEQ ID NO: 372.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} _{SEQ ID NO: 382 and a VL domain of SEQ ID NO: 383.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} _{SEQ ID NO: 393 and a VL domain of SEQ ID NO: 394.} In an embodiment, the bispecific binding protein comprises a CD4 domain having a _{sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof comprising a VH domain of} SEQ ID NO: 404 and a VL domain of SEQ ID NO: 405. In an embodiment, the bispecific binding protein comprises a CD4 domain having a sequence of SEQ ID NO: 11 and an anti-apex bNAb or fragment thereof, comprises a VH domain of _{SEQ ID NO: 415 and a VL domain of SEQ ID NO: 416.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO:60. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 60 and a sequence according to SEQ ID NO: 100.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 61. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 61 and a sequence according to SEQ ID NO: 111.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 62. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 62 and a sequence according to SEQ ID NO: 122. I_{n an embodiment,the bispecific binding protein comprises a sequence according to SEQ ID} NO: 63. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 63 and a sequence according to SEQ ID NO: 133. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 64. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 64 and a sequence according to SEQ ID NO: 144. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 65. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 65 and a sequence according to SEQ ID NO: 155. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 66. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 66 and a sequence according to SEQ ID NO: 166. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 67. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 67 and a sequence according to SEQ ID NO: 177. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 68. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 68 and a sequence according to SEQ ID NO: 188. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 69. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 69 and a sequence according to SEQ ID NO: 199. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 70. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 70 and a sequence according to SEQ ID NO: 210. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 71. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 71 and a sequence according to SEQ ID NO: 221. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 72. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 72 and a sequence according to SEQ ID NO: 232.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 73. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 73 and a sequence according to SEQ ID NO: 243.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 74. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 74 and a sequence according to SEQ ID NO: 254.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 75. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 75 and a sequence according to SEQ ID NO: 265.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 76. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 76 and a sequence according to SEQ ID NO: 276.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID NO: 77. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 77 and a sequence according to SEQ ID NO: 287.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 78. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 78 and a sequence according to SEQ ID NO: 298.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 79. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 79 and a sequence according to SEQ ID NO: 309.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 80. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 80 and a sequence according to SEQ ID NO: 320.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 81. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 81 and a sequence according to SEQ ID NO: 331.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 82. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 82 and a sequence according to SEQ ID NO: 342.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 83. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 83 and a sequence according to SEQ ID NO: 353.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 84. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 84 and a sequence according to SEQ ID NO: 364.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 85. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 85 and a sequence according to SEQ ID NO: 375.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 86. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 86 and a sequence according to SEQ ID NO: 386.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 87. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 87 and a sequence according to SEQ ID NO: 397.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 88. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 88 and a sequence according to SEQ ID NO: 408.} In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO: 89. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} _{NO: 89 and a sequence according to SEQ ID NO: 419.} Exemplary bispecific binding proteins Interface-bNAb17 e.g. supported by data in Figure 20 I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} _{antibody which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at} least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the _{N-terminus or C-terminus of one of the heavy chains or light chains of the broadly neutralizing} antibody. I_{n an embodiment, the bispecific binding protein comprises a broadly neutralizing antibody} _{which has a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2 and CDRL3 as set out in row 1 of Table 3} _{(interface-bNAb17). In an embodiment, the bispecific binding protein comprises a broadly} neutralizing antibody or fragment thereof which has a VH and VL as set out in row 1 of Table 4 (interface-bNAb17). I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 according to SEQ ID NO: 90- 95 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the _{N-terminus or C-terminus of one of the heavy chains or light chains of the broadly neutralizing} antibody. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain having at least 95% sequence identity to SEQ ID NO: 96 and a VL _{domain having at least 95% sequence identity to SEQ ID NO: 97 and which binds to the gp120-} _{gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds} to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or C-terminus of one of _{the heavy chains or light chains of the broadly neutralizing antibody. Optionally wherein the} _{antibody comprises six CDRs according SEQ ID NO: 90-95.} _{In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or _{C-terminus of one of the heavy chains or light chains of the broadly neutralizing antibody.} _{In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of _{one of the heavy chains or light chains of the broadly neutralizing antibody.} _{In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of _{one of the heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4} domain comprises a sequence according to SEQ ID NO: 1-21. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of _{one of the heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4} domain comprises a sequence according to SEQ ID NO: 5-21. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of _{one of the heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4} domain comprises a sequence according to SEQ ID NO: 5-15. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of _{one of the heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4} domain comprises a sequence according to SEQ ID NO: 11. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of _{one of the heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4} domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of a sequence according to SEQ ID NO: 30-35. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of _{one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain} comprises a sequence according to SEQ ID NO: 11 and the linker consists of a sequence according to SEQ ID NO: 30-35. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 96 and a VL domain of SEQ ID NO: 97 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of _{one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain} comprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 98 or 99 and a light chain of SEQ ID NO: 100 and _{which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one} CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C- terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-21 and the linker consists of SEQ ID NO: 30-35. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 98 or 99 and a light chain of SEQ ID NO: 100 and _{which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one} CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C- terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-21 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 98 or 99 and a light chain of SEQ ID NO: 100 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C- terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-15 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing _{antibody comprising a heavy chain of SEQ ID NO: 98 or 99 and a light chain of SEQ ID NO: 100 and} which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C- terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 _{domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30.} In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 99 and a light chain of SEQ ID NO: 100 and which binds to the gp120-gp41 interface region of a gp120 and a gp41 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO:60. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} NO:60 and a sequence according to SEQ ID NO: 100. Apex-bNAb1 e.g. supported by data in Figure 4 I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or C- _{terminus of one of heavy chains or light chains of the broadly neutralizing antibody.} _{In an embodiment, the bispecific binding protein comprises a broadly neutralizing antibody} which has a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2 and CDRL3 as set out in row 15 of Table 3 _{(apex-bNAb1). In an embodiment, the bispecific binding protein comprises a broadly neutralizing} antibody or fragment thereof which has a VH and VL as set out in row 15 of Table 4 (apex-bNAb1). I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 according to SEQ ID NO: 244-249 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or _{C-terminus of one of the heavy chains or light chains of the broadly neutralizing antibody.} _{In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain having at least 95% sequence identity to SEQ ID NO: 250 and a VL domain having at least 95% sequence identity to SEQ ID NO: 251 and which binds to the V1/V2 _{apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the} CD4 domain is attached by a linker to the N-terminus or C-terminus of one of the heavy chains or _{light chains of the broadly neutralizing antibody. Optionally wherein the antibody comprises six CDRs} according SEQ ID NO: 244-249. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or C-terminus of _{one of the heavy chains or light chains of the broadly neutralizing antibody.} _{In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains or light chains of the broadly neutralizing antibody.} _{In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domain} comprises a sequence according to SEQ ID NO: 1-21. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domain} comprises a sequence according to SEQ ID NO: 5-21. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domain} comprises a sequence according to SEQ ID NO: 5-15. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domain} comprises a sequence according to SEQ ID NO: 11. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domain} comprises a sequence according to SEQ ID NO: 11 and the linker consists of a sequence according to SEQ ID NO: 30-35. _{In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a} sequence according to SEQ ID NO: 11 and the linker consists of a sequence according to SEQ ID NO: 30-35. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 250 and a VL domain of SEQ ID NO: 251 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a} sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 252 or 253 and a light chain of SEQ ID NO: 254 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-21 and the linker consists of SEQ ID NO: 30-35. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 252 or 253 and a light chain of SEQ ID NO: 254 and which binds to V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which _{binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the} heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-21 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 252 or 253 and a light chain of SEQ ID NO: 254 and which binds to V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-15 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 252 or 253 and a light chain of SEQ ID NO: 254 and which binds to V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 253 and a light chain of SEQ ID NO: 254 and which binds to V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO:74. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} NO:74 and a sequence according to SEQ ID NO: 254. _{Apex-bNAb2 – e.g. supported by data in Figure 5} _{In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or C- _{terminus of one of the heavy chains or light chains of the broadly neutralizing antibody.} _{In an embodiment, the bispecific binding protein comprises a broadly neutralizing antibody} thereof which has a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2 and CDRL3 as set out in row 16 of Table 3 (apex-bNAb2). In an embodiment, the bispecific binding protein comprises a broadly neutralizing antibody or fragment thereof which has a VH and VL as set out in row 16 of Table 4 (apex-bNAb2). I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 according to SEQ ID NO: 255-260 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or _{C-terminus of one of the heavy chains or light chains of the broadly neutralizing antibody.} _{In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain having at least 95% sequence identity to SEQ ID NO: 261 and a VL domain having at least 95% sequence identity to SEQ ID NO: 262 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or C-terminus of one of the heavy chains or _{light chains of the broadly neutralizing antibody. Optionally wherein the antibody comprises six CDRs} according SEQ ID NO: 255-260. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the N-terminus or C-terminus of _{one of the heavy chains or light chains of the broadly neutralizing antibody.} _{In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains or light chains of the broadly neutralizing antibody.} _{In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domain} comprises a sequence according to SEQ ID NO: 1-21. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domain} comprises a sequence according to SEQ ID NO: 5-21. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domain} comprises a sequence according to SEQ ID NO: 5-15. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domain} comprises a sequence according to SEQ ID NO: 11. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains or light chains of the broadly neutralizing antibody, and wherein the CD4 domain} comprises a sequence according to SEQ ID NO: 11 and the linker consists of a sequence according to SEQ ID NO: 30-35. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a} sequence according to SEQ ID NO: 11 and the linker consists of a sequence according to SEQ ID NO: 30-35. I_{n an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing} antibody comprising a VH domain of SEQ ID NO: 261 and a VL domain of SEQ ID NO: 262 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the _{heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a} sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 263 or 264 and a light chain of SEQ ID NO: 265 and which binds to the V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-21 and the linker consists of SEQ ID NO: 30-35. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 263 or 264 and a light chain of SEQ ID NO: 265 and which binds to V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-21 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 263 or 264 and a light chain of SEQ ID NO: 265 and which binds to V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 5-15 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 263 or 264 and a light chain of SEQ ID NO: 265 and which binds to V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises (i) a broadly neutralizing antibody comprising a heavy chain of SEQ ID NO: 264 and a light chain of SEQ ID NO: 265 and _{which binds to V1/V2 apex region of a gp120 protein; and (ii) at least one CD4 domain which binds} to gp120, wherein the CD4 domain is attached by a linker to the C-terminus of one of the heavy chains of the broadly neutralizing antibody, and wherein the CD4 domain comprises a sequence according to SEQ ID NO: 11 and the linker consists of SEQ ID NO: 30. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID _{NO:75. In an embodiment, the bispecific binding protein comprises a sequence according to SEQ ID} NO:75 and a sequence according to SEQ ID NO: 265. Production methods _{Antigen binding proteins may be prepared by any of a number of conventional techniques. For} _{example, antigen binding proteins may be purified from cells that naturally express them (e.g., an} antibody can be purified from a hybridoma that produces it), or produced in recombinant expression systems. A_{number of different expression systems and purification regimes can be used to generate} the antigen binding proteins of the invention. Generally, host cells are transformed with a recombinant expression vector encoding the desired antigen binding protein. The expression vector may be maintained by the host as a separate genetic element or integrated into the host chromosome depending on the expression system. A wide range of host cells can be employed, _{including Prokaryotes (including Gram-negative or Gram-positive bacteria, for example Escherichia} coli, Bacilli sp., Pseudomonas sp., Corynebacterium sp.), Eukaryotes including yeast (for example Saccharomyces cerevisiae, Pichia pastoris), fungi (for example Aspergilus sp.), or higher Eukaryotes including insect cells and cell lines of mammalian origin (for example, CHO, NS0, PER.C6, HEK293, HeLa). The host cell may be an isolated host cell. The host cell is usually not part of a multicellular _{organism (e.g., plant or animal). The host cell may be a non-human host cell. The host cell may be} a microorganism cell. Appropriate cloning and expression vectors for use with bacterial, fungal, yeast, and mammalian host cells are known in the art. The cells can be cultured under conditions that promote expression of the antigen binding protein using a variety of equipment such as shake flasks, spinner flasks, and bioreactors. The polypeptide(s) is(are) recovered by conventional protein purification procedures. Protein purification procedures typically consist of a series of unit operations comprised of various filtration and chromatographic processes developed to selectively concentrate and isolate the antigen binding protein. The purified antigen binding protein may be formulated in a pharmaceutically acceptable composition. Fc modifications Fc engineering methods can be applied to modify the functional or pharmacokinetics properties of an antigen binding protein, in particular an antibody. Effector function may be altered by making mutations in the Fc region that increase or decrease binding to C1q or Fcγ receptors and modify CDC or ADCC activity respectively. Modifications to the glycosylation pattern of an antibody can also be made to change the effector function. The interaction between the Fc region of an antigen binding protein or antibody and various Fc receptors (FcR), including FcγRI (CD64), FcγRII (CD32), FcγRIII (CD16), FcRn, C1q, and type II Fc receptors is believed to mediate the effector functions of the antigen binding protein or antibody. Significant biological effects can be a consequence of effector functionality. Usually, the ability to mediate effector function requires binding of the antigen binding protein or antibody to an antigen and not all antigen binding proteins or antibodies will mediate every effector function. Effector function can be assessed in a number of ways including, for example, evaluating ADCC effector function of antibody coated to target cells mediated by Natural Killer (NK) cells via FcγRIII, or monocytes/macrophages via FcγRI, or evaluating CDC effector function of antibody coated to target cells mediated by complement cascade via C1q. For example, an antigen binding protein of the present invention can be assessed for ADCC effector function in a Natural Killer cell _{assay. Examples of such assays can be found in Shields et al, 2001, The Journal of Biological} _{Chemistry, Vol. 276, p. 6591-6604; Chappel et al, 1993, The Journal of Biological Chemistry, Vol} _{268, p. 25124-25131; Lazar et al, 2006, PNAS, 103; 4005-4010.} Examples of assays to determine CDC function include those described in J Imm Meth, 1995, 184: 29-38. T_{he effects of mutations on effector functions (e.g., FcRn binding, FcγRs and C1q binding,} _{CDC, ADCML, ADCC, ADCP) can be assessed, e.g., as described in Grevys et al., J Immunol. 2015} _{Jun 1; 194(11): 5497–5508, or Tam et al., Antibodies 2017, 6(3); Monnet et al., 2014 mAbs, 6:2,} 422-436. Throughout this specification, amino acid residues in Fc regions, in antibody sequences or full-length antigen binding protein sequences, are numbered according to the EU index numbering convention. The long half-life of IgG antibodies is reported to be dependent on their binding to FcRn. Therefore, substitutions that increase the binding affinity of IgG to FcRn at pH 6.0 while maintaining the pH dependence of the interaction with target, by engineering the constant region, have been _{extensively studied (Ghetie et al., Nature Biotech. 15: 637-640, 1997; Hinton et al., JBC 279: 6213-} _{6216’ 2004; Dall'Acqua et al., 10 J Immunol 117: 1129-1138, 2006). The in-vivo half-life of antigen} binding proteins of the present invention may be altered by modification of a heavy chain constant domain or an FcRn binding domain therein. In adult mammals, FcRn, plays a key role in maintaining serum antibody levels by acting as a protective receptor that binds and salvages antibodies of the IgG isotype from degradation. IgG molecules are endocytosed by endothelial cells and, if they bind to FcRn, are recycled out of the cells back into circulation. In contrast, IgG molecules that enter the cells and do not bind to FcRn and are targeted to the lysosomal pathway where they are degraded. FcRn is believed to be involved in both antibody clearance and the transcytosis across _{tissues (see Junghans R.P (1997) Immunol.Res 16. 29-57 and Ghetie et al (2000) Annu. Rev.} Immunol. 18, 739-766). Human IgG1 residues determined to interact directly with human FcRn include Ile253, Ser254, Lys288, Thr307, Gln311, Asn434 and His435. Mutations at any of these positions may enable increased serum half-life and/or altered effector properties of antigen binding proteins of the invention. Antigen binding proteins of the present invention may have amino acid modifications that increase the affinity of the constant domain or fragment thereof for FcRn. Increasing the half-life _{(i.e., serum half-life) of therapeutic and diagnostic IgG antibodies and other bioactive molecules has} many benefits including reducing the amount and/or frequency of dosing of these molecules. In one embodiment, an antigen binding protein of the invention comprises all or a portion (an FcRn binding portion) of an IgG constant domain having one or more of the following amino acid modifications. For example, with reference to IgG1, M252Y/S254T/T256E (commonly referred to as “YTE” mutations) and M428L/N434S (commonly referred to as “LS” mutations) increase FcRn binding at _{pH 6.0 (Wang et al. 2018). In an embodiment, an antigen binding protein of the invention} comprises an Fc domain with the LS mutations. In an embodiment, an antigen binding protein of the invention comprises a bNAb in which the LS mutations are present in both of the heavy chain Fc domains. Half-life and FcRn binding can also be extended by introducing H433K and N434F mutations _{(commonly referred to as “HN” or “NHance” mutations) (with reference to IgG1) (WO2006/130834).} Additionally, various publications describe methods for obtaining physiologically active molecules with modified half-lives, either by introducing an FcRn-binding polypeptide into the molecules (WO97/43316, US5869046, US5747035, WO96/32478 and WO91/14438) or by fusing the molecules with antibodies whose FcRn-binding affinities are preserved, but affinities for other Fc receptors have been greatly reduced (WO99/43713), or fusing with FcRn binding domains of antibodies (WO00/09560, US4703039). Post-translational modifications The skilled person will appreciate that, upon production of an antigen binding protein, such as a bispecific molecule of the invention in a host cell, post-translational modifications may occur. For example, this may include the cleavage of certain leader sequences, the addition of various sugar moieties in various glycosylation patterns, non-enzymatic glycation, deamidation, oxidation, disulfide bond scrambling and other cysteine variants such as free sulfhydryls, racemized disulfides, thioethers and trisulfide bonds, isomerisation, C-terminal lysine clipping, and N-terminal glutamine cyclisation. The present invention encompasses the use of antigen binding proteins that have been subjected to, or have undergone, one or more post-translational modifications. Thus an antigen binding protein of the invention includes an “antigen binding protein” as defined earlier that has undergone a post-translational modification such as described herein. Glycation is a post-translational non-enzymatic chemical reaction between a reducing sugar, such as glucose, and a free amine group in the protein, and is typically observed at the epsilon amine of lysine side chains or at the N-Terminus of the protein. Glycation can occur during production and storage only in the presence of reducing sugars. Deamidation can occur during production and storage, is an enzymatic reaction primarily converting asparagine (N) to iso-aspartic acid (iso-aspartate) and aspartic acid (aspartate) (D) at approximately 3:1 ratio. This deamidation reaction is therefore related to isomerization of aspartate (D) to iso-aspartate. The deamidation of asparagine and the isomerisation of aspartate, both involve the intermediate succinimide. To a much lesser degree, deamidation can occur with glutamine residues in a similar manner. Deamidation can occur in a CDR, in a Fab (non-CDR region), or in the Fc region. O_{xidation can occur during production and storage (i.e., in the presence of oxidizing} conditions) and results in a covalent modification of a protein, induced either directly by reactive oxygen species or indirectly by reaction with secondary by-products of oxidative stress. Oxidation happens primarily with methionine residues, but may occur at tryptophan and free cysteine residues. Oxidation can occur in a CDR, in a Fab (non-CDR) region, or in the Fc region. Disulfide bond scrambling can occur during production and basic storage conditions. Under certain circumstances, disulfide bonds can break or form incorrectly, resulting in unpaired cysteine residues (-SH). These free (unpaired) sulfhydryls (-SH) can promote shuffling. The formation of a thioether and racemization of a disulphide bond can occur under basic conditions, in production or storage, through a beta elimination of disulphide bridges back to cysteine residues via a dehydroalanine and persulfide intermediate. Subsequent crosslinking of dehydroalanine and cysteine results in the formation of a thioether bond or the free cysteine _{residues can reform a disulphide bond with a mixture of D- and L-cysteine.} Trisulfides result from insertion of a sulfur atom into a disulphide bond (Cys-S-S-S-Cys) and are formed due to the presence of hydrogen sulphide in production cell culture. N-terminal glutamine (Q) and glutamate (glutamic acid) (E) in the heavy chain and/or light chain is likely to form pyroglutamate (pGlu) via cyclization. Most pGlu formation happens in the production bioreactor, but it can be formed non-enzymatically, depending on pH and temperature of processing and storage conditions. Cyclization of N-terminal Q or E is commonly observed in natural human antibodies. C-terminal lysine clipping is an enzymatic reaction catalyzed by carboxypeptidases, and is commonly observed in recombinant and natural human antibodies. Variants of this process include removal of lysine from one or both heavy chains due to cellular enzymes from the recombinant host cell. Upon administration to the human subject/patient is likely to result in the removal of any remaining C-terminal lysines. Pharmaceutical compositions Antigen binding proteins as described herein may be incorporated into pharmaceutical compositions for use in the treatment or prevention of HIV infection. In one embodiment, the pharmaceutical composition comprises an antigen binding protein in combination with one or more pharmaceutically _{acceptable excipient.} Such compositions comprise a pharmaceutically acceptable carrier as known and called for by acceptable pharmaceutical practice. Pharmaceutical compositions may be administered by injection or continuous infusion (examples include, but are not limited to, intravenous, intraperitoneal, intradermal, subcutaneous, intramuscular, intraocular, and intraportal). In one embodiment, the composition is suitable for intravenous administration. In one embodiment, the composition is suitable for subcutaneous administration. Pharmaceutical compositions may be suitable for topical administration (which includes, but is not limited to, epicutaneous, inhaled, intranasal or ocular administration) or enteral administration (which includes, but is not limited to, oral, vaginal, or rectal administration). The pharmaceutical composition may be included in a kit containing the antigen binding protein together with other medicaments, for example dolutegravir or cabotegravir, and/or with _{instructions for use. For convenience, the kit may comprise the reagents in predetermined amounts} with instructions for use. The kit may also include devices used for administration of the pharmaceutical composition. The terms “individual”, “subject” and “patient” are used herein interchangeably. In one embodiment the subject is a human. Treatment The antigen binding proteins described herein may be used in methods of treatment or prevention of HIV infection and AIDs. The antigen binding proteins described herein may be used in the manufacture of medicaments for the treatment or prevention of HIV infection and AIDs. The antigen binding proteins described may be used in an effective amount for therapeutic, prophylactic or preventative treatment. A therapeutically effective amount of the antigen binding protein described herein is an amount effective to ameliorate or reduce one or more symptoms of HIV infection. A prophylactically effective amount of the antigen binding protein described herein is an amount effective to prevent one or more symptoms of HIV infection. Combinations Antigen binding proteins of the present invention may be employed alone or in combination with other therapeutic agents, or a prodrug thereof. Combination therapies according to the present invention thus comprise the administration of an antigen binding protein and the administration of at least one other agent which may be useful in the treatment or prevention of HIV infection and/or AIDS. An antigen binding protein of the present invention and the other therapeutic agent may be formulated and administered together in a single pharmaceutical composition or may be formulated and administered separately. When formulated and administered separately, administration may occur simultaneously or sequentially in any order. Antigen binding proteins as described herein may be combined with, for example, one or more of an antiretroviral agent, an anti-infective agent, an immunomodulator, and other HIV entry inhibitors. Antiretroviral agents include Nucleoside Reverse Transcriptase Inhibitors (NRTIs), Non- Nucleoside Reverse Transcriptase Inhibitors (NNRTIs), Nucleoside Reverse Transcriptase _{Translocation Inhibitors (NRTTIs), Protease Inhibitors (PIs), Entry Inhibitors (EI), Integrase Strand} _{Transfer Inhibitors (INSTI), Maturation Inhibitors (MIs), and Capsid Inhibitors (CIs).} NRTIs may include, but are not limited to: abacavir, adefovir, adefovir dipivoxil, alovudine, amdoxovir, apricitabine, calanolide A, censavudine, didanosine, elvucitabine, emtricitabine, fozivudine, lamivudine, racivir, stampidine, stavudine, tenofovir disoproxil fumerate, tenofovir alafenamide, todoxil, zalcitabine, and zidovudine. NNRTIs may include, but are not limited to, HBY 097 (Hoechst/Bayer), capravirine, _{delaviridine, doravirine, efavirenz, etravirine, immunocal, lersivirine, loviride, nevirapine, oltipraz, and} rilpivirine. NRTTIs include, but are not limited to, islatravir. P_{Is may include, but are not limited to, amprenavir, atazanavir, brecanavir, cobicistat,} _{darunavir, fosamprenavir, indinavir, lasinavir, lopinavir, palinavir, nelfinavir, ritonavir, saquinavir, and} tipranavir. EIs are discussed in DRUGS OF THE FUTURE 1999, 24(12), 1355-1362; CELL, Vol. 9, 243- 246, Oct. 29, 1999; and DRUG DISCOVERY TODAY, Vol. 5, No. 5, May 2000, pp. 183-194; and _{Meanwell et al., Current Opinion in Drug Discovery & Development (2003), 6(4), 451-461. In} particular, the antigen binding proteins of the invention can be utilized in combination with attachment inhibitors, fusion inhibitors, and chemokine receptor antagonists aimed at either the CCR5 or CXCR4 coreceptor. HIV attachment inhibitors are also set forth in US 7,354,924 and uS _{7,745,625. EIs may include, but are not limited to, cenicriviroc, enfuvirtide, fostemsavir, ibalizumab,} leronlimab, maraviroc, vicriviroc and VIR-576. INSTIs may include, but are not limited to, bictegravir, cabotegravir, dolutegravir, elvitegravir, and raltegravir, . In an embodiment, the INSTI is dolutegravir or cabotegravir. In an embodiment, the INSTI is cabotegravir. Maturation inhibitors may include, but are not limited to, bevirimat, BMS-955176, GSK3640254, GSK3739937, PA-344 and PA-457. It will be understood that GSK3640254 is a compound as described in Dicker I, Jeffrey JL, Protack T, et al., Antimicrob Agents Chemother. 2022;66(1). GSK3739937, also known as VH3739937, is the compound of clinical trial NCT04493684. Capsid inhibitors may include, but are not limited to, GSK4004280, GSK4011499, and lencapavir. A_{nti-infective agents include, but are not limited to, clindamycin with primaquine,} _{daunorubicin, fluconazole, intraconazole, nystatin pastille, ornidyl eflornithine, megestrol acetate,} pentamidine isethionate, piritrexim, trimethoprim, trimetrexate, recombinant human erythropoietin, recombinant human growth hormone, spiramycin, testosterone and total enteral nutrition, Immunomodulators include, but are not limited to, acemannan, alpha-2-interferon, AS-101, bropirimine, CL246,738, FP-21399, gamma interferon, granulocyte macrophage colony stimulating factor, HIV core particle immunostimulant, interleukin-2, immune globulin, IMREG-1, IMREG-2, _{imuthiol diethyl dithio carbamate, methionine enkephalin, MTP-PE muramyl tripeptide, remune,} recombinant soluble human CD4, rCD4-IgG hybrids, SK&F106528, thymopentin, and tumour necrosis factor (TNF). The antigen binding proteins of the present invention may also be used in combination with agents that induce HIV expression, such as latency reversing agents. Several latency reversing agents include, but are not limited to, the following: histone deacetylase inhibitors (e.g66anobinostatt, panobinostat, romidepin), histone crotonyl transferase inhibitors (sodium _{corotonate), protein kinase C agonists (e.g., bryostatin, ingenol B), disulfiram, TLR7 agonists (e.g.,} _{GS-9620), and bromodomain inhibitors (e.g., JQ1, iBET151).} The antigen binding proteins of the present invention may also be used in combination with other agents that induce HIV expression, such as agents for clearance therapy. Several examples of agents for clearance therapy, or of immunological combinations for clearance, include, but are not limited to, the following: bNAbs, CD4-Ig, eCD4-Ig, and dual-affinity re-targeting (DART) proteins. Antigen binding proteins of the invention may be used in combination with broadly _{neutralizing HIV-1 antibodies, including 1NC9, 1B2530, 2F5, 2G12, 3NBC60, 3BNC117, 4E10,} _{8ANC131, 8ANC134, 10-1074, 10-1074LS, 10E8, 12A12, 12A21, b12, CAP206-CH12, CH01-04,} CH103-106, elipovimab (formerly known as GS-9722), HJ16, M66.6, N6LS (also known as VRC- HIVMAB091-00-AB and the compound of clinical trial NCT03538626), NIH45–46, PG9, PG16, PGT121-123, PGT125-131, PCT135-137, PGT141-145, PGT121.414.LS, PGT1512G12, QA013.2, VRC01-03, VRC-PG04, VRC-PG04b, VRC-CH30–34. Other agents that may be combined with antigen binding proteins of the invention include BIT225, GSK4000422/VH4000422, and S-648414 (the compound of clinical trial NCT04147715). The scope of combinations of compounds of this invention with HIV agents is not limited to those mentioned above, but includes in principle any combination with any pharmaceutical composition useful for the treatment and/or prevention of HIV infection and/or AIDS. Nucleic acid In some embodiments, a subject is administered DNA or RNA encoding an multimeric antigen _{binding protein of the invention to provide in vivo antibody production, for example using the cellular} machinery of the subject. Administration of nucleic acid constructs is known in the art and taught. for example, in U.S. Patent No. 5,643,578, U.S. Patent. No. 5,593,972 and U.S. Patent No. 5,817,637. U.S. Patent. No. 5,880,103 describes several methods of delivery of nucleic acids encoding proteins to an organism. One approach to administration of nucleic acids is direct administration with plasmid DNA. such as with a mammalian expression plasmid. The nucleotide sequence encoding the disclosed antigen _{binding protein can be placed under the control of a promoter to increase expression. The methods} _{include liposomal delivery of the nucleic acids. Such methods can be applied to the production of an} antigen binding protein of the invention. In some embodiments, a multimeric antigen binding protein of _{the invention is expressed in a subject using the pVRC8400 vector (described in Barouch er u/., J.} Virol., 79(14), 8828-8834, 2005). I_{n some embodiments, a subject (such as a human subject at risk of HIV infection) can be} _{administered an effective amount of an adeno-associated virus (AAV) viral vector that includes one or} _{more nucleic acid molecules encoding an multimeric antigen binding protein of the invention. The AAV} _{viral vector is designed for expression of the nucleic acid molecules encoding a disclosed antigen} _{binding protein, and administration of an effective amount of the AAV viral vector to the subject leads} _{to expression of an effective amount of the antigen binding protein in the subject. Non-limiting} _{examples of AAV viral vectors that can be used to express a disclosed antigen binding protein in a} _{subject include those provided in Johnson et al., Nut. Med., 15(8):901-906, 2009 and Gardner et al.,} Nature, 519(7541):87-91, 2015. The invention is illustrated by the following clauses: 1_{. A multimeric anti-HIV envelope spike complex-binding protein comprising:} _{i. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at least} one heavy chain or light chain, wherein the antibody binds to the V1/V2 loop of a g_{p120 protein or the gp120-gp41 interface of a gp120 and a gp41 protein; and} _{ii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached} directly or by a linker to the N-terminus or C-terminus of one of the heavy chains or l_{ight chains of the broadly neutralizing antibody.} _{2. The binding protein of clause 1, wherein the broadly neutralizing antibody binds to the} V1/V2 loop of a gp120 protein. _{3. The binding protein of clause 1, wherein the broadly neutralizing antibody binds to the} _{gp120-gp41 interface of a gp120 protein and a gp41 protein.} _{4. The binding protein of clause 1, wherein the broadly neutralizing antibody binds to at least} one complex N-glycan at the V1/V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41 protein. _{5. A multimeric anti-HIV envelope spike complex-binding protein comprising:} _{i. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at least} one heavy chain or light chain, wherein the antibody or fragment binds to at least o_{ne complex N-glycan on a gp120 or gp41 protein; and} _{ii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached} directly or by a linker to the N-terminus or C-terminus of one of the heavy chains or l_{ight chains of the broadly neutralizing antibody.} _{6. The binding protein of clause 5, wherein the broadly neutralizing antibody binds to at least} one complex N-glycan at the V1/V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 protein and a gp41 protein. _{7. The binding protein of any preceding clause, wherein the CD4 domain is attached via a} linker to the N-terminus or C-terminus of at least one heavy or light chain of the broadly neutralizing antibody. _{8. The binding protein of any preceding clause, wherein the CD4 domain is attached via a} linker to the N-terminus at least one heavy chain or light chain of the broadly neutralizing antibody. _{The binding protein of any preceding clause, wherein the CD4 domain is attached via a} linker to the N-terminus at least one heavy chain of the broadly neutralizing antibody. _{The binding protein of any preceding clause, wherein the binding protein comprises at least} four CD4 domains. _{The binding protein of clause 10, wherein the broadly neutralizing antibody has two heavy} chains and two light chains; and the C-terminus of a first CD4 domain is attached by a linker to the N-terminus of a first heavy chain, a second CD4 domain is attached by a linker to the N-terminus of a second heavy chain, a third CD4 domain is attached by a linker to the N- terminus of a first light chain, an a fourth CD4 domain is attached by a linker to the N- terminus of a second light chain. _{A multimeric anti-HIV envelope spike complex-binding protein comprising:} _{i. A broadly neutralizing anti-HIV envelope spike complex antibody or an antigen-} _{binding Fab’ or F(ab’)2 fragment thereof comprising at least one heavy chain variable} region or light chain variable region, wherein siad antibody fragment binds to the V1/V2 loop of a gp120 protein or the gp120-gp41 interface of a gp120 and a gp41 protein; and i_{i. at least one CD4 domain, wherein the C-terminus of the CD4 domain is attached} directly or by a linker to the N-terminus of the heavy chain variable region or light chain variable region. _{The binding protein of clause 12, wherein the fragment is an antigen-binding Fab’ fragment,} and wherein the CD4 domain is attached via a linker to the heavy chain variable region of the Fab’ fragment. _{The binding protein of clause 12, wherein the fragment is an antigen-binding Fab’ fragment,} and wherein the CD4 domain is attached via a linker to the light chain variable region of the Fab’ fragment. _{The binding protein of clause 12, comprising at least two CD4 domains, wherein the} _{fragment is an antigen-binding Fab’ fragment, wherein the first CD4 domain is attached via a} linker to the heavy chain variable region of the Fab’ fragment and the second CD4 domain is _{attached via a linker to the light chain variable region of the Fab’ fragment.} _{16. The binding protein of clause 12, comprising at least two CD4 domains, wherein the} _{fragment is an antigen-binding F(ab’)2 fragment, and wherein each of the CD4 domains is} attached via a linker to each of the heavy chain variable regions of the F(ab’)2 fragment. _{17. The binding protein of clause 12, comprising at least two CD4 domains, wherein the} _{fragment is an antigen-binding F(ab’)2 fragment, and wherein each of the CD4 domains is} attached via a linker to each of the light chain variable regions of the F(ab’)2 fragment. _{18. The binding protein of clause 12, comprising at least four CD4 domains, wherein the} _{fragment is an antigen-binding F(ab’)2 fragment, and wherein each of the CD4 domains is} attached via a linker to each of the heavy chain variable regions and each of the light chain variable regions of the F(ab’)2 fragment. _{19. The binding protein of clauses 12 to 18, wherein the C-terminus of the CD4 domains are} each attached via a linker to the N-terminus of the heavy chain variable region or light chain variable region of the Fab or F(ab’)2 fragment. _{20. A multimeric anti-HIV envelope spike complex-binding protein comprising:} _{i. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at least} _{one heavy chain or light chain, wherein the antibody comprises a VH domain and VL} _{domain pair according to SEQ ID NOs: 96 and 97, 250 and 251, or 261 and 262; and} _{ii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached} directly or by a linker to the N-terminus or C-terminus of one of the heavy chains or light chains of the broadly neutralizing antibody. _{21. The binding protein of any preceding clause, wherein the binding protein is a bispecific} binding protein. _{22. The binding protein of any preceding clause, wherein the linker is a peptide linker.} _{23. The binding protein of any preceding clause, wherein the peptide linker is between 5 and 30} amino acids in length. _{24. The binding protein of any preceding clause, wherein the linker is a multimer of the amino} _{acid sequence as set forth in SEQ ID NO: 30.} _{25. The binding protein of any preceding clause, wherein the linker is selected from one of SEQ} _{ID NOs: 30 to 35.} _{26. The binding protein of any preceding clause, wherein the CD4 domain is a human CD4 D1} domain or CD4 D1D2 domain. _{27. The binding protein of any preceding clause, wherein the CD4 domain comprises at least one} stabilizing mutation compared to a wild type CD4 domain. _{28. The binding protein of any preceding clause, wherein the CD4 domain comprises at least one} _{mutation selected from: L5Y, S23N, A55V, I79P, L96V and/or F98V.} _{29. The binding protein of any preceding clause, wherein the CD4 domain comprises L5Y, S23N,} _{A55V, I79P, L96V and F98V mutations; and at least one further mutation selected from:} E91Q, E91H, E87G, N52W, K8V, K8I, K8C, G99C, T11C, K72C, E13C, I70C, H27C, G38C, K_{21C, G65C, Q25E, H27D, R58V, R58N, R58Y, and/or L61M.} _{30. The binding protein of any preceding clause, wherein the CD4 domain comprises or consists} _{of any one of SEQ ID NO: 4 – 21.} _{31. The binding protein of any preceding clause, wherein the CD4 domain comprises or consists} _{of any one of SEQ ID NO: 5 – 21.} _{32. The binding protein of any preceding clause, wherein the CD4 domain comprises or consists} _{of any one of SEQ ID NO: 5 – 15.} _{33. The binding protein of any preceding clause, wherein the CD4 domain comprises or consists} of SEQ ID NO: 11. _{34. The binding protein of any preceding clause, wherein the CD4 domain has a Tm above about} 70℃. _{35. The binding protein of any preceding clause, wherein the CD4 domain has a Tm between} about 70℃ and 95℃. _{36. The binding protein of any preceding clause, wherein the CD4 domain has a Tm of about} 90℃. _{37. The binding protein of any preceding clause, wherein the broadly neutralizing antibody} comprises a mutation that increases the half-life of the binding protein compared to the same binding protein without said mutation. _{38. The binding protein of clause 37, wherein the binding protein comprises an Fc domain and} the half-life increasing mutation is a mutation in said Fc domain. _{39. The binding protein of clause 38, wherein the Fc domain comprises at least one of the} following sets of mutations (EU numbering): M428L and N434S (LS); L309D, Q311H and N434S (DHS); M252Y, S254T and T256E (YTE); and H433K and N434F (HN). _{40. The binding protein of clause 38, wherein the Fc domain comprises M428L and N434S (LS)} mutations (EU numbering). _{41. The binding protein of any preceding clause, wherein the broadly neutralizing antibody} comprises CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 as set out in any one row of Table 3. _{42. The binding protein of any preceding clause, wherein the broadly neutralizing antibody} _{comprises a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 according to:} _{i. SEQ ID NOs: 90 – 95, or} _{ii. SEQ ID NOs: 244 - 249, or} _{iii. SEQ ID NOs: 255 - 260.} _{43. The binding protein of any preceding clause, wherein the broadly neutralizing antibody} comprises a heavy chain variable domain and a light chain variable domain pair that is at least 95% identical to any of the variable domain pairs set out in any one row of Table 4. _{44. The binding protein of any preceding clause, wherein the broadly neutralizing antibody} _{comprises a heavy chain variable domain and a light chain variable domain pair that is at} _{least 95% identical to:} _{i. SEQ ID NOs: 96 and 97, or} _{ii. SEQ ID NOs: 250 and 251, or} _{iii. SEQ ID NOs: 261 and 261.} _{45. The binding protein of any preceding clause, wherein the broadly neutralizing antibody} comprises a heavy chain variable domain and a light chain variable domain pair that is at least 95% identical to any of the variable domain pairs set out in any one row of Table 4, and a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 according to the equivalent row in Table 3. _{46. The binding protein of any preceding clause, wherein the broadly neutralizing antibody} comprises: i_{. a heavy chain variable domain and a light chain variable domain pair that is at least} _{95% identical to SEQ ID NOs: 96 and 97 and a CDRH1, CDRH2, CDRH3, CDRL1,} _{CDRL2, CDRL3 according to SEQ IS NOs: 90-95, or} _{ii. a heavy chain variable domain and a light chain variable domain pair that is at least} _{95% identical to SEQ ID NOs: 250 and 251 and a CDRH1, CDRH2, CDRH3, CDRL1,} _{CDRL2, CDRL3 according to SEQ IS NOs: 244-249, or} _{iii. a heavy chain variable domain and a light chain variable domain pair that is at least} _{95% identical to SEQ ID NOs: 261 and 261 and a CDRH1, CDRH2, CDRH3, CDRL1,} _{CDRL2, CDRL3 according to SEQ IS NOs: 255-260.} _{47. The binding protein of any preceding clause, wherein the broadly neutralizing antibody} comprises a heavy chain variable domain and a light chain variable domain pair according to any of the variable domain pairs set out in any one row of Table 4. _{48. The binding protein of any preceding clause, wherein the broadly neutralizing antibody} _{comprises a heavy chain variable domain and a light chain variable domain pair according} to: i_{. SEQ ID NOs: 96 and 97, or} _{ii. SEQ ID NOs: 250 and 251, or} _{iii. SEQ ID NOs: 261 and 261.} _{The binding protein of any preceding clause, wherein the broadly neutralizing antibody} comprises a heavy chain and a light chain pair that is at least 95% identical to any of the chain pairs set out in any one row of Table 4. _{The binding protein of any preceding clause, wherein the broadly neutralizing antibody} _{comprises a heavy chain and a light chain pair that is at least 95% identical to:} _{i. SEQ ID NOs: 98 or 99, and 100, or} _{ii. SEQ ID NOs: 252 or 253, and 254, or} _{iii. SEQ ID NOs: 263 or 264, and 265.} _{The binding protein of any preceding clause, wherein the broadly neutralizing antibody} comprises a heavy chain and a light chain pair that is at least 95% identical to any of the _{chain pairs set out in any one row of Table 4, and a CDRH1, CDRH2, CDRH3, CDRL1,} CDRL2, CDRL3 according to the equivalent row in Table 3. _{The binding protein of any preceding clause, wherein the broadly neutralizing antibody:} _{i. a heavy chain and a light chain pair that is at least 95% identical to SEQ ID NOs: 98} _{or 99, and 100 and; a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3 according to} SEQ IS NOs: 90-95, or i_{i. a heavy chain and a light chain pair that is at least 95% identical to SEQ ID NOs:} _{252 or 253, and 254; and a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3} according to SEQ IS NOs: 244-249, or i_{ii. a heavy chain and a light chain pair that is at least 95% identical to SEQ ID NOs:} _{263 or 264, and 265; and a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDRL3} according to SEQ IS NOs: 255-260. _{The binding protein of any preceding clause, wherein the binding protein comprises or} _{consists of a sequence at least 95% identical to SEQ ID NO: 60 - 89.} _{The binding protein of any preceding clause wherein binding protein comprises or consists of} _{a sequence according to SEQ ID NO: 60-89.} _{55. The binding protein of any preceding clause, wherein the binding protein can reduce the} _{IC50 of at least one HIV envelope in a PSV assay compared to the IC50 reduction caused by} _{the broadly neutralizing antibody and CD4 domain alone or in combination.} _{56. The binding protein of any preceding clause, wherein the binding protein is linked to an} effector molecule or detectable marker, optionally wherein the detectable marker is a fluorescent, enzymatic or radioactive marker. _{57. A method of detecting an HIV infection in a human subject comprising contacting a} biological sample from the human subject with the binding protein according to any one of c_{lauses 1 to 56 under conditions sufficient to form an immune complex; and detecting the} presence of the immune complex in the sample, wherein the presence of the immune complex in the sample indicates that the subject has a HIV infection. _{58. A pharmaceutical composition comprising the binding protein as defined in any one of the} _{preceding clauses and a pharmaceutically acceptable excipient.} _{59. A method of treating or preventing an HIV infection in a human comprising administering to} the human an anti-HIV binding protein according to any one of clauses 1 to 56, or a pharmaceutical composition according to clause 58. _{60. The method of clause 59, whereby viral load in the human is decreased.} _{61. An anti-HIV binding protein according to any one of clauses 1 to 56, or a pharmaceutical} composition according to clause 58, for use in treating or preventing an HIV infection in a human. _{62. Use of an anti-HIV binding protein according to any one of clauses 1 to 56, or a} pharmaceutical composition according to clause 58, in the manufacture of a medicament for treating or preventing an HIV infection in a human. _{63. A kit comprising in separate containers: an anti-HIV binding protein according to any one of} _{clauses 1 to 56 and at least one anti-viral drug that inhibits cellular entry, replication, or} transcription of HIV in a human. _{64. The kit of clause 63, wherein the antiviral drug is selected from: Nucleoside Reverse} Transcriptase Inhibitors (NRTIs), Non-Nucleoside Reverse Transcriptase Inhibitors (NNRTIs), P_{rotease Inhibitors (PIs), Entry Inhibitors, Integrase Strand Transfer Inhibitors (INSTI),} _{Maturation Inhibitors (MIs), Capsid Inhibitors (CIs) and/or Nucleoside Reverse Transcriptase} Translocation Inhibitors (NRTTIs). 6_{5. The kit of clause 64, wherein the antiviral drug is an INSTI.} _{66. The kit of clause 65, wherein the INSTI is dolutegravir or cabotegravir.} _{67. A nucleic acid sequence that encodes an anti-HIV binding protein according to any one of} clauses 1 to 56. 6_{8. An expression vector that comprises the nucleic acid sequence of clause 67.} _{69. A recombinant host cell that comprises the nucleic acid sequence of clause 67 or the} expression vector of clause 68. 7_{0. A method of producing an anti-HIV binding protein, comprising culturing the host cell as} _{defined in clause 69 under conditions suitable for expression of said nucleic acid sequence or} vector, whereby an anti-HIV binding protein is produced. 7_{1. The anti-HIV binding protein produced by the method of clause 70.} EXAMPLES E_{xample 1 – Antigen Binding Protein Production} Plasmids encoding the antigen binding proteins of the invention were expressed in EXPI293 or FREESTYLE 293-F cells using the manufacturer’s standard protocol (ThermoFisher Scientific, Waltham, MA). The expressed medium was harvested by centrifugation (4000 rpm for 10 min) and the antigen binding proteins were purified by filtration through a 0.22 µm filter (Millipore Sigma, Burlington, MA) and fast protein liquid chromatography (FPLC) (ÄKTATM Pure, Cytiva, Marlborough MA). The medium was then passed through a Mabselect SuRe column (Cytiva, Marlborough MA) to capture the antigen binding proteins and the column was washed sequentially with phosphate- buffered saline (PBS) before elution. The antigen binding proteins were then exchanged into a final buffer by using dialysis, a desalting column and preparative size exclusion column (SEC). The purity of the antigen binding proteins was evaluated by using sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS- PAGE) and on a size exclusion column on a high-performance liquid chromatography system (SEC- HPLC). Antigen binding protein concentrations were determined by measuring absorbance at 280nm wavelength (A280) on a NanoDrop machine (ThermoFisher Scientific, Waltham, MA), and their _{molecular mass was measured by using liquid –hromatography - mass spectrometry (LC-MS) to} confirm their identity. The endotoxin level in the final purified products was measured on an ENDOSAFE system (Charles River Labs, Wilmington MA) to make sure it was sufficiently low (usually < 1 EU (Endotoxin Unit) / mg of protein) for downstream anti-viral studies. E_{xample 2 – Anti-Viral Activity Using Pseudotyped Virus Assay} The anti-viral activity of the antigen binding proteins was measured in a pseudotyped virus (PSV) assay. Pseudotyped HIV-1 virus (PSV) contains deletions in the genome that make it unable to produce infectious virions, but it can be used to measure the activity of cell entry inhibitors (i.e., molecules that prevent the binding of HIV-1 virions to the target cell membrane and/or prevent entry of HIV-1 into target cells), which include the antigen binding proteins of the invention. PSV was produced in HEK-293T cells (ATCC, Manassas VA) by co-transfecting expression plasmids encoding the HIV-1 gp160 envelope gene and an HIV-1 backbone plasmid using TRANSIT- 2020 transfection reagent (Mirus Bio, Madison WI). A panel of HIV-1 PSVs expressing different gp160 envelope trimers was generated to evaluate the effectiveness of the antigen binding proteins of the invention against a wide spectrum of HIV-1 strains. Meanwhile, to facilitate mechanistic studies of the antigen binding proteins, the complex N- glycans on selected HIV-1 envelopes were removed by adding Kifunensine during PSV production. Kifunensine inhibits mannosidase I, prevents processing of high mannose N-glycans into complex N- glycans in the cells and consequently produces high mannose glycoproteins. In brief, after 6 hours of transfection, Kifunensine was added to a final concentration of 100 µM, the cells were incubated for another 48 hours, and the supernatant which contains the PSV was harvested and aliquoted. i_{. ACTOne cells} The genome of PSV used in this assay contains a luciferase gene that is expressed once the virus enters cells. Accordingly, the luminescence signal (after adding a substrate of luciferase) can be used to determine the level of viral infection. The 50% tissue culture infectious dose (TCID) of a single thawed aliquot of each batch of PSV was determined in ACTOne cells. The ACTOne cell-line used in this assay was derived in-house from a genetically engineered 293T cell clone that expresses CD4, CXCR4, and CCR5. Cells were maintained in growth medium composed of Dulbecco’s modified Eagle’s medium (DMEM, Life Technologies) at 37 ⁰C in a humidified 5% CO2–95% air environment. Cell monolayers were split by treatment with Trypsin-EDTA (0.05%). To run the anti-viral assay, ACTOne cells were detached by treating the cell culture flask with trypsin (trypsinization) and resuspended in growth medium containing 2% of DMSO to a density of 2.5 x 10⁵ cells/ml. One hundred µl of such cells was added to 10 µl of antigen binding protein pre-loaded in a 96-well plate. Ninety µl of PSV was then added to each well. The assay plates were incubated at 37°C in a humidified incubator at 5% CO₂ level. Plates were developed after 72 hours of incubation by adding 50 µl of BRIGHTGLO luciferase reagent (Promega, Madison WI) to each well, and transferring the plates to an ENVISION multilabel plate reader (PerkinElmer, Waltham MA) to measure the luminescence and determine the level of virus that had infected the cells. The higher the luminescence signal, the higher the level of infection. Raw data were analyzed using an in-house template in an IDBS system to calculate half- maximal inhibitory concentration (IC50) values which reflects the activity of the antigen binding proteins of the invention at inhibiting viral entry (the smaller the number is, the more active the _{molecule is). Maximal percent inhibition values were calculated as MPI = 100 – (mean signals at the} 2 highest concentrations of compound/mean signal of 2 no-drug control wells) × 100 (PMID: 34780263). i_{i. TMZ.bl cells} Alternatively, the PSV assay was carried out using a luciferase-based assay in a TZM.bl cell line. The TZM-bl cell line is derived from a HeLa cell clone that was engineered to express CD4, CCR5 and CXCR4 and to contain integrated reporter genes for firefly luciferase and E. coli β-galactosidase under the control of an HIV-1 long terminal repeat (Wei et al., Antimicrobial agents and chemotherapy 46:1896–905(2002)) permitting sensitive and accurate measurements of infection. The detailed materials and methodology have been described elsewhere (Mentefiori, Curr. Protoc. Immunol., 2005, Chapter 12; Seaman et al., Journal of Virology, Feb. 2010, 84(3), p. 1439- 1452). In brief, the assay measures the reduction in luciferase reporter gene expression in TZM.bl cells following a single round of virus infection. Five-fold serial dilutions of the antigen binding proteins of the invention, from 50 µg/ml to 3.2 ng/ml, were performed in duplicate in 10% DMEM growth medium (100 µ/well). An amount of 200 TCID50 (50% tissue culture infectious dose) of virus was added to each well in a volume of µl, and the plates were incubated for 1 h at 37°C. TZM.bl cells were then added (1x10⁴/well in a 100-µl volume) in 10% D-MEM growth medium containing DEAE-dextran (Sigma, St. Louis, MO) at a final concentration of 11 µg/ml. Assay controls included TZM.bl cells alone (cell control) and TZM.bl cells with virus (virus control). Following a 48-hour incubation at 37°C, 150 µl of assay medium was removed from each well and 100 µl of BRIGHTGLO luciferase reagent (Promega, Madison, WI) was added. The cells were allowed to lyse for 2 min, and then 150 µl of the cell lysate was transferred to a 96-well black solid plate, and luminescence was measured using a Victor 3 luminometer (Perkin Elmer). The 50% and 80% inhibitory concentration (IC50 and IC80) values were calculated as the serum dilution that caused a 50% and 80% reduction respectively, in relative luminescence units (RLU) compared to the level in the virus control wells after subtraction of cell control RLU. All data were analyzed with 5-parameter curve fitting using neutralizing antibody analysis software provided _{by the CAVD Vaccine Immunology Statistical Center. Maximal percent inhibition values were} _{calculated as MPI = 100 – (mean signals at the 2 highest concentrations of compound/mean signal} of 2 no-drug control wells) × 100 (PMID: 34780263). E_{xample 3 – Anti-Viral Activity Using Pseudotyped Virus Assay} The anti-viral activity of the antigen binding proteins was also measured in a replicating virus assay against NL4-3 strain and its variants in MT2 cells. The proviral clone of NL4-3 (obtained from NIH) was used to make the replicating reporter virus NLRepRluc, in which a section of the nef gene from the proviral clone of NL4˗3 was replaced with the Renilla luciferase gene (Techniques in HIV Research. Tech HIV Res. Published online 1990. doi:10.1007/978-1-349-11888-5). Virus was produced through transfection of HEK293T cells using _{Lipofectamine Plus (Invitrogen, Carlsbad CA), according to the manufacturer's instructions. The} replication-competent virus was harvested 3 days after transfection of HEK 293T cells with the modified pNLRepRluc proviral clone and titrated in MT-2 cells using luciferase activity as a biomarker. The 10E8-insensitive strains are engineered based on this proviral clone NL4-3 by introducing point mutations into its envelope gene, including W680R/K683Q and W672L/F673L. MT-2 cells were obtained from the American Type Culture Collection (ATCC) and were propagated in RPMI 1640 medium supplemented with 10% heat-inactivated fetal bovine serum (FBS), 100 units/ml of penicillin G, 100 μg/ml of streptomycin, 10 mM HEPES buffer pH 7.55 and 2-mM L-glutamine. HEK293T cells were obtained from the ATCC and propagated in DMEM media supplemented with 10% heat-inactivated FBS. The NLRepRluc was used to infect MT-2 cells at a multiplicity of 0.01 for 1 hour before adding the proteins to the 96-well plates. The antigen binding proteins were serially diluted four-fold _{and 11 concentrations were plated in triplicate. After 4 days of incubation, cells were processed and} quantitated for virus growth by the amount of expressed luciferase. Luciferase was quantitated using the ENDUREN substrate from Promega (Madison, WI) according to the manufacturer’s instructions. Luciferase activity was measured immediately on an ENVISION multilabel plate reader (PerkinElmer, Waltham MA). EC50 values were calculated by comparing the amount of luciferase produced in the presence of antigen binding protein compared to wells where no antigen binding protein (DMSO control) was added. A 5-parameter sigmoidal equation was used to fit the resulting signal vs. concentration curves, and the concentration of each antigen binding protein that produced 50% maximal inhibition _{(EC50) was determined. Maximal percent inhibition values were calculated as MPI = 100 – (mean} signals at the 2 highest concentrations of compound/mean signal of 2 no-drug control wells) × 100 (PMID: 34780263). Those in the field will know that half maximal inhibitory concentration (IC50) is a measure of _{the potency of a substance in inhibiting a specific biological or biochemical function (in this case,} viral replication). IC50 is a quantitative measure that indicates how much of a substance (e.g. drug) _{is needed to inhibit, in vitro, a given biological process or biological component by 50%. Similarly,} _{IC80 or IC90 are the amount of the particular inhibitory substance needed to inhibit, in vitro, a given} _{biological process or biological component by 80% or 90% respectively.} _{Example 4 – Stability of soluble CD4 domains} All soluble human CD4 domains tested contain a set of “base” mutations in human CD4 domain 1 (D1) over the wild-type sequence (SEQ ID NO:3) that enable the folding of human CD4 D1 on its own. Soluble CD4 D1 with this set of mutations is known as mD1.22 (Chen et al., J Virol. 2014 Jan;88(2):1125-39) and the mutations therein consist of: L5Y, S23N, A55V, I76P, L96V, and F98V (SEQ ID NO:4, also referred to as D1m herein). To achieve better developability and pharmacokinetics, further mutations were introduced into mD1.22 (SEQ ID NO:4) to enhance its thermal stability. The additional stabilizing mutations were designed based on several methodologies: 1) computational simulation by using Free Energy Perturbation (FEP+, Schrodinger, New York, NY USA); 2) computational simulation by using disulfide-bond scan in Molecular Operating Environment program (MOE, Chemical Computing Group, Montreal Canada); and 3) panning a library of human CD4 D1 with each residue mutated, one by one, to the other 19 types of amino acids (site saturation mutagenesis, TWIST BioScience, San Francisco, CA USA) using phage display under thermally challenging conditions (i.e., incubating the phage at room temperature, 70 °C, and 80 °C, then selecting the CD4 domain variants that can still bind to recombinant HIV-1 gp120 (CN54 strain, Acro Biosystems, Beijing China)). The best performing variants (SEQ ID NOs: 5-21) were fused with 6xHis tag at their C- termini, expressed and purified from mammalian cells using methods as described in Example 1, except that purification was via a Ni-NTA resin (Cytiva, Marlborough MA) instead of Mabselect SuRe column, with standard protocol from the vendor. These purified CD4 D1 variants (with C-terminal 6xHis tag) were then evaluated to determine their melting temperature (Tm, using Prometheus System, NanoTemper, München Germany), which indicates thermal stability, as well as their anti-viral activity against HIV-1 pseudotyped virus (see Example 2 above for methods using ACTOne cells). A_{s shown in Table 6 below and in Figure 2, several CD4 D1 variants (SEQ ID NO:5-15)} showed dramatically improved thermal stability over the “baseline” or “control” CD4 D1 (D1m, SEQ 5 ID NO:4), while maintaining similar anti-viral activity. _{Table 6 – Melting temperature of soluble CD4 domains} _{CD4 Domain SEQ ID NO: Tm (℃)} _{D1m 4 68.2} _{D1m-E91Q 6 72.4} _{D1m-E91H 7 72.6} _{D1m-E87G 8 71.9} _{D1m-N52W 9 72} _{D1m-K8V 5 77.1} _{D1m-K8I 10 75.9} _{D1m-K8C-G99C 11 88.8} _{D1m-T11C-K72C 12 79.9} _{D1m-E13C-I70C 13 78.8} _{D1m-H27C-G38C 14 90.1} _{D1m-K21C-G65C 15 80.1} _{Example 5 – Antigen Binding Protein Format and Linker Length} _{The fusion position of the CD4 domain in the broadly neutralizing mAbs (e.g., whether to fuse the} CD4 domain to the light chain or heavy chain or both, whether to fuse the CD4 domain to the N- terminus or C-terminus of these chains, or whether to fuse the CD4 domain in the middle of the heavy chain (in between CH1 and CH2 domains)) was tested in some examples V3-bNAbs (another class of bNAbs that bind to a distinct target called the V3 loop). We observed that the most potent bispecific molecule resulted from fusing CD4 D1 to the N- _{terminus of the heavy chain of V3-bNAb1 (molecule 1 in Table 7, which neutralized 6 envelopes with} IC50 < 160 pM and 1 envelope with IC50 about 3 nM in PSV assay). In this bispecific format, the _{linker length between the CD4 domain and V3-bNAb1 heavy chain N-terminus does not particularly} _{affect anti-viral activity (Figure 3A) but changes the pharmacokinetics (PK) of the resultant bispecific} molecules dramatically (Figure 3B). A_{s shown in Figure 3B, the shorter-linker bispecific (D1m_1xG4S_bNAb1, SEQ ID NOs: 36} and 23) showed much better PK (longer half-life and lower clearance rate) than the longer-linker _{bispecific (D1m_4xG4S_bNAb1, SEQ ID NOs: 37 and 23)) in a humanized mouse model (Tg32} strain where human neonatal Fc receptor (hFcRn) replaced the corresponding mouse gene (mFcRn), The Jackson Laboratory, Bar Harbor, Maine USA).

* 6 5 4 3 2 1 ^l _{u = = = = = =} CA X E a T p Z ^s _b M 2 T N C 4 n ^s _s ab _a N _b N _b N _{D D D} 0 ₆ A A A 1m 1m 1m ^. P G4 1 0 2 8 7 ^L C1 23 ^v _a _e ^{y l} _e 35 ^x _H b1 b1 b1 _ ^{- - .} 0 2 6 8 8 ₄ .^{. .} ₅ -₃ ^/ ₈ 6 ^l _{o (A 7} ^is _t -_L - 1 _{K 9 C} 0 5 8 p C ^: 8 _K 8 ^. ₀ 9 e T _IC _a C _H -_m C ^x _G C C O 5g _1 _ ⁱ _d 4S -_G -_G ne 0 ⁽ 1 _ ^s _ix ^x _G ^x _G 1 _ 9 9 3 0 0 x_G b 9 9 N C C ^. ₀ ^. ₀ ^. ₀ 0 0 .₁ ^. 0 0 ^. 0 0 ^. ₁ 1 c_e ⁽ _nM _C 4 - S 4 4 _ _ 8 4 6 6 3 4 ^lls ⁾ ^t _ S e_r D _ S A 1 1 ₎ _ b ^{x x} _o _m 1 D D 1 _{G G} ^f m 1 -_B 4 4 _d _n ⁱ m 1 a -^l _K _h 8 - m o S S ⁱ K -_K ^t _h _ C b _ ^f _f b 2 0 0 0 0 0 0 _e ^is C 8 N N ^r _t C 8 h A A ^. ₆8 ^. ₁8 ^. ₈ ^. ₁ ^. ₁ ^. ₀ ^. ₉ 2 _en_id -_G -_G C a b b 6 2 7 5 1 ^t _n ^{- i} ⁱ 9 9 _{G n} 1 1 e 9C 9 9 ^{s -} _V 3 ^r _e C 9 ₍ ^s _id ⁽ _S ^L _C ⁽ _S E -_b _{S (} C E _S EQ (_S Q N 2 0 0 1 ue Q E ⁽ _S Q E E ^I Q I_D Q _D ^. 0 0 1 A 5 ^. ₃ ^. ₇ ^. ₂ ^. ₁ ^. ₄ ^. ₄ 3 b N 3 8 2 9 7 9 9 1^s ₎ ^I _D ^I _{D N} ^I _D -_d _N ^I _D O O e O _N s O _N ^s _N _: ^s _: ^r :₂ ^s O ₃ O 4 ⁱ _ve :₄ ^s _: 6 ^s + :₂ 4+ 13 0 1 0 0 0 4 d 2+ 0 ₃ 9 3 2 2 ^. ₈ ^. ₀ 3 .₂ ^. ₀ ^. ₁ ^. ₀ ^. ₉ 4 _b 4 + + 8 + 3) 9 4 8 4 0 1 0 ^is 1 2 2 ) 4 _p 2 e ) 3) 3) 6) ^cific 2 . 0 1 0 0 0 1 _fo ₁ 5 b 3 ^. ₀3 ^. ₅0 ^. ₀2 ^. ₁4 ^. ₀1 ^. ₂4 N ^r _m A a b1 ^ts 1 1 9 _a 1 0 8 7 = -_D n =_{= = =} 2 6 1 e d b N _{D D D D} 1 1m 1m 1 0 0 m ^. ₄ ^. ₀ 7 0 0 0 4 5 ^. ₆ ^. ₀ ^. ₅ ^. ₀ 5 ^r 8 6 2 3 ^. ₇ 6 ⁱ _ve ^c _o d n A m b _ 1 -_K H -_K _ 3 ^t H _M ^r _o (_S 8C ^is 8C ^is o ^l ^l _{e m} EQ - ₍ _{G S} -_{G (} 9 _S 1 1 ^c _u o l_e I 9 E D 9 Q 9 E C I C Q 02 0 .₀ 8 0 0 0 5 .^. ₁ ^. ₄ ^. ₀ ^. ₆ 7 ^l _e ^c _u _N _ _D _ I ^. ₁ 7 ₂ 3 5 4 0 s F _D 6 5 ^l _e O F s_: ^c _N ^c _{( N} ^s _a _{2 (} O S 2 E ^: _S O g 4 E ^: ₄ a + Q * Q ) * 20 0 5 0 0 0 1 _n ⁱ 2 I ^{) .} 3 ^I _{D D +} ^. _{4 0}9 ^. ₂5 ^. ₁1 ^. ₂2 ^. ₀7 ^. ₄ 8 ^s 4 ^t _a ) _{N N} O _b 1 N _p O :₅ ^: ₅ A a b ne 3 3 ) ⁾ 1 + ⁽ _S 1 2 1 3 0 7 ^l _o _b E 3 Q 1 6 . 7 0 ^. ₄ ^. 4 9 ^. ₃ ^. ₀ ^. ₃ 9 ^f _H N ^. ₄ 2 9 9 1 2 2 A b ^I _D 3 ^I _V 1 _N -₁ ( _e _S O n E ^s Q :₂ 2 2 0 15 9 1 0 1 1 1 ^v _e I_D + ^. ₄ ^. ₁ ^. ₂ ^. ₄ ^. ₃ ^. ₉ ^. ₅ 0 ^l _o _N 2 8 4 0 3 1 8 8 p 3 e O ^{) s} ^{s (} _{c in} _{:2 o} m 4 1 _a 2 > + b 5 0 02 0 31 0 > 5 1 _PS 2 o) 0 ^. ₀ ^. ₃ ^. ₁ ^{. .} ₀ 0 1 V 3 0 7 5 7 ₂ 3 0 ) 0 (_co m bo) H H C * C H A H ^I A Z X2 T C E C ^I _V TM^I _V _V -₂ 0 . P M 2 N 4 n G4 1 08 7 ^L C1 2 ^v _e H T no ^{- - -} 5 0 8 8 ₄ ^/ 36 ^l _o ^I a^t ₀1 ₂ 8 - 8₂- -_A 3 ^. ₂ 6 .₉ ^. _C ^. ₅0 -_{3 8}5 8 p _V - b _te ^I _D ^. ₀ 9 e ₁ ^l _e ^s _te 3 1 1 0 0 0 0 _en ₈d 5 . 4 0 0 1 9 ^. ₃ 1 ^{v :} 4 4 ^. ₁ ^. ₁ 6 0 ^. ₀5 ^. ₀6 ^. ₁6 ^. ₄4 ^. ₆4 ^. ₇9 _e l _I _{o C} p 5 e 0 17 1 1 .₄ ^. 0 0 0 0 0 ₍ ₂ 9 2 ^. ₁ ^. ₁0 ^. ₀ ^. ₀ ^. ₁ ^. 0 2 ^. 0 4 ^. ₇ 2 ^s V _{in n} M 7 3 2 5 0 6 6 5 3 _P ⁾ 2 -_b S _o 4 2 2 .₃ ^. ₂ 0 0 . 0 0 0 0 0 1 N V 1 ^. ₀ ^. ₀ ^. ₀ ^. ₄ ^. ₃ ^. 3 A _a ^f _d 6 8 ^. ₂8 1 2 5 9 2 3 ₂4 b2 ^ss ⁱ a ^f _fe > 1 1 2 -_D ^r _e 5 2 0 ^. ₀ 36 2 . 0 0 0 8 4 ^. ₀ ^. ₀ ^. ₄ ^. ₄ 07 69 4 e ^y _(A n 0 6 ^. ₈ ^t 8 9 4 7 8 4 ^. ₄6 ^. ₂ ^r 0 ⁱ _ve C _V 3 > 7 > 1 d TO -_b 5 0 0 5 2 0 . 0 . 0 0 9 4 _M n N 0 ^. ₅8 00 ^. _{5 0 0} ^. ₃ ^. ₈ ^. ₄ ^. ₅ 5 o e A 1 1 2 0 0 4 9 ^l _e b c_u ^c _e 3 0 0 0 0 1 2 * * * ^. ₆ ^. ₀ ^. ₀ ^. ₁ ^. ₂ ^. ₉ ^. 6 ^l _e ^l 2 s^l s ₎ ^-, _V 3 3 2 9 4 2 8 ₀3 -_bN > > > 3 1 A 50 5 5 6 0 0 0 5 > > b 0 00 00 ^. ₅ ^. ₀ ^. ₀ ^. ₄ 0 5 5 7 3 3 3 9 3 ^. ₃ 0 2 0 00 - _an 1 0 0 0 0 0 0 d * * * ^. ₆ ^. _V 3 ^. 6 ^. 2 ^. 8 ^. 9 ^. 8 9 _{0 0 0 0 2 3}7 V 3 3 - 0 0 0 0 0 - _bN 0 0 _b A * * * ^. ₂ ^. ₀ ^. ₀ ^. ₀ ^. ₀7 ^. 7 ^. 9 N A b 5 3 3 3 _{0 1}7 b 4 3 -^- _d e 9 0 0 0 0 4 5 _D e ^r * * * 6 .₇ ^. ₀ ^{. . . . .} 1 ⁱ _ve 5 1 ₀5 ₀2 ₁1 ₀7 ₀1 0 ^ri _ve d d _b 6 0 0 0 0 1 _M ^is _p * * * 1 .₈ ^. 2 0 1 3 ^. ₀3 ^. ₀2 ^. ₀6 ^. ₁5 ^. ₁ 1 o e 2 1 ^l _e ^c ^c _u ^if _c ⁱ > 0 0 3 > ^l _{e fo} * * * 50 ^. 0 0 0 ^. ₀ ^. ₀ ^. ₁ 8 .₃ 5 1 s 0 2 ^r _m 0 3 3 1 5 3 0 a t 1 ^s 0 0 0 0 0 0 V _a * * * 3 .₁ ^. ₀ ^. ₀ ^. ₁ ^. ₁ ^. ₁ ^. ₅ 1 3 n 3 d 8 3 3 3 9 0 0 -_b N A ^c _o 4 n 6 0 0 0 0 1 8 b ^t * * * 9 .₁ ^. ₀2 ^. ₀1 ^. ₂3 ^. ₈6 ^. ₃9 ^. ₇ 1 4 _r 4 -_{D o} l 6 8 e _m rⁱ _v o 4 0 0 0 0 _e ^l _e * * * 2 0 3 .₉ ^. ₀ ^. ₀ ^. ₄ ^. ₄ ^. ₇ ^. ₄ 15 d ^c _u 8 3 4 1 8 7 2 _M o ^l _e > 0 0 0 3 2 > ^l _e ^s _ag * * * 5 2 0 ^. ₀ ^. ₀ ^. ₄ 7 ^. ₃ 5 1 ^c 0 3 2 7 ^. ₆ 0 6 _u 1 6 0 ^l _e a s _n ⁱ ^s > 3 1 4 ^t _a 5 8 0 0 61 21 15 1 9 7 C _p 00 ^. ₉ 3 3 9 ^. ₅ ^. ₃ ^. ₀ ^. ₅ ^. ₁ ^. ₂4 ^. ₈3 ^. ₄ 1 3 7 D 4 an 4 9 8 4 0 _C e 2 o ^l 2 6 1 1 n _o 28 2 4 0 8 1 3 0 2 2 1 ^tr _o ^f ^. ₉ ^. ₇ ^. ₃ ^{. . . .} ₅ ^. ₄ ^. ₂ ^. ₇ 8 0 2 5 ₄8 ₀4 ₄7 2 4 4 7 _s ^l _{Table 8 Molecule Key:} _{1 = D1m-K8C-G99C_2xG4S_bNAb2 (SEQ ID NOs:46+25)} _{2 = D1m-K8C-G99C_3xG4S_bNAb2 (SEQ ID NOs:47+25)} _{3 = D1m-K8C-G99C_4xG4S_bNAb2 (SEQ ID NOs:48+25)} 4 = bNAb2-LC_1xG4S_D1m-K8C-G99C (SEQ ID NOs:24+49) _{5 = bNAb2 (SEQ ID NOs:24+25) + D1m_His (SEQ ID NO:4*) (combo)} _{6 = bNAb2 (SEQ ID NOs:24+25) + D1m-K8C-G99C_Fc (SEQ ID NO:53) (combo)} _{7 = bNAb2 (SEQ ID NOs:24+25)} _{8 = D1m-K8C-G99C_1xG4S_bNAb3 (SEQ ID NOs:50+27)} _{9 = D1m-K8C-G99C_4xG4S_bNAb3 (SEQ ID NOs:51+27)} _{10 = bNAb3 (SEQ ID NOs:26+27) + D1m_His (SEQ ID NO:4*) (combo)} _{11 = bNAb3 (SEQ ID NOs:26+27) + D1m-K8C-G99C_Fc (SEQ ID NO:53) (combo)} _{12 = bNAb3 (SEQ ID NOs:26+27)} _{13 = D1m-K8C-G99C_4xG4S_bNAb4 (SEQ ID NOs:52+29)} _{14 = bNAb4 (SEQ ID NOs:28+29) + D1m_His (SEQ ID NO:4*) (combo)} _{15 = bNAb4 (SEQ ID NOs:28+29) + D1m-K8C-G99C_Fc (SEQ ID NO:53) (combo)} _{16 = bNAb4 (SEQ ID NOs:28+29)} 17 = D1m_His (SEQ ID NO:4*) 18 = D1m-K8C-G99C_Fc (SEQ ID NO:53) * plus a 6xHis tag (six C-terminal histidine residues) T_{hermal stabilization of CD4 D1 (see Example 3 above) further enhanced the PK of the} _{bispecific molecules (D1m-K8C-G99C_1xG4S_bNAb1, SEQ ID NOs:44 and 23; D1m-T11C-} _{K72C_1xG4S_bNAb1, SEQ ID NOs:45 and 23; D1m-K8I_1xG4S_bNAb1, SEQ ID NOs:42 and 23; and} _{D1m-K8V_1xG4S_bNAb1, SEQ ID NOs:43 and 23) as shown in Table 9 below.} _{Table 9: The effect of (1) linker length between the CD4 domain and V3-bNAb1 heavy chain, and} _{(2) thermal stability of CD4 D1, on the PK of bispecific molecules in hFcRn mice (Tg32)} Molecule Tm of CD4 D1 Half-life Clearance (ml/day/kg) (SEQ ID NOs) (ºC) (days) b_{NAb1 (22+23) - 5.8 21.6} _{D1m_4xG4S_bNAb1 (37+23) 68.2 2.2 144} _{D1m_1xG4S_bNAb1 (36+23) 68.2 4.1 31.7} _{D1m-K8C-G99C_1xG4S_bNAb1 (44+23) 88.8 10.2 7.4} _{D1m-T11C-K72C_1xG4S_bNAb1 (45+23) 79.9 8.9 12.9} _{D1m-K8I_1xG4S_bNAb1 (42+23) 75.9 9.3 12} _{D1m-K8V_1xG4S_bNAb1 (43+23) 77.1 7.3 12.8} _{Accordingly, the best molecules for further development contain shorter linker lengths} _{between the CD4 domain and bNAb (1xG4S) and contain a thermally stable CD4 domain(s).} _{Example 6 – Bispecifics based on V1/V2 Apex Binders} To generate “CD4-apex” bispecifics, CD4 domain 1 was fused to broadly neutralizing antibodies (bNAbs) that target the V1/V2 loop apex region of the HIV-1 envelope protein gp120 (part of the _{gp160 trimer/envelope spike complex). This resulted in the production of bispecific molecules} _{comprising sequences according to SEQ ID NOs: 74-89 and associated light chains (see description} _{of Figures 4 to 19 above). These bispecifics were tested against a panel of HIV-1 envelopes in PSV} assay, along with control molecules including CD4 domain 1 alone, bNAbs alone, and their mixtures (combo). Several such bispecifics showed much higher anti-viral activity than the control molecules, indicating strong anti-viral synergy between the CD4 domain and the fused bNAb. This is particularly surprising since the binding of these V1/V2 apex bNAbs relies on a closed conformation of the gp160 _{trimer (Gorman et al., Cell Rep. 2020 Apr 7;31(1):107488.) while CD4 induces the opening of the} _{gp160 trimer/envelope spike complex (Dam et al., Nature. 2024 Feb;626(7998):E7.). Furthermore, it} has been shown that soluble CD4 abolishes the anti-viral activity of V1/V2 apex bNAbs when mixed together (Ivan et al., PLoS Biol. 2019 Jan 16;17(1):e3000114.). In contrary, our experiments demonstrated that the covalent fusion of CD4 domain to one of a range of V1/V2 apex bNAbs can _{boost their anti-viral potency and spectrum (Figures 4 to 19). Most strikingly, the resulting} bispecifics potently neutralized the HIV-1 envelopes that are insensitive to the parental bNAb, CD4 domain or their mixture, indicating a strong functional synergy between the CD4 domain and the bNAb it is attached to (Table 10). Table 10: Anti-viral activity of bNAb1-derived bispecifics and control molecules against “double- insensitive” HIV-1 envelopes in PSV assay (ACTOne cells) _{Envelope Bispecific1-1 Bispecific1-2 bNAb1 CD4 Combo} _{3637_V5_C3 IC50 1.2 3.8 >500 >500 >500} _{3468_V1_C12} nM _{0.16 4.4 >500 >500 >500} _{3637_V5_C3 IC90 44.9 33 >500 >500 >500} _{3468_V1_C12} nM _{24.3 135 >500 >500 >500} _{3637_V5_C3 MPI 99 100 18 32 43} _{3468_V1_C12} (%) _{99 99 19 43 53} Without being bound by theory, we believe this synergy might be a combined outcome from 1) the CD4 domain and the linked bNAb bind to a same gp160 envelope trimer; 2) CD4-induced conformational change of the HIV envelope spike protein complex, which exposes new epitopes for the bNAb, which overcomes the low susceptibility of insensitive envelopes; 3) the bNAb is sequestered at a high local concentration near the CD4 domain, providing advantage of binding kinetics, and 4) the combination of N-glycan binding coupled with CD4 domain anchoring to such N- _{glycans . Indeed, we observed in the case of CD4-bNAb1 and CD4-bNAb2 fusions, the synergy is} particularly obvious when the CD4 domain is attached to the N-terminus of the bNAb1 heavy or light _{chain (“bispecific 1-1” comprising a heavy chain (including a linked CD4 domain) of SEQ ID NO: 74} _{and a light chain of SEQ ID NO: 254 and “bispecific 1-2” comprising a heavy chain of SEQ ID NO:} 253 and a light chain (including a linked CD4 domain) of SEQ ID NO: 420; Figure 4), or the N- terminus of the bNAb2 heavy chain (“bispecific 2-1” comprising a heavy chain of SEQ ID NO: 75 (including a linked CD4 domain) and a light chain of SEQ ID NO: 265; Figure 5). Based on structural modeling, these N-terminal fusions can accommodate the co-binding of the CD4 domain and the linked bNAb to a same gp160 trimer/envelope spike complex. W_{e also tested one such bispecific (Apex bispecific1, (also known as “bispecific 1-1” – SEQ} _{ID NO: 74 (HC) and 254 (LC))) and its parental bNAb (Apex bNAb1 – SEQ ID NO: 253 (HC) and 254} _{(LC)) against pseudotyped viruses treated with Kifunensine, which removes complex glycans on the} envelopes and shall reduce their susceptibility to Apex-bNAb1. The result demonstrated that the _{anti-viral synergy of the bispecific can be driven by the presence of complex glycans.} As shown in Table 11, if an envelope is sensitive to Apex-bNAb1, treatment with Kifunensine greatly decreases its susceptibility to Apex-bNAb1 as well as the bispecific. If an envelope is resistant to Apex-bNAb1 (IC50 >500 nM) and shows synergy against the bispecific (lower IC50 against the bispecific than against CD4 and combo of CD4 with bNAb17), Kifunensine treatment destroys the synergy and gives an IC50 similar to that of the CD4 (treatment with Kifunensine can also alter the susceptibility to CD4 probably through changing the glycosylation pattern near the _{CD4 binding site (Liang et al., J Virol. 2016 Sep 29;90(20):9224-36.)). This proves that binding to} _{complex glycans is important for the synergy observed within the bispecific.} _{Table 11: Anti-viral activity of Apex- bNAb1-derived bispecific and control molecules against} _{Kifunensine-treated HIV-1 envelopes in PSV assay (ACTOne cells)} Envelope _{Untreated Kifunensine treated} _{IC50 nM IC90 nM IC50 nM IC90 nM} _{Bispecific1 0.008 0.1 0.1 2.1} 3326V4C3 _{Apex-bNAb1 <0.002 0.0 0.02 1.1} _{CD4 1000.3 5333.9 977.6 4872.7} _{Combo 0.0 0.1 0.0 1.1} _{Bispecific1 12.6 149.5 214.3 >500} _{Apex-bNAb1 >500 >500 >500 >500} 3637-V5-C3 _{CD4 521.7 2245.6 940.5 5374.0} _{Combo >500 >500 >500 >500} _{Example 7 – Bispecifics based on interface binders} To generate “CD4-interface” bispecifics, CD4 domain 1 was fused to broadly neutralizing antibodies _{(bNAbs) that target the gp41-gp120 interface region of the HIV-1 envelope proteins gp120 and} _{gp41 (part of the gp160 trimer/envelope spike complex). This resulted in the production of bispecific} _{molecules comprising sequences according to SEQ ID NOs: 60-73 and associated light chains (see} _{description of Figures 20 to 33 above). These bispecifics were tested against a panel of HIV-1} envelopes in PSV assay, along with control molecules including CD4 domain 1 alone, bNAbs alone, and their mixtures (combo). Several such bispecifics showed much higher anti-viral activity than the control molecules, indicating strong anti-viral synergy between the CD4 domain and the fused _{bNAbs (Figures 20 to 33).} _{These “synergistic” bispecifics contain a lineage of bNAbs that binds to complex tri- and} tetra-antennary glycans in a conserved epitope on gp41 and distinguish cleaved from uncleaved envelope trimers (Falkowska et al., Immunity. 2014 May 15;40(5):657-68.). Therefore, we also _{tested one such bispecific (bispecific17 – comprising a heavy chain (including a linked CD4 domain)} _{according to SEQ ID NO: 60 and a light chain according to SEQ ID NO: 100) and its parental bNAb} _{(bNAb17, comrpising CDRs: 90-95, VH/VL: SEQ ID NOs: 97 and 97, HC/LC: 99 and 100) against} pseudotyped viruses treated with Kifunensine, which removes complex glycans on the envelopes and shall reduce their susceptibility to bNAb17. The result demonstrated that the anti-viral synergy of the bispecific relies on the presence of complex glycans. As shown in Table 12, if an envelope is sensitive to bNAb17, treatment with Kifunensine greatly decreases its susceptibility to bNAb17 as well as the bispecific. If an envelope is resistant to bNAb17 (IC50 >500 nM) and shows synergy against the bispecific (lower IC50 against the bispecific than against CD4 and combo of CD4 with bNAb17), Kifunensine treatment destroys the synergy and gives an IC50 similar to that of the CD4 (treatment with Kifunensine can also alter the susceptibility _{to CD4 probably through changing the glycosylation pattern near the CD4 binding site (Liang et al.,} _{J Virol. 2016 Sep 29;90(20):9224-36.)). This proves that binding to complex glycans is necessary for} the synergy observed within the bispecific. Without being bound by theory, we believe this synergy might be a combined outcome from 1) the CD4 domain and the linked bNAb bind to a same gp160 envelope trimer; 2) CD4-induced conformational change of the HIV envelope spike protein complex, which exposes new epitopes for the bNAb, which overcomes the low susceptibility of insensitive envelopes; 3) the bNAb is sequestered at a high local concentration near the CD4 domain, providing advantage of binding kinetics, and 4) the combination of N-glycan binding coupled with CD4 domain anchoring to such N- glycans _{Table 12: Anti-viral activity of bNAb17-derived bispecific and control molecules against Kifunensine-} treated HIV-1 envelopes in PSV assay (ACTOne cells) U_{ntreated Kifunensine treated} Envelope _{IC50 nM IC90 nM IC50 nM IC90 nM} _{Bispecific17 0.04 0.5 6.3 268.1} _{bNAb17 0.03 0.6 82.2 >500} MP11.38 _{CD4 19.5 377.2 8.5 428.3} _{Combo 0.02 0.3 3 459.4} _{Bispecific17 0.03 0.6 5.8 >500} 398F1 _{bNAb17 0.1 1.4 >500 >500} _{CD4 6.2 >500 29.2 >500} _{Combo 0 0.5 17 >500} _{Bispecific17 2.5 70.3 8.5 194.2} _{bNAb17 25.5 >500 >500 >500} 93UG065 _{CD4 82.3 >500 6.2 >428} _{Combo 5.6 >500 29.7 >500} _{Bispecific17 0.5 34.8 187.8 >500} 0260.v5.c36 _{bNAb17 >500 >500 >500 >500} _{CD4 328.8 >500 332.5 >500} _{Combo 28.5 >500 404.8 >500} _{Bispecific17 0.7 45.2 195.1 >500} MP35.2 _{bNAb17 >500 >500 >500 >500} _{CD4 50.1 276 423 >500} _{Combo 93.7 >500 439 >500} _{Bispecific17 1.6 19.2 85.1 >500} TRO11 _{bNAb17 >500 >500 >500 >500} _{CD4 196.1 >500 98.6 >500} _{Combo >500 >500 56.9 >500} _{Bispecific17 1.7 313.6 29.1 >500} _{bNAb17 >500 >500 >500 >500} CNE8 _{CD4 65.7 >500 90.1 >500} _{Combo >500 >500 104.1 >500} SEQUENCE LISTING SEQ _{Name/Identifier Description} ID NO 1_{D1D2 Human CD4 D1D2 (wild type)} _{2 D1mD2 Human CD4 mD1.22-D2 (D1 mutations S23N, A55V, and} L96V) 3_{D1 Human CD4 D1 (wild type)} _{4 D1m Human CD4 mD1.22 (NCBI accession code:} QHY83614.1; D1 mutations L5Y, S23N, A55V, I76P, L96V and F98V) 5_{D1m-K8V Human CD4 mD1.22 + K8V} _{6 D1m-E91Q Human CD4 mD1.22 + E91Q} _{7 D1m-E91H Human CD4 mD1.22 + E91H} _{8 D1m-E87G Human CD4 mD1.22 + E87G} _{9 D1m-N52W Human CD4 mD1.22 + N52W} _{10 D1m-K8I Human CD4 mD1.22 + K8I} _{11 D1m-K8C-G99C Human CD4 mD1.22 + K8C, G99C} _{12 D1m-T11C-K72C Human CD4 mD1.22 + T11C, K72C} _{13 D1m-E13C-I70C Human CD4 mD1.22 + E13C, I70C} _{14 D1m-H27C-G38C Human CD4 mD1.22 + H27C, G38C} _{15 D1m-K21C-G65C Human CD4 mD1.22 + K21C, G65C} _{16 D1m-Q25E Human CD4 mD1.22 + Q25E} _{17 D1m-H27D Human CD4 mD1.22 + H27D} _{18 D1m-R58V Human CD4 mD1.22 + R58V} _{19 D1m-R58N Human CD4 mD1.22 + R58N} _{20 D1m-R58T Human CD4 mD1.22 + R58T} _{21 D1m-L61M Human CD4 mD1.22 + L61M} _{22 V3-bNAb1 HC+LS Full heavy chain of model V3-bNAb1 with M428L/N434S} mutations 2_{3 V3-bNAb1 LC Full light chain of model V3-bNAb1} _{24 V3-bNAb2 HC+LS Full heavy chain of model V3-bNAb2 with M428L/N434S} mutations 2_{5 V3-bNAb2 LC Full light chain of model V3-bNAb2} _{26 V3-bNAb3 HC+LS Full heavy chain of model V3-bNAb3 with M428L/N434S} mutations 2_{7 V3-bNAb3 LC Full light chain of model V3-bNAb3} _{V3-bNAb4 HC+LS Full heavy chain of model V3-bNAb4 with M428L/N434S} mutations _{V3-bNAb4 LC Full light chain of model V3-bNAb4} _{1xG4S Linker} _{2xG4S Linker} _{3xG4S Linker} _{4xG4S Linker} _{5xG4S Linker} _{6xG4S Linker} _{D1m_1xG4S_bNAb1-HC Human CD4 mD1.22 fused to the N-terminus of model} _{V3-bNAb1 heavy chain with 1xG4S linker, Fc includes} M428L/N434S _{D1m_4xG4S_bNAb1-HC Human CD4 mD1.22 fused to the N-terminus of model} _{V3-bNAb1 heavy chain with 4xG4S linker, Fc includes} M428L/N434S _{D1m_1xG4S_bNAb1-LC Human CD4 mD1.22 fused to the N-terminus of model} _{V3-bNAb1 light chain with 1xG4S linker} _{bNAb1-HC-mid_1xG4S_D1m-} Human CD4 mD1.22 + K8C + G99C fused in between K8C-G99C _{the CH1 domain and hinge of model V3-bNAb1 heavy} chain with 1xG4S linker, Fc includes M428L/N434S _{bNAb1-HC_1xG4S_ D1m-K8C-} Human CD4 mD1.22 + K8C + G99C fused to the C- G99C _{terminus of model V3-bNAb1 heavy chain with 1xG4S} linker, Fc includes M428L/N434S _{bNAb1-LC_1xG4S_D1m-K8C-} Human CD4 mD1.22 + K8C + G99C fused to the C- G99C _{terminus of model V3-bNAb1 light chain with 1xG4S} linker _{D1m-K8I_1xG4S_bNAb1-HC Human CD4 mD1.22 + K8I fused to the N-terminus of} _{model V3-bNAb1 heavy chain with 1xG4S linker, Fc} includes M428L/N434S _{D1m-K8V_1xG4S_bNAb1-HC Human CD4 mD1.22 + K8V fused to the N-terminus of} _{model V3-bNAb1 heavy chain with 1xG4S linker, Fc} includes M428L/N434S _{D1m-K8C-G99C_1xG4S_bNAb1-} Human CD4 mD1.22 + K8C + G99C fused to the N- HC _{terminus of model V3-bNAb1 heavy chain with 1xG4S} linker, Fc includes M428L/N434S _D1m-T11C- Human CD4 mD1.22 + T11C + K72C fused to the N- K72C_1xG4S_bNAb1-HC _{terminus of model V3-bNAb1 heavy chain with 1xG4S} linker, Fc includes M428L/N434S _{D1m-K8C-G99C_2xG4S_bNAb2-} Human CD4 mD1.22 + K8C + G99C fused to the N- HC _{terminus of model V3-bNAb2 heavy chain with 2xG4S} linker, Fc includes M428L/N434S _{D1m-K8C-G99C_3xG4S_bNAb2-} Human CD4 mD1.22 + K8C + G99C fused to the N- HC _{terminus of model V3-bNAb2 heavy chain with 3xG4S} linker, Fc includes M428L/N434S _{D1m-K8C-G99C_4xG4S_bNAb2-} Human CD4 mD1.22 + K8C + G99C fused to the N- HC _{terminus of model V3-bNAb2 heavy chain with 4xG4S} linker, Fc includes M428L/N434S _{bNAb2-LC_1xG4S_D1m-K8C-} Human CD4 mD1.22 + K8C + G99C fused to the C- G99C _{terminus of model V3-bNAb2 light chain with 1xG4S} linker _{D1m-K8C-G99C_1xG4S_bNAb3-} Human CD4 mD1.22 + K8C + G99C fused to the N- HC _{terminus of model V3-bNAb3 heavy chain with 1xG4S} linker, Fc includes M428L/N434S _{D1m-K8C-G99C_4xG4S_bNAb3-} Human CD4 mD1.22 + K8C + G99C fused to the N- HC _{terminus of model V3-bNAb3 heavy chain with 4xG4S} linker, Fc includes M428L/N434S _{D1m-K8C-G99C_4xG4S_bNAb4-} Human CD4 mD1.22 + K8C + G99C fused to the N- HC _{terminus of model V3-bNAb4 heavy chain with 4xG4S} linker, Fc includes M428L/N434S _{D1m-K8C-G99C_Fc Human CD4 mD1.22 + K8C, G99C with C-terminal Fc} tag including M428L/N434S _{V3 loop V3 loop consensus sequence} _{Exemplary gp160 Exemplary gp160 sequence} _{Exemplary gp120 Exemplary gp120 sequence} _{Exemplary gp41 Exemplary gp41 sequence} _{V1/V2 loop Apex V1/V2 apex consensus sequence} _{Interface Gp120-gp41 interface consensus non-continuous} sequence _{Interface bispecific (based on} Human CD4 mD1.22 + K8C + G99C fused to the N- Interface-bNAb17) terminus of interface-bNAb17 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{Interface bispecific (based on} Human CD4 mD1.22 + K8C + G99C fused to the N- interface-bNAb18) terminus of interface-bNAb18 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{Interface bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- _{(based on interface-bNAb19)} terminus of interface-bNAb19 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{Interface bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on interface-bNAb20) terminus of interface-bNAb20 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{Interface bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- _{(based on interface-bNAb21)} terminus of interface-bNAb21 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{Interface bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- _{(based on interface-bNAb22)} terminus of interface-bNAb22 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{Interface bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- _{(based on interface-bNAb23)} terminus of interface-bNAb23 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{Interface bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- _{(based on interface-bNAb24)} terminus of interface-bNAb24 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{Interface bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on interface-bNAb25) terminus of interface-bNAb25 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{Interface bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- _{(based on interface-bNAb26)} terminus of interface-bNAb26 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{Interface bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- _{(based on interface-bNAb27)} terminus of interface-bNAb27 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{Interface bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- _{(based on interface-bNAb29)} terminus of interface-bNAb29 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{Interface bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- _{(based on interface-bNAb30)} terminus of interface-bNAb30 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{Interface bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- _{(based on interface-bNAb31)} terminus of interface-bNAb31 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- _{(based on Apex-bNAb1)} terminus of apex-bNAb1 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb2) terminus of apex-bNAb2 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb3) terminus of apex-bNAb3 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb4) terminus of apex-bNAb4 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb5) terminus of apex-bNAb5 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb6) terminus of apex-bNAb7 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb7) terminus of apex-bNAb8 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific (based on} Human CD4 mD1.22 + K8C + G99C fused to the N- Apex-bNAb8) terminus of apex-bNAb9 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb9) terminus of apex-bNAb10 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb10) terminus of apex-bNAb11 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb11) terminus of apex-bNAb12 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb12) terminus of apex-bNAb13 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb13) terminus of apex-bNAb14 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb14) terminus of apex-bNAb15 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb15) terminus of apex-bNAb16 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{V1/V2 apex bispecific} Human CD4 mD1.22 + K8C + G99C fused to the N- (based on Apex-bNAb16) terminus of apex-bNAb7 heavy chain with 1xG4S linker, Fc includes M428L/N434S _{(Interface-bNAb17) CDRH1 CDRH1 of interface-bNAb17} _{(Interface-bNAb17) CDRH2 CDRH2 of interface-bNAb17} _{(Interface-bNAb17) CDRH3 CDRH3 of interface-bNAb17} _{(Interface-bNAb17) CDRL1 CDRL1 of interface-bNAb17} _{(Interface-bNAb17) CDRL2 CDRL2 of interface-bNAb17} _{(Interface-bNAb17) CDRL3 CDRL3 of interface-bNAb17} _{(Interface-bNAb17) VH VH domain of interface-bNAb17} _{(Interface-bNAb17) VL VL domain of interface-bNAb17} _{(Interface-bNAb17) HC (no LS) Heavy chain of interface-bNAb17} _{(Interface-bNAb17) HC (LS) Heavy chain of interface-bNAb17, Fc includes} M428L/N434S _{(Interface-bNAb17) LC Light chain of interface-bNAb17} _{(Interface-bNAb18) CDRH1 CDRH1 of interface-bNAb18} _{(Interface-bNAb18) CDRH2 CDRH2 of interface-bNAb18} _{(Interface-bNAb18) CDRH3 CDRH3 of interface-bNAb18} _{(Interface-bNAb18) CDRL1 CDRL1 of interface-bNAb18} _{(Interface-bNAb18) CDRL2 CDRL2 of interface-bNAb18} _{(Interface-bNAb18) CDRL3 CDRL3 of interface-bNAb18} _{(Interface-bNAb18) VH VH domain of interface-bNAb18} _{(Interface-bNAb18) VL VL domain of interface-bNAb18} _{(Interface-bNAb18) HC (no LS) Heavy chain of interface-bNAb18} _{(Interface-bNAb18) HC (LS) Heavy chain of interface-bNAb18, Fc includes} M428L/N434S _{(Interface-bNAb18) LC Light chain of interface-bNAb18} _{(Interface-bNAb19) CDRH1 CDRH1 of interface-bNAb19} _{(Interface-bNAb19) CDRH2 CDRH2 of interface-bNAb19} _{(Interface-bNAb19) CDRH3 CDRH3 of interface-bNAb19} _{(Interface-bNAb19) CDRL1 CDRL1 of interface-bNAb19} _{(Interface-bNAb19) CDRL2 CDRL2 of interface-bNAb19} _{(Interface-bNAb19) CDRL3 CDRL3 of interface-bNAb19} _{(Interface-bNAb19) VH VH domain of interface-bNAb19} _{(Interface-bNAb19) VL VL domain of interface-bNAb19} _{(Interface-bNAb19) HC (no LS) Heavy chain of interface-bNAb19} _{(Interface-bNAb19) HC (LS) Heavy chain of interface-bNAb19, Fc includes} M428L/N434S _{(Interface-bNAb19) LC Light chain of interface-bNAb19} _{(Interface-bNAb20) CDRH1 CDRH1 of interface-bNAb20} _{(Interface-bNAb20) CDRH2 CDRH2 of interface-bNAb20} _{(Interface-bNAb20) CDRH3 CDRH3 of interface-bNAb20} _{(Interface-bNAb20) CDRL1 CDRL1 of interface-bNAb20} _{(Interface-bNAb20) CDRL2 CDRL2 of interface-bNAb20} _{(Interface-bNAb20) CDRL3 CDRL3 of interface-bNAb20} _{(Interface-bNAb20) VH VH domain of interface-bNAb20} _{(Interface-bNAb20) VL VL domain of interface-bNAb20} _{(Interface-bNAb20) HC (no LS) Heavy chain of interface-bNAb20} _{(Interface-bNAb20) HC (LS) Heavy chain of interface-bNAb20, Fc includes} M428L/N434S _{(Interface-bNAb20) LC Light chain of interface-bNAb20} _{(Interface-bNAb21) CDRH1 CDRH1 of interface-bNAb21} _{(Interface-bNAb21) CDRH2 CDRH2 of interface-bNAb21} _{(Interface-bNAb21) CDRH3 CDRH3 of interface-bNAb21} _{(Interface-bNAb21) CDRL1 CDRL1 of interface-bNAb21} _{(Interface-bNAb21) CDRL2 CDRL2 of interface-bNAb21} _{(Interface-bNAb21) CDRL3 CDRL3 of interface-bNAb21} _{(Interface-bNAb21) VH VH domain of interface-bNAb21} _{(Interface-bNAb21) VL VL domain of interface-bNAb21} _{(Interface-bNAb21) HC (no LS) Heavy chain of interface-bNAb21} _{(Interface-bNAb21) HC (LS) Heavy chain of interface-bNAb21, Fc includes} M428L/N434S _{(Interface-bNAb21) LC Light chain of interface-bNAb21} _{(Interface-bNAb22) CDRH1 CDRH1 of interface-bNAb22} _{(Interface-bNAb22) CDRH2 CDRH2 of interface-bNAb22} _{(Interface-bNAb22) CDRH3 CDRH3 of interface-bNAb22} _{(Interface-bNAb22) CDRL1 CDRL1 of interface-bNAb22} _{(Interface-bNAb22) CDRL2 CDRL2 of interface-bNAb22} _{(Interface-bNAb22) CDRL3 CDRL3 of interface-bNAb22} _{(Interface-bNAb22) VH VH domain of interface-bNAb22} _{(Interface-bNAb22) VL VL domain of interface-bNAb22} _{(Interface-bNAb22) HC (no LS) Heavy chain of interface-bNAb22} _{(Interface-bNAb22) HC (LS) Heavy chain of interface-bNAb22, Fc includes} M428L/N434S _{(Interface-bNAb22) LC Light chain of interface-bNAb22} _{(Interface-bNAb23) CDRH1 CDRH1 of interface-bNAb23} _{(Interface-bNAb23) CDRH2 CDRH2 of interface-bNAb23} _{(Interface-bNAb23) CDRH3 CDRH3 of interface-bNAb23} _{(Interface-bNAb23) CDRL1 CDRL1 of interface-bNAb23} _{(Interface-bNAb23) CDRL2 CDRL2 of interface-bNAb23} _{(Interface-bNAb23) CDRL3 CDRL3 of interface-bNAb23} _{(Interface-bNAb23) VH VH domain of interface-bNAb23} _{(Interface-bNAb23) VL VL domain of interface-bNAb23} _{(Interface-bNAb23) HC (no LS) Heavy chain of interface-bNAb23} _{(Interface-bNAb23) HC (LS) Heavy chain of interface-bNAb23, Fc includes} M428L/N434S _{(Interface-bNAb23) LC Light chain of interface-bNAb23} _{(Interface-bNAb24) CDRH1 CDRH1 of interface-bNAb24} _{(Interface-bNAb24) CDRH2 CDRH2 of interface-bNAb24} _{(Interface-bNAb24) CDRH3 CDRH3 of interface-bNAb24} _{(Interface-bNAb24) CDRL1 CDRL1 of interface-bNAb24} _{(Interface-bNAb24) CDRL2 CDRL2 of interface-bNAb24} _{(Interface-bNAb24) CDRL3 CDRL3 of interface-bNAb24} _{(Interface-bNAb24) VH VH domain of interface-bNAb24} _{(Interface-bNAb24) VL VL domain of interface-bNAb24} _{(Interface-bNAb24) HC (no LS) Heavy chain of interface-bNAb24} _{(Interface-bNAb24) HC (LS) Heavy chain of interface-bNAb24, Fc includes} M428L/N434S _{(Interface-bNAb24) LC Light chain of interface-bNAb24} _{(Interface-bNAb25) CDRH1 CDRH1 of interface-bNAb25} _{(Interface-bNAb25) CDRH2 CDRH2 of interface-bNAb25} _{(Interface-bNAb25) CDRH3 CDRH3 of interface-bNAb25} _{(Interface-bNAb25) CDRL1 CDRL1 of interface-bNAb25} _{(Interface-bNAb25) CDRL2 CDRL2 of interface-bNAb25} _{(Interface-bNAb25) CDRL3 CDRL3 of interface-bNAb25} _{(Interface-bNAb25) VH VH domain of interface-bNAb25} _{(Interface-bNAb25) VL VL domain of interface-bNAb25} _{(Interface-bNAb25) HC (no LS) Heavy chain of interface-bNAb25} _{(Interface-bNAb25) HC (LS) Heavy chain of interface-bNAb25, Fc includes} M428L/N434S _{(Interface-bNAb25) LC Light chain of interface-bNAb25} _{(Interface-bNAb26) CDRH1 CDRH1 of interface-bNAb26} _{(Interface-bNAb26) CDRH2 CDRH2 of interface-bNAb26} _{(Interface-bNAb26) CDRH3 CDRH3 of interface-bNAb26} _{(Interface-bNAb26) CDRL1 CDRL1 of interface-bNAb26} _{(Interface-bNAb26) CDRL2 CDRL2 of interface-bNAb26} _{(Interface-bNAb26) CDRL3 CDRL3 of interface-bNAb26} _{(Interface-bNAb26) VH VH domain of interface-bNAb26} _{(Interface-bNAb26) VL VL domain of interface-bNAb26} _{(Interface-bNAb26) HC (no LS) Heavy chain of interface-bNAb26} _{(Interface-bNAb26) HC (LS) Heavy chain of interface-bNAb26, Fc includes} M428L/N434S _{(Interface-bNAb26) LC Light chain of interface-bNAb26} _{(Interface-bNAb27) CDRH1 CDRH1 of interface-bNAb27} _{(Interface-bNAb27) CDRH2 CDRH2 of interface-bNAb27} _{(Interface-bNAb27) CDRH3 CDRH3 of interface-bNAb27} _{(Interface-bNAb27) CDRL1 CDRL1 of interface-bNAb27} _{(Interface-bNAb27) CDRL2 CDRL2 of interface-bNAb27} _{(Interface-bNAb27) CDRL3 CDRL3 of interface-bNAb27} _{(Interface-bNAb27) VH VH domain of interface-bNAb27} _{(Interface-bNAb27) VL VL domain of interface-bNAb27} _{(Interface-bNAb27) HC (no LS) Heavy chain of interface-bNAb27} _{(Interface-bNAb27) HC (LS) Heavy chain of interface-bNAb27, Fc includes} M428L/N434S _{(Interface-bNAb27) LC Light chain of interface-bNAb27} _{(Interface-bNAb29) CDRH1 CDRH1 of interface-bNAb29} _{(Interface-bNAb29) CDRH2 CDRH2 of interface-bNAb29} _{(Interface-bNAb29) CDRH3 CDRH3 of interface-bNAb29} _{(Interface-bNAb29) CDRL1 CDRL1 of interface-bNAb29} _{(Interface-bNAb29) CDRL2 CDRL2 of interface-bNAb29} _{(Interface-bNAb29) CDRL3 CDRL3 of interface-bNAb29} _{(Interface-bNAb29) VH VH domain of interface-bNAb29} _{(Interface-bNAb29) VL VL domain of interface-bNAb29} _{(Interface-bNAb29) HC (no LS) Heavy chain of interface-bNAb29} _{(Interface-bNAb29) HC (LS) Heavy chain of interface-bNAb29, Fc includes} M428L/N434S _{(Interface-bNAb29) LC Light chain of interface-bNAb29} _{(Interface-bNAb30) CDRH1 CDRH1 of interface-bNAb30} _{(Interface-bNAb30) CDRH2 CDRH2 of interface-bNAb30} _{(Interface-bNAb30) CDRH3 CDRH3 of interface-bNAb30} _{(Interface-bNAb30) CDRL1 CDRL1 of interface-bNAb30} _{(Interface-bNAb30) CDRL2 CDRL2 of interface-bNAb30} _{(Interface-bNAb30) CDRL3 CDRL3 of interface-bNAb30} _{(Interface-bNAb30) VH VH domain of interface-bNAb30} _{(Interface-bNAb30) VL VL domain of interface-bNAb30} _{(Interface-bNAb30) HC (no LS) Heavy chain of interface-bNAb30} _{(Interface-bNAb30) HC (LS) Heavy chain of interface-bNAb30, Fc includes} M428L/N434S _{(Interface-bNAb30) LC Light chain of interface-bNAb30} _{(Interface-bNAb31) CDRH1 CDRH1 of interface-bNAb31} _{(Interface-bNAb31) CDRH2 CDRH2 of interface-bNAb31} _{(Interface-bNAb31) CDRH3 CDRH3 of interface-bNAb31} _{(Interface-bNAb31) CDRL1 CDRL1 of interface-bNAb31} _{(Interface-bNAb31) CDRL2 CDRL2 of interface-bNAb31} _{(Interface-bNAb31) CDRL3 CDRL3 of interface-bNAb31} _{(Interface-bNAb31) VH VH domain of interface-bNAb31} _{(Interface-bNAb31) VL VL domain of interface-bNAb31} _{(Interface-bNAb31) HC (no LS) Heavy chain of interface-bNAb31} _{(Interface-bNAb30) HC (LS) Heavy chain of interface-bNAb31, Fc includes} M428L/N434S _{(Interface-bNAb30) LC Light chain of interface-bNAb31} _{(Apex-bNAb1) CDRH1 CDRH1 of apex-bNAb1} _{(Apex-bNAb1) CDRH2 CDRH2 of apex-bNAb1} _{(Apex-bNAb1) CDRH3 CDRH3 of apex-bNAb1} _{(Apex-bNAb1) CDRL1 CDRL1 of apex-bNAb1} _{(Apex-bNAb1) CDRL2 CDRL2 of apex-bNAb1} _{(Apex-bNAb1) CDRL3 CDRL3 of apex-bNAb1} _{(Apex-bNAb1) VH VH domain of apex-bNAb1} _{(Apex-bNAb1) VL VL domain of apex-bNAb1} _{(Apex-bNAb1) HC (no LS) Heavy chain of apex-bNAb1} _{(Apex-bNAb1) HC (LS) Heavy chain of apex-bNAb1, Fc includes M428L/N434S} _{(Apex-bNAb1) LC Light chain of apex-bNAb1} _{(Apex-bNAb2) CDRH1 CDRH1 of apex-bNAb2} _{(Apex-bNAb2) CDRH2 CDRH2 of apex-bNAb2} _{(Apex-bNAb2) CDRH3 CDRH3 of apex-bNAb2} _{(Apex-bNAb2) CDRL1 CDRL1 of apex-bNAb2} _{(Apex-bNAb2) CDRL2 CDRL2 of apex-bNAb2} _{(Apex-bNAb2) CDRL3 CDRL3 of apex-bNAb2} _{(Apex-bNAb2) VH VH domain of apex-bNAb2} _{(Apex-bNAb2) VL VL domain of apex-bNAb2} _{(Apex-bNAb2) HC (no LS) Heavy chain of apex-bNAb2} _{(Apex-bNAb2) HC (LS) Heavy chain of apex-bNAb2, Fc includes M428L/N434S} _{(Apex-bNAb2) LC Light chain of apex-bNAb2} _{(Apex-bNAb3) CDRH1 CDRH1 of apex-bNAb3} _{(Apex-bNAb3) CDRH2 CDRH2 of apex-bNAb3} _{(Apex-bNAb3) CDRH3 CDRH3 of apex-bNAb3} _{(Apex-bNAb3) CDRL1 CDRL1 of apex-bNAb3} _{(Apex-bNAb3) CDRL2 CDRL2 of apex-bNAb3} _{(Apex-bNAb3) CDRL3 CDRL3 of apex-bNAb3} _{(Apex-bNAb3) VH VH domain of apex-bNAb3} _{(Apex-bNAb3) VL VL domain of apex-bNAb3} _{(Apex-bNAb3) HC (no LS) Heavy chain of apex-bNAb3} _{(Apex-bNAb3) HC (LS) Heavy chain of apex-bNAb3, Fc includes M428L/N434S} _{(Apex-bNAb3) LC Light chain of apex-bNAb3} _{(Apex-bNAb4) CDRH1 CDRH1 of apex-bNAb4} _{(Apex-bNAb4) CDRH2 CDRH2 of apex-bNAb4} _{(Apex-bNAb4) CDRH3 CDRH3 of apex-bNAb4} _{(Apex-bNAb4) CDRL1 CDRL1 of apex-bNAb4} _{(Apex-bNAb4) CDRL2 CDRL2 of apex-bNAb4} _{(Apex-bNAb4) CDRL3 CDRL3 of apex-bNAb4} _{(Apex-bNAb4) VH VH domain of apex-bNAb4} _{(Apex-bNAb4) VL VL domain of apex-bNAb4} _{(Apex-bNAb4) HC (no LS) Heavy chain of apex-bNAb4} _{(Apex-bNAb4) HC (LS) Heavy chain of apex-bNAb4, Fc includes M428L/N434S} _{(Apex-bNAb4) LC Light chain of apex-bNAb4} _{(Apex-bNAb5) CDRH1 CDRH1 of apex-bNAb5} _{(Apex-bNAb5) CDRH2 CDRH2 of apex-bNAb5} _{(Apex-bNAb5) CDRH3 CDRH3 of apex-bNAb5} _{(Apex-bNAb5) CDRL1 CDRL1 of apex-bNAb5} _{(Apex-bNAb5) CDRL2 CDRL2 of apex-bNAb5} _{(Apex-bNAb5) CDRL3 CDRL3 of apex-bNAb5} _{(Apex-bNAb5) VH VH domain of apex-bNAb5} _{(Apex-bNAb5) VL VL domain of apex-bNAb5} _{(Apex-bNAb5) HC (no LS) Heavy chain of apex-bNAb5} _{(Apex-bNAb5) HC (LS) Heavy chain of apex-bNAb5, Fc includes M428L/N434S} _{(Apex-bNAb5) LC Light chain of apex-bNAb5} _{(Apex-bNAb6) CDRH1 CDRH1 of apex-bNAb6} _{(Apex-bNAb6) CDRH2 CDRH2 of apex-bNAb6} _{(Apex-bNAb6) CDRH3 CDRH3 of apex-bNAb6} _{(Apex-bNAb6) CDRL1 CDRL1 of apex-bNAb6} _{(Apex-bNAb6) CDRL2 CDRL2 of apex-bNAb6} _{(Apex-bNAb6) CDRL3 CDRL3 of apex-bNAb6} _{(Apex-bNAb6) VH VH domain of apex-bNAb6} _{(Apex-bNAb6) VL VL domain of apex-bNAb6} _{(Apex-bNAb6) HC (no LS) Heavy chain of apex-bNAb6} _{(Apex-bNAb6) HC (LS) Heavy chain of apex-bNAb6, Fc includes M428L/N434S} _{(Apex-bNAb6) LC Light chain of apex-bNAb6} _{(Apex-bNAb7) CDRH1 CDRH1 of apex-bNAb7} _{(Apex-bNAb7) CDRH2 CDRH2 of apex-bNAb7} _{(Apex-bNAb7) CDRH3 CDRH3 of apex-bNAb7} _{(Apex-bNAb7) CDRL1 CDRL1 of apex-bNAb7} _{(Apex-bNAb7) CDRL2 CDRL2 of apex-bNAb7} _{(Apex-bNAb7) CDRL3 CDRL3 of apex-bNAb7} _{(Apex-bNAb7) VH VH domain of apex-bNAb7} _{(Apex-bNAb7) VL VL domain of apex-bNAb7} _{(Apex-bNAb7) HC (no LS) Heavy chain of apex-bNAb7} _{(Apex-bNAb7) HC (LS) Heavy chain of apex-bNAb7, Fc includes M428L/N434S} _{(Apex-bNAb7) LC Light chain of apex-bNAb7} _{(Apex-bNAb8) CDRH1 CDRH1 of apex-bNAb8} _{(Apex-bNAb8) CDRH2 CDRH2 of apex-bNAb8} _{(Apex-bNAb8) CDRH3 CDRH3 of apex-bNAb8} _{(Apex-bNAb8) CDRL1 CDRL1 of apex-bNAb8} _{(Apex-bNAb8) CDRL2 CDRL2 of apex-bNAb8} _{(Apex-bNAb8) CDRL3 CDRL3 of apex-bNAb8} _{(Apex-bNAb8) VH VH domain of apex-bNAb8} _{(Apex-bNAb8) VL VL domain of apex-bNAb8} _{(Apex-bNAb8) HC (no LS) Heavy chain of apex-bNAb8} _{(Apex-bNAb8) HC (LS) Heavy chain of apex-bNAb8, Fc includes M428L/N434S} _{(Apex-bNAb8) LC Light chain of apex-bNAb8} _{(Apex-bNAb9) CDRH1 CDRH1 of apex-bNAb9} _{(Apex-bNAb9) CDRH2 CDRH2 of apex-bNAb9} _{(Apex-bNAb9) CDRH3 CDRH3 of apex-bNAb9} _{(Apex-bNAb9) CDRL1 CDRL1 of apex-bNAb9} _{(Apex-bNAb9) CDRL2 CDRL2 of apex-bNAb9} _{(Apex-bNAb9) CDRL3 CDRL3 of apex-bNAb9} _{(Apex-bNAb9) VH VH domain of apex-bNAb9} _{(Apex-bNAb9) VL VL domain of apex-bNAb9} _{(Apex-bNAb9) HC (no LS) Heavy chain of apex-bNAb9} _{(Apex-bNAb9) HC (LS) Heavy chain of apex-bNAb9, Fc includes M428L/N434S} _{(Apex-bNAb9) LC Light chain of apex-bNAb9} _{(Apex-bNAb10) CDRH1 CDRH1 of apex-bNAb10} _{(Apex-bNAb10) CDRH2 CDRH2 of apex-bNAb10} _{(Apex-bNAb10) CDRH3 CDRH3 of apex-bNAb10} _{(Apex-bNAb10) CDRL1 CDRL1 of apex-bNAb10} _{(Apex-bNAb10) CDRL2 CDRL2 of apex-bNAb10} _{(Apex-bNAb10) CDRL3 CDRL3 of apex-bNAb10} _{(Apex-bNAb10) VH VH domain of apex-bNAb10} _{(Apex-bNAb10) VL VL domain of apex-bNAb10} _{(Apex-bNAb10) HC (no LS) Heavy chain of apex-bNAb10} _{(Apex-bNAb10) HC (LS) Heavy chain of apex-bNAb10, Fc includes M428L/N434S} _{(Apex-bNAb10) LC Light chain of apex-bNAb10} _{(Apex-bNAb11) CDRH1 CDRH1 of apex-bNAb11} _{(Apex-bNAb11) CDRH2 CDRH2 of apex-bNAb11} _{(Apex-bNAb11) CDRH3 CDRH3 of apex-bNAb11} _{(Apex-bNAb11) CDRL1 CDRL1 of apex-bNAb11} _{(Apex-bNAb11) CDRL2 CDRL2 of apex-bNAb11} _{(Apex-bNAb11) CDRL3 CDRL3 of apex-bNAb11} _{(Apex-bNAb11) VH VH domain of apex-bNAb11} _{(Apex-bNAb11) VL VL domain of apex-bNAb11} _{(Apex-bNAb11) HC (no LS) Heavy chain of apex-bNAb11} _{(Apex-bNAb11) HC (LS) Heavy chain of apex-bNAb11, Fc includes M428L/N434S} _{(Apex-bNAb11) LC Light chain of apex-bNAb11} _{(Apex-bNAb12) CDRH1 CDRH1 of apex-bNAb12} _{(Apex-bNAb12) CDRH2 CDRH2 of apex-bNAb12} _{(Apex-bNAb12) CDRH3 CDRH3 of apex-bNAb12} _{(Apex-bNAb12) CDRL1 CDRL1 of apex-bNAb12} _{(Apex-bNAb12) CDRL2 CDRL2 of apex-bNAb12} _{(Apex-bNAb12) CDRL3 CDRL3 of apex-bNAb12} _{(Apex-bNAb12) VH VH domain of apex-bNAb12} _{(Apex-bNAb12) VL VL domain of apex-bNAb12} _{(Apex-bNAb12) HC (no LS) Heavy chain of apex-bNAb12} _{(Apex-bNAb12) HC (LS) Heavy chain of apex-bNAb12, Fc includes M428L/N434S} _{(Apex-bNAb12) LC Light chain of apex-bNAb12} _{(Apex-bNAb13) CDRH1 CDRH1 of apex-bNAb13} _{(Apex-bNAb13) CDRH2 CDRH2 of apex-bNAb13} _{(Apex-bNAb13) CDRH3 CDRH3 of apex-bNAb13} _{(Apex-bNAb13) CDRL1 CDRL1 of apex-bNAb13} _{(Apex-bNAb13) CDRL2 CDRL2 of apex-bNAb13} _{(Apex-bNAb13) CDRL3 CDRL3 of apex-bNAb13} _{(Apex-bNAb13) VH VH domain of apex-bNAb13} _{(Apex-bNAb13) VL VL domain of apex-bNAb13} _{(Apex-bNAb13) HC (no LS) Heavy chain of apex-bNAb13} _{(Apex-bNAb13) HC (LS) Heavy chain of apex-bNAb13, Fc includes M428L/N434S} _{(Apex-bNAb13) LC Light chain of apex-bNAb13} _{(Apex-bNAb14) CDRH1 CDRH1 of apex-bNAb14} _{(Apex-bNAb14) CDRH2 CDRH2 of apex-bNAb14} _{(Apex-bNAb14) CDRH3 CDRH3 of apex-bNAb14} _{(Apex-bNAb14) CDRL1 CDRL1 of apex-bNAb14} _{(Apex-bNAb14) CDRL2 CDRL2 of apex-bNAb14} _{(Apex-bNAb14) CDRL3 CDRL3 of apex-bNAb14} _{(Apex-bNAb14) VH VH domain of apex-bNAb14} _{(Apex-bNAb14) VL VL domain of apex-bNAb14} _{(Apex-bNAb14) HC (no LS) Heavy chain of apex-bNAb14} _{(Apex-bNAb14) HC (LS) Heavy chain of apex-bNAb14, Fc includes M428L/N434S} _{(Apex-bNAb14) LC Light chain of apex-bNAb14} _{398 (Apex-bNAb15) CDRH1 CDRH1 of apex-bNAb15} _{399 (Apex-bNAb15) CDRH2 CDRH2 of apex-bNAb15} _{400 (Apex-bNAb15) CDRH3 CDRH3 of apex-bNAb15} _{401 (Apex-bNAb15) CDRL1 CDRL1 of apex-bNAb15} _{402 (Apex-bNAb15) CDRL2 CDRL2 of apex-bNAb15} _{403 (Apex-bNAb15) CDRL3 CDRL3 of apex-bNAb15} _{404 (Apex-bNAb15) VH VH domain of apex-bNAb15} _{405 (Apex-bNAb15) VL VL domain of apex-bNAb15} _{406 (Apex-bNAb15) HC (no LS) Heavy chain of apex-bNAb15} _{407 (Apex-bNAb15) HC (LS) Heavy chain of apex-bNAb15, Fc includes M428L/N434S} _{408 (Apex-bNAb15) LC Light chain of apex-bNAb15} _{409 (Apex-bNAb16) CDRH1 CDRH1 of apex-bNAb16} _{410 (Apex-bNAb16) CDRH2 CDRH2 of apex-bNAb16} _{411 (Apex-bNAb16) CDRH3 CDRH3 of apex-bNAb16} _{412 (Apex-bNAb16) CDRL1 CDRL1 of apex-bNAb16} _{413 (Apex-bNAb16) CDRL2 CDRL2 of apex-bNAb16} _{414 (Apex-bNAb16) CDRL3 CDRL3 of apex-bNAb16} _{415 (Apex-bNAb16) VH VH domain of apex-bNAb16} _{416 (Apex-bNAb16) VL VL domain of apex-bNAb16} _{417 (Apex-bNAb16) HC (no LS) Heavy chain of apex-bNAb16} _{418 (Apex-bNAb16) HC (LS) Heavy chain of apex-bNAb16, Fc includes M428L/N434S} _{419 Apex-bNAb16 LC Light chain of apex-bNAb16} _{420 V1/V2 apex bispecific 2} Human CD4 mD1.22 + K8C + G99C fused to the N- (bispecific1-2, based on Apex- terminus of apex-bNAb1 light chain with 1xG4S linker, bNAb1) Fc includes M428L/N434S 4_{21 V1/V2 apex bispecific 3} Human CD4 mD1.22 + K8C + G99C fused to the C- (bispecific1-3, based on Apex- terminus of apex-bNAb1 heavy chain with 1xG4S linker, bNAb1) Fc includes M428L/N434S 4_{22 V1/V2 apex bispecific 4} Human CD4 mD1.22 + K8C + G99C fused to the C- (bispecific1-4, based on Apex- terminus of apex-bNAb1 light chain with 1xG4S linker, bNAb1) Fc includes M428L/N434S 4_{23 V1/V2 apex bispecific 2} Human CD4 mD1.22 + K8C + G99C fused to the N- (bispecific2-2, based on Apex- terminus of apex-bNAb2 light chain with 1xG4S linker, bNAb2) Fc includes M428L/N434S 4_{24 V1/V2 apex bispecific 3} Human CD4 mD1.22 + K8C + G99C fused to the C- (bispecific2-3, based on Apex- terminus of apex-bNAb2 heavy chain with 1xG4S linker, bNAb2) Fc includes M428L/N434S 4_{25 V1/V2 apex bispecific 4} Human CD4 mD1.22 + K8C + G99C fused to the C- (bispecific2-4, based on Apex- terminus of apex-bNAb2 light chain with 1xG4S linker, bNAb2) Fc includes M428L/N434S 4_{26 D1m-K8C-G99C_1xG4S_bNAb1- Human CD4 mD1.22 + K8C + G99C fused to the N-} LC _{terminus of model V3-bNAb1 light chain with 1xG4S} linker SEQ ID NO: 1 (D1D2) KKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLK IEDSDTYICEVEDQKEEVQLLVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLEL QDSGTWTCTVLQNQKKVEFKIDIVVLA SEQ ID NO:2 (D1mD2) KKVVLGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KIEDSDTYICEVEDQKEEVQLVVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLE LQDSGTWTCTVLQNQKKVEFKIDIVVLAF SEQ ID NO:3 (D1) KKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLK IEDSDTYICEVEDQKEEVQLLVFG SEQ ID NO:4 (D1m) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:5 (D1m-K8V) KKVVYGKVGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:6 (D1m-E91Q) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKQEVQLVVVG SEQ ID NO:7 (D1m-E91H) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKHEVQLVVVG SEQ ID NO:8 (D1m-E87G) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVGDQKEEVQLVVVG SEQ ID NO:9 (D1m-N52W) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLWDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:10 (D1m-K8I) KKVVYGKIGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNLK PEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:11 (D1m-K8C-G99C) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVC SEQ ID NO:12 (D1m-T11C-K72C) KKVVYGKKGDCVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIICNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:13 (D1m-E13C-I70C) KKVVYGKKGDTVCLTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLCIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:14 (D1m-H27C-G38C) KKVVYGKKGDTVELTCTASQKKNIQFCWKNSNQIKILCNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:15 (D1m-K21C-G65C) KKVVYGKKGDTVELTCTASQCKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQCNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:16 (D1m-Q25E) KKVVYGKKGDTVELTCTASQKKNIEFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG _{SEQ ID NO:17 (D1m-H27D)} KKVVYGKKGDTVELTCTASQKKNIQFDWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG _{SEQ ID NO:18 (D1m-R58V)} KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSVRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:19 (D1m-R58N) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSNRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG _{SEQ ID NO:20 (D1m-R58T)} KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSTRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:21 (D1m-L61M) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSMWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVG SEQ ID NO:22 (V3-bNAb1 HC+LS) QPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPPGKGLEWVGSLSHCASYWNRGWTYHNPSLK SRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDWPKPAWVDLWGRGTLVTVSSASTKGPSVFPL APSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV LHEALHSHYTQKSLSLSPGK SEQ ID NO:23 (V3-bNAb1 LC) QSALTQPPSASGSPGQSITISCTGTSNNFVSWYQQHAGKAPKLVIYDVNKRPSGVPDRFSGSKSGNTASLTVSG LQTDDEAVYYCGSLVGNWDVIFGGGTKLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKA DSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS SEQ ID NO:24 (V3-bNAb2 HC+LS) QMQLQESGPGLVKPSETLSLTCSVSGASISDSYWSWIRRSPGKGLEWIGYVHKSGDTNYSPSLKSRVNLSLDTS KNQVSLSLVAATAADSGKYYCARTLHGRRIYGIVAFNEWFTYFYMDVWGNGTQVTVSSASTKGPSVFPLAPSSK STSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSN TKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVE VHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDEL TKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEAL HSHYTQKSLSLSPGK SEQ ID NO:25 (V3-bNAb2 LC) SDISVAPGETARISCGEKSLGSRAVQWYQHRAGQAPSLIIYNNQDRPSGIPERFSGSPDSPFGTTATLTITSVEAG DEADYYCHIWDSRVPTKWVFGGGTTLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKAD SSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPTECS SEQ ID NO:26 (V3-bNAb3 HC+LS) QVQLRESGPGLVKPSETLSLSCTVSNDSRPSDHSWTWVRQSPGKALEWIGDIHYNGATTYNPSLRSRVRIELDQ SIPRFSLKMTSMTAADTGMYYCARNAIRIYGVVALGEWFHYGMDVWGQGTAVTVSSASTKGPSVFPLAPSSKST SGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTK VDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVH NAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTK NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHS HYTQKSLSLSPGK SEQ ID NO:27 (V3-bNAb3 LC) SSELTQPPSVSVSPGQTARITCSGAPLTSRFTYWYRQKPGQAPVLIISRSSQRSSGWSGRFSASWSGTTVTLTIR GVQADDEADYYCQSSDTSDSYKMFGGGTKLTVLGQPAAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVA WKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPTEC SEQ ID NO:28 (V3-bNAb4 HC+LS) QVQLQESGPGLVKPSETLSVTCSVSGDSMNNYYWTWIRQSPGKGLEWIGYISDRESATYNPSLNSRVVISRDTS KNQLSLKLNSVTPADTAVYYCATARRGQRIYGVVSFGEFFYYYSMDVWGKGTTVTVSSASTKGPSVFPLAPSSKS TSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNT KVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEV HNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELT KNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALH SHYTQKSLSLSPGK SEQ ID NO:29 (V3-bNAb4 LC) SYVRPLSVALGETARISCGRQALGSRAVQWYQHRPGQAPILLIYNNQDRPSGIPERFSGTPDINFGTRATLTISG VEAGDEADYYCHMWDSRSGFSWSFGGATRLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVA WKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS SEQ ID NO:30 (1XG4S) GGGGS SEQ ID NO: 31 (2XG4S) GGGGSGGGGS SEQ ID NO: 32 (3XG4S) GGGGSGGGGSGGGGS SEQ ID NO: 33 (4XG4S) GGGGSGGGGSGGGGSGGGGS SEQ ID NO: 34 (5XG4S) GGGGSGGGGSGGGGSGGGGSGGGGS SEQ ID NO: 35 (6XG4S) GGGGSGGGGSGGGGSGGGGSGGGGSGGGGS SEQ ID NO: 36 (D1m_1xG4S_bNAb1-HC) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVGGGGGSQPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPP GKGLEWVGSLSHCASYWNRGWTYHNPSLKSRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDW PKPAWVDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 37 (D1m_4xG4S_bNAb2-HC) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVGGGGGSGGGGSGGGGSGGGGSQPQLQESGPTLVEASETLSLTCAVSGDS TAACNSFWGWVRQPPGKGLEWVGSLSHCASYWNRGWTYHNPSLKSRLTLALDTPKNLVFLKLNSVTAADTAT YYCARFGGEVLRYTDWPKPAWVDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTV SWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPA PELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVL TVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEW ESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 38 (D1m_1xG4S_bNAb1-LC) KKVVYGKKGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVGGGGGSQSALTQPPSASGSPGQSITISCTGTSNNFVSWYQQHAGKAPKLV IYDVNKRPSGVPDRFSGSKSGNTASLTVSGLQTDDEAVYYCGSLVGNWDVIFGGGTKLTVLGQPKAAPSVTLFP PSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQ VTHEGSTVEKTVAPTECS SEQ ID NO: 39 (bNAb1-HC-mid_1xG4S_D1m-K8C-G99C) QPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPPGKGLEWVGSLSHCASYWNRGWTYHNPSLK SRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDWPKPAWVDLWGRGTLVTVSSASTKGPSVFPL APSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCGGGGSKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLN DRVDSRRSLWDQGNFPLIIKNLKPEDSDTYICEVEDQKEEVQLVVVCGGGGSDKTHTCPPCPAPELLGGPSVFLF PPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNG KEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNY KTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 40 (bNAb1-HC_1xG4S_ D1m-K8C-G99C) QPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPPGKGLEWVGSLSHCASYWNRGWTYHNPSLK SRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDWPKPAWVDLWGRGTLVTVSSASTKGPSVFPL APSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV LHEALHSHYTQKSLSLSPGGGGGSKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSK LNDRVDSRRSLWDQGNFPLIIKNLKPEDSDTYICEVEDQKEEVQLVVVC SEQ ID NO: 41 (bNAb1-LC_1xG4S_D1m-K8C-G99C) QSALTQPPSASGSPGQSITISCTGTSNNFVSWYQQHAGKAPKLVIYDVNKRPSGVPDRFSGSKSGNTASLTVSG LQTDDEAVYYCGSLVGNWDVIFGGGTKLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKA DSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECSGGGGSKKVVYGK CGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNLKPEDSDT YICEVEDQKEEVQLVVVC SEQ ID NO: 42 (D1m-K8I_1xG4S_bNAb1-HC) KKVVYGKIGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNLK PEDSDTYICEVEDQKEEVQLVVVGGGGGSQPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPPG KGLEWVGSLSHCASYWNRGWTYHNPSLKSRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDWP KPAWVDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 43 (D1m-K8V_1xG4S_bNAb1-HC) KKVVYGKVGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVGGGGGSQPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPP GKGLEWVGSLSHCASYWNRGWTYHNPSLKSRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDW PKPAWVDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 44 (D1m-K8C-G99C_1xG4S_bNAb1-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPP GKGLEWVGSLSHCASYWNRGWTYHNPSLKSRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDW PKPAWVDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 45 (D1m-T11C-K72C_1xG4S_bNAb1-HC) KKVVYGKKGDCVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIICNL KPEDSDTYICEVEDQKEEVQLVVVGGGGGSQPQLQESGPTLVEASETLSLTCAVSGDSTAACNSFWGWVRQPP GKGLEWVGSLSHCASYWNRGWTYHNPSLKSRLTLALDTPKNLVFLKLNSVTAADTATYYCARFGGEVLRYTDW PKPAWVDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 46 (D1m-K8C-G99C_2xG4S_bNAb2-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSGGGGSQMQLQESGPGLVKPSETLSLTCSVSGASISDSYWSWIRR SPGKGLEWIGYVHKSGDTNYSPSLKSRVNLSLDTSKNQVSLSLVAATAADSGKYYCARTLHGRRIYGIVAFNEWF TYFYMDVWGNGTQVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 47 (D1m-K8C-G99C_3xG4S_bNAb2-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSGGGGSGGGGSQMQLQESGPGLVKPSETLSLTCSVSGASISDSY WSWIRRSPGKGLEWIGYVHKSGDTNYSPSLKSRVNLSLDTSKNQVSLSLVAATAADSGKYYCARTLHGRRIYGI VAFNEWFTYFYMDVWGNGTQVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTS GVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVF LFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 48 (D1m-K8C-G99C_4xG4S_bNAb2-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSGGGGSGGGGSGGGGSQMQLQESGPGLVKPSETLSLTCSVSGAS ISDSYWSWIRRSPGKGLEWIGYVHKSGDTNYSPSLKSRVNLSLDTSKNQVSLSLVAATAADSGKYYCARTLHGR RIYGIVAFNEWFTYFYMDVWGNGTQVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSG ALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQ DWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQ PENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 49 (bNAb2-LC_1xG4S_D1m-K8C-G99C) SDISVAPGETARISCGEKSLGSRAVQWYQHRAGQAPSLIIYNNQDRPSGIPERFSGSPDSPFGTTATLTITSVEAG DEADYYCHIWDSRVPTKWVFGGGTTLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKAD SSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPTECSGGGGSKKVVYGKC GDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNLKPEDSDTYI CEVEDQKEEVQLVVVC SEQ ID NO: 50 (D1m-K8C-G99C_1xG4S_bNAb3-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLRESGPGLVKPSETLSLSCTVSNDSRPSDHSWTWVRQSPG KALEWIGDIHYNGATTYNPSLRSRVRIELDQSIPRFSLKMTSMTAADTGMYYCARNAIRIYGVVALGEWFHYGM DVWGQGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMIS RTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKA LPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDG SFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 51 (D1m-K8C-G99C_4xG4S_bNAb3-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSGGGGSGGGGSGGGGSQVQLRESGPGLVKPSETLSLSCTVSNDS RPSDHSWTWVRQSPGKALEWIGDIHYNGATTYNPSLRSRVRIELDQSIPRFSLKMTSMTAADTGMYYCARNAI RIYGVVALGEWFHYGMDVWGQGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSG ALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQ DWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQ PENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 52 (D1m-K8C-G99C_4xG4S_bNAb4-HC) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSGGGGSGGGGSGGGGSQVQLQESGPGLVKPSETLSVTCSVSGDS MNNYYWTWIRQSPGKGLEWIGYISDRESATYNPSLNSRVVISRDTSKNQLSLKLNSVTPADTAVYYCATARRGQ RIYGVVSFGEFFYYYSMDVWGKGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGA LTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGP SVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQD WLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQP ENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 53 (D1m-K8C-G99C_Fc) KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSGGGGSGGGGSGGGGSDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK SEQ ID NO: 54 (V3 loop) CTRPNNNTRKSIHIGPGRAFYTTGEIIGDIRQAHC SEQ ID NO: 55 (Exemplary gp160) MKVMGTKKNYQHLWRWGIMLLGMLMMSSAAEQLWVTVYYGVPVWREANTTLFCASDAKAYDTEVHNVWAT HACVPTDPNPQEVVMGNVTEDFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLHCTNVTISSTNGSTA NVTMREEMKNCSFNTTTVIRDKIQKEYALFYKLDIVPIEGKNTNTSYRLINCNTSVITQACPKVSFEPIPIHYCAPA GFAILKCNNKTFNGKGPCRNVSTVQCTHGIKPVVSTQLLLNGSLAEEDIIIRSENFTNNGKNIIVQLKEPVKINCTR PGNNTRRSINIGPGRAFYATGAIIGDIRKAHCNISTEQWNNTLTQIVDKLREQFGNKTIIFNQSSGGDPEVVMHT FNCGGEFFYCNSTQLFNSTWFNNGTSTWNSTADNITLPCRIKQVINMWQEVGKAMYAPPIRGQIDCSSNITGLI LTRDGGSNSSQNETFRPGGGNMKDNWRSELYKYKVVKIEPLGIAPTRAKRRVVQREKRAVTLGAVFLGFLGAAG STMGAASLTLTVQARLLLSGIVQQQSNLLRAIEAQQHMLQLTVWGIKQLQARVLAIERYLKDQQLLGIWGCSGK LICTTTVPWNTSWSNKSYDYIWNNMTWMQWEREIDNYTGFIYTLIEESQNQQEKNELELLELDKWASLWNWF NITNWLWYIKLFIMIIGGLVGLRIVCAVLSIVNRVRQGYSPLSFQTRLPNPRGPDRPEETEGEGGERDRDRSARLV NGFLAIIWDDLRSLCLFSYHRLRDLLLIVARVVEILGRRGWEILKYWWNLLKYWSQELKNSAVSLLNVTAIAVAE GTDRVIEIVQRAVRAILHIPTRIRQGFERALL SEQ ID NO: 56 (Exemplary AEQLWVIVYYGVPVWREANTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVMGNVTEDFNMWKNNMV EQMHEDIISLWDQSLKPCVKLTPLCVTLHCTNVTISSTNGSTANVTMREEMKNCSFNTTTVIRDKIQKEYALFYK LDIVPIEGKNTNTSYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGKGPCRNVSTVQCTHGIKP VVSTQLLLNGSLAEEDIIIRSENFTNNGKNIIVQLKEPVKINCTRPGNNTRRSINIGPGRAFYATGAIIGDIRKAHC NISTEQWNNTLTQIVDKLREQFGNKTIIFNQSSGGDPEVVMHTFNCGGEFFYCNSTQLFNSTWFNNGTSTWNS TADNITLPCRIKQVINMWQEVGKAMYAPPIRGQIDCSSNITGLILTRDGGSNSSQNETFRPGGGNMKDNWRSE LYKYKVVKIEPLGIAPTRAKRRVVQREKR SEQ ID NO: 57 (Exemplary AVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVER YLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNE QELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEG IEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQEL KNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL SEQ ID NO: 58 Apex CTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSC _{SEQ ID NO: 59 Interface} SDAKAYDTVPTDPNPQTKAKRRVVNASWSNKSLEQIWN _{SEQ ID NO: 60 PGT151 interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSRVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGK GLEWVAAISGDAWHVVYSNSVQGRFLVSRDNVKNTLYLEMNSLKIEDTAVYRCARMFQESGPPRLDRWSGRNY YYYSGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 61 PGT152 interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSRVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGK GLEWVAAISADAWHVVYSGSVQGRFLVSRDNSKNILYLEMNTLKIEDTAVYRCARMFQESGPPRFDSWSGRNY YYYSGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 62 PGT153 interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVESGGGVVQPGKSLRLSCVVSNFLFNKRHMHWVRQAPGK GLEWIAVISSDAIHVDYASSVRGRSLISRDNSKNSLYLDMNNLKIEDTATYYCARDRDGYGPPQIQTWSGRYLHL YSGIDAWGLGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTL MISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVS NKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDS DGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 63 PGT154 interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVESGGGVVQPGKSLRLSCVVSNFIFNKYPMYWVRQAPGK GLEWVAAISADAWHVDYAASVKDRFLISRDNSKNALYLEMNTLRVEDTGIYYCARNIEEFSVPQFDSWSGRSYY HYFGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 64 PGT155 interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVHLVESGGGVVQPGKSLRLSCETSGFIFNEYPMYWIRQAPGKG PEWVAAISADAWHVDYAGSVRGRFTVSRDNSKNSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNLY HYTGFDVWGPGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 65 PGT156 interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVHLVESGGGVVQPGKSLRLSCETSGFIFNQYPMYWVRQAPGK GPEWVAAISADAWHVDYPGSVRGRFTVSRDNSKSSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNL YHYTGFDVWGPGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPK DTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKC KVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 66 PGT157 interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVHLVESGGGVVQPGKSLRLSCVTSGFIFKQYPMYWIRQAPGKG LEWVAAISADAWHVDYAGSVRGRFTVSRDNSKNSLYLDMNSLTVEDTAIYFCAKDGEEHEVPQLHSWSGRNLY HYTGVDIWGPGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDT LMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKV SNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLD SDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 67 PGT158 interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVRLMESGGGVVQPGKSLRLSCVTSGFIFKKYPMYWIRQAPGKG LEWVAAISADAWHVDYPGSVRGRFTVSRDNSKNSLYLDMNSLTVEDTAIYFCAKDGEEHEVPQLHSWSGRNLY HYTGVDVWGPGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 68 8ANC195 interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQIHLVQSGTEVKKPGSSVTVSCKAYGVNTFGLYAVNWVRQAPG QSLEYIGQIWRWKSSASHHFRGRVLISAVDLTGSSPPISSLEIKNLTSDDTAVYFCTTTSTYDKWSGLHHDGVM AFSSWGQGTLISVSAASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMI SRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNK ALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSD GSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 69 35O22 interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQGQLVQSGAELKKPGASVKISCKTSGYRFNFYHINWIRQTAGRG PEWMGWISPYSGDKNLAPAFQDRVIMTTDTEVPVTSFTSTGAAYMEIRNLKFDDTGTYFCAKGLLRDGSSTWL PYLWGQGTLLTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMIS RTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKA LPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDG SFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 70 ACS202 interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVQLVESGGGVVQPGGSLRLSCAASGFAFKDFGMHWVRQAPGK GLEWVAVIGGGHGQHQSYSESVKGRFAITRDNEKNKLYLHMDRLRTEDTAVYYCAKDRLGRPWNIGGRLVYYY YGMDVWGQGTTATVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTL MISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVS NKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDS DGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 71 LN02 interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQAPLPESGPGVVRPTGTLSLTCTAAYGSISRHFWGWVRQSPQG TLEWIAHMHHLGVKYVNPSLKNRVSISMDTSKNQMSLTLKTVTATDAAKYHCVRMGARMSDIAFFSFGDWGPG SLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVV TVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCV VVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTI SKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLT VDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 72 CAP248-2B interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVQLQQSGPGLVKPSQTLSLTCNVYGVAISNEDYYWTWIRQHP GKGLEWIGDIYYNSGTTHYNPSLKSRASVSVDLSRNQFTLKVTSVTTADAAVYYCAREASTKITDDGGAFDFWG RGTMVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLS SVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEV TCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPI EKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLY SKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 73 3BC315 interface bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVQSGAEMKDPGASVKVSCRASGYKFTDYYMHWVRQAPG QGLEWVGWVNTNGGFTKYGAKFQGRVTVTRDTSTNTVFLELSRLTFGDTAMYFCARPMRPVSHGIDYSGLFVF QFWGRGTMVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMIS RTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKA LPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDG SFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 74 CAP256V2LS V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVESGGGVVQPGTSLRLSCAASQFRFDGYGMHWVRQAPG KGLEWVASISHDGIKKYHAEKVWGRFTISRDNSKNTLYLQMNSLRPEDTALYYCAKDLREDECEEWWSDYYDF GAQLPCAKSRGGLVGIADNWGQGTMVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSG ALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQ DWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQ PENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 75 PGDM1400 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQAQLVQSGPEVRKPGTSVKVSCKAPGNTLKTYDLHWVRSVPGQ GLQWMGWISHEGDKKVIVERFKAKVTIDWDRSTNTAYLQLSGLTSGDTAVYYCAKGSKHRLRDYALYDDDGAL NWAVDVDYLSNLEFWGQGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSG VHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFL FPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 76 PG9 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQRLVESGGGVVQPGSSLRLSCAASGFDFSRQGMHWVRQAPGQ GLEWVAFIKYDGSEKYHADSVWGRLSISRDNSKDTLYLQMNSLRVEDTATYFCVREAGGPDYRNGYYYYDFYD GYYNYHYMDVWGKGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTF PAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPK PKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEY KCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTT PPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 77 PG16 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQEQLVESGGGVVQPGGSLRLSCLASGFTFHKYGMHWVRQAPGK GLEWVALISDDGMRKYHSDSMWGRVTISRDNSKNTLYLQFSSLKVEDTAMFFCAREAGGPIWHDDVKYYDFN DGYYNYHYMDVWGKGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVH TFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFP PKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGK EYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYK TTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 78 PG20 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVRLVQSGPEVKKPGSSVTVSCQASGGTFSSYAFTWVRQAPGQ GLEWLGMVTPIFGEAKYSQRFEGRVTITADESTSTTSIELRGLTSEDTAIYYCARDRRAVPIATDNWLDPWGQG TLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVV TVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCV VVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTI SKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLT VDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 79 PGG14 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVLLVQSGTEVKKPGSSVKVSCQASGGAFSSYAFSWVRQAPGQ GLEWMGMITPVFGETKYAPRFQGRLTLTAEESLSTTYMELRSLTSDDTAFYYCTRDRRVVPMATDNWLDPWGQ GTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSV VTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTC VVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEK TISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSK LTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 80 PGC14 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSDGHLVQSGVEVKKTGATVKISCKVSGYSFIDYYLHWVQRAPGKG LEWVGLIDPENGEARYAEKFQGRVTIIADTSIDTGYMEMRSLKSEDTAVYFCAAGAVGADSGSWFDPWGQGTL VTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTV PSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVV DVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISK AKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVD KSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 81 CH01 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVQLVESGANVVRPGGSLRLSCKASGFIFENFGFSWVRQAPGKG LQWVAGLNWNGGDTRYADSVKGRFRMSRDNSRNFVYLDMDKVGVDDTAFYYCARGTDYTIDDAGIHYQGSG TFWYFDLWGRGTLVSVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDT LMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKV SNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLD SDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 82 CH02 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVQLVESGGSVVRPGGSLRLSCRASGFIFENYGLTWVRQVPGKG LHWVSGMNWNGGDTRYADSVRGRFSMSRDNSNNIAYLQMNNLRVEDTALYYCARGTDYTIDDQGRFYQGSG TFWYFDFWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKD TLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCK VSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 83 CH03 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVQLVESGGGVVRPGGSLRLSCAASGFIFENYGLTWVRQVPGKG LHWVSGMNWNGGDTRYADSVRGRFSMSRDNSNNIAYLQMKNLRVDDTALYYCARGTDYTIDDQGIFYKGSGT FWYFDLWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDT LMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKV SNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLD SDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 84 CH04 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSEVQLVESGGGLIRPGGSLRLSCKGSGFIFENFGFGWVRQGPGKG LEWVSGTNWNGGDSRYGDSVKGRFTISRDNSNNFVYLQMNSLRPEDTAIYYCARGTDYTIDDQGIRYQGSGTF WYFDVWGRGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTL MISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVS NKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDS DGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 85 PGT141 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVQSGPEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQ GLEWVGWMSHEGDKTESAQRFKGRVTFTRDTSASTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLI NYQEWNDYLEFLDVWGHGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSG VHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFL FPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 86 PGT142 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVQSGPEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQ GLEWVGWISHERDKTESAQRFKGRVTFTRDTSATTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLIN YQEWNDYLEFLDVWGHGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGV HTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLF PPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNG KEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNY KTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 87 PGT143 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLEQSGAEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQ GLEWVGWMSHEGDKTESAQRFKGRVTFTRDTSASTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLI NYQEWNDYLEFLDVWGHGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSG VHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFL FPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 88 PGT144 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVQSGAEVKKPGSSVKVSCKASGNTFRKYDVHWVRQATGQ GLEWVGWMSHEGDKTESAQRFKGRVSFTRDNSASTAYIELRGLTSDDTAIYYCTGGSKHRLRDYVLYDDYGLI NQQEWNDYLEFLDVWGHGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTS GVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVF LFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 89 PGT145 V1/V2 apex bispecific} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQVQLVQSGAEVKKPGSSVKVSCKASGNSFSNHDVHWVRQATG QGLEWMGWMSHEGDKTGLAQKFQGRVTITRDSGASTVYMELRGLTADDTAIYYCLTGSKHRLRDYFLYNEYGP NYEEWGDYLATLDVWGHGTAVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSG VHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFL FPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLN GKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENN YKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 90 PGT151 (Interface-bNAb17) CDRH1} KYPMY _{SEQ ID NO: 91 PGT151 (Interface-bNAb17) CDRH2} AISGDAWHVVYSNSVQG _{SEQ ID NO: 92 PGT151 (Interface-bNAb17) CDRH3} MFQESGPPRLDRWSGRNYYYYSGMDV _{SEQ ID NO: 93 PGT151 (Interface-bNAb17) CDRL1} KSSESLRQSNGKTSLY _{SEQ ID NO: 94 PGT151 (Interface-bNAb17) CDRL2} EVSNRFS _{SEQ ID NO: 95 PGT151 (Interface-bNAb17) CDRL3} MQSKDFPLT _{SEQ ID NO: 96 PGT151 (Interface-bNAb17) VH} RVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGKGLEWVAAISGDAWHVVYSNSVQGRFLVSR DNVKNTLYLEMNSLKIEDTAVYRCARMFQESGPPRLDRWSGRNYYYYSGMDVWGQGTTVTVSS _{SEQ ID NO: 97 PGT151 (Interface-bNAb17) VL} DIVMTQTPLSLSVTPGQPASISCKSSESLRQSNGKTSLYWYRQKPGQSPQLLVFEVSNRFSGVSDRFVGSGSGT DFTLRISRVEAEDVGFYYCMQSKDFPLTFGGGTKVDLK _{SEQ ID NO: 98 PGT151 (Interface-bNAb17) HC (no LS)} RVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGKGLEWVAAISGDAWHVVYSNSVQGRFLVSR DNVKNTLYLEMNSLKIEDTAVYRCARMFQESGPPRLDRWSGRNYYYYSGMDVWGQGTTVTVSSASTKGPSVFP LAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV MHEALHNHYTQKSLSLSPGK _{SEQ ID NO: 99 PGT151 (Interface-bNAb17) HC} RVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGKGLEWVAAISGDAWHVVYSNSVQGRFLVSR DNVKNTLYLEMNSLKIEDTAVYRCARMFQESGPPRLDRWSGRNYYYYSGMDVWGQGTTVTVSSASTKGPSVFP LAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV LHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 100 PGT151 (Interface-bNAb17) LC} DIVMTQTPLSLSVTPGQPASISCKSSESLRQSNGKTSLYWYRQKPGQSPQLLVFEVSNRFSGVSDRFVGSGSGT DFTLRISRVEAEDVGFYYCMQSKDFPLTFGGGTKVDLKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 101 PGT152 (Interface-bNAb18) CDRH1} KYPMY _{SEQ ID NO: 102 PGT152 (Interface-bNAb18) CDRH2} AISADAWHVVYSGSVQG _{SEQ ID NO: 103 PGT152 (Interface-bNAb18) CDRH3} MFQESGPPRFDSWSGRNYYYYSGMDV _{SEQ ID NO: 104 PGT152 (Interface-bNAb18) CDRL1} KSSQSLRQSNGKTSLY _{SEQ ID NO: 105 PGT152 (Interface-bNAb18) CDRL2} EVSNRFS _{SEQ ID NO: 106 PGT152 (Interface-bNAb18) CDRL3} MQSKDFPLT _{SEQ ID NO: 107 PGT152 (Interface-bNAb18) VH} RVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGKGLEWVAAISADAWHVVYSGSVQGRFLVSR DNSKNILYLEMNTLKIEDTAVYRCARMFQESGPPRFDSWSGRNYYYYSGMDVWGQGTTVTVSS _{SEQ ID NO: 108 PGT152 (Interface-bNAb18) VL} DIVMTQTPLSLSVDPGQPASISCKSSQSLRQSNGKTSLYWYQQKPGQSPQLLIFEVSNRFSGVSDRFVGSGSGT DFTLRISRVEAEDVGFYYCMQSKDFPLTFGGGTKVDLN _{SEQ ID NO: 109 PGT152 (Interface-bNAb18) HC (no LS)} RVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGKGLEWVAAISADAWHVVYSGSVQGRFLVSR DNSKNILYLEMNTLKIEDTAVYRCARMFQESGPPRFDSWSGRNYYYYSGMDVWGQGTTVTVSSASTKGPSVFP LAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV MHEALHNHYTQKSLSLSPGK _{SEQ ID NO: 110 PGT152 (Interface-} RVQLVESGGGVVQPGKSVRLSCVVSDFPFSKYPMYWVRQAPGKGLEWVAAISADAWHVVYSGSVQGRFLVSR DNSKNILYLEMNTLKIEDTAVYRCARMFQESGPPRFDSWSGRNYYYYSGMDVWGQGTTVTVSSASTKGPSVFP LAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV LHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 111 PGT152 (Interface-bNAb18) LC} DIVMTQTPLSLSVDPGQPASISCKSSQSLRQSNGKTSLYWYQQKPGQSPQLLIFEVSNRFSGVSDRFVGSGSGT DFTLRISRVEAEDVGFYYCMQSKDFPLTFGGGTKVDLNRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 112 PGT153 (Interface-bNAb19) CDRH1} KRHMH _{SEQ ID NO: 113 PGT153 (Interface-bNAb19) CDRH2} VISSDAIHVDYASSVRG _{SEQ ID NO: 114 PGT153 (Interface-bNAb19) CDRH3} DRDGYGPPQIQTWSGRYLHLYSGIDA _{SEQ ID NO: 115 PGT153 (Interface-bNAb19) CDRL1} KSSQSLRQSNGKTYLY DIVLTQSPLFLSVSPGQPASISCKSSQSLRQSNGKTYLYWYVQKSGQSPQPLIQEVSIRFSGVPGRFAGSGSGTD FTLKISRVEAEDVGVYFCMQSKDFPLTFGGGTKVDLN _{SEQ ID NO: 120 PGT153 (Interface-bNAb19) HC (no LS)} QVQLVESGGGVVQPGKSLRLSCVVSNFLFNKRHMHWVRQAPGKGLEWIAVISSDAIHVDYASSVRGRSLISRDN SKNSLYLDMNNLKIEDTATYYCARDRDGYGPPQIQTWSGRYLHLYSGIDAWGLGTTVTVSSASTKGPSVFPLAP SSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHK PSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVD GVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR DELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM HEALHNHYTQKSLSLSPGK _{SEQ ID NO: 121 PGT153 (Interface-bNAb19) HC} QVQLVESGGGVVQPGKSLRLSCVVSNFLFNKRHMHWVRQAPGKGLEWIAVISSDAIHVDYASSVRGRSLISRDN SKNSLYLDMNNLKIEDTATYYCARDRDGYGPPQIQTWSGRYLHLYSGIDAWGLGTTVTVSSASTKGPSVFPLAP SSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHK PSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVD GVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR DELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLH EALHSHYTQKSLSLSPGK _{SEQ ID NO: 122 PGT153 (Interface-bNAb19) LC} DIVLTQSPLFLSVSPGQPASISCKSSQSLRQSNGKTYLYWYVQKSGQSPQPLIQEVSIRFSGVPGRFAGSGSGTD FTLKISRVEAEDVGVYFCMQSKDFPLTFGGGTKVDLNRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKV QWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 123 PGT154 (Interface-bNAb20) CDRH1} KYPMY _{SEQ ID NO: 124 PGT154 (Interface-bNAb20) CDRH2} AISADAWHVDYAASVKD _{SEQ ID NO: 125 PGT154 (Interface-bNAb20) CDRH3} NIEEFSVPQFDSWSGRSYYHYFGMDV _{SEQ ID NO: 126 PGT154 (Interface-bNAb20) CDRL1} SSSESLGRGDGRTYLH _{SEQ ID NO: 127 PGT154 (Interface-bNAb20) CDRL2} EVSTRFS _{SEQ ID NO: 128 PGT154 (Interface-bNAb20) CDRL3} MQSRDFPIT _{SEQ ID NO: 129 PGT154 (Interface-bNAb20) VH} QVQLVESGGGVVQPGKSLRLSCVVSNFIFNKYPMYWVRQAPGKGLEWVAAISADAWHVDYAASVKDRFLISRD NSKNALYLEMNTLRVEDTGIYYCARNIEEFSVPQFDSWSGRSYYHYFGMDVWGQGTTVTVSS _{SEQ ID NO: 130 PGT154 (Interface-bNAb20) VL} DIVMTQTPVSLSVSLGQAASISCSSSESLGRGDGRTYLHWYRQKPGQTPQLLMYEVSTRFSGVSDRFAGSGSRT QFTLKISRVEAEDVGVYYCMQSRDFPITFGGGTRVDLK _{SEQ ID NO: 131 PGT154 (Interface-bNAb20) HC (no LS)} QVQLVESGGGVVQPGKSLRLSCVVSNFIFNKYPMYWVRQAPGKGLEWVAAISADAWHVDYAASVKDRFLISRD NSKNALYLEMNTLRVEDTGIYYCARNIEEFSVPQFDSWSGRSYYHYFGMDVWGQGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM HEALHNHYTQKSLSLSPGK _{SEQ ID NO: 132 PGT154 (Interface-bNAb20) HC (LS)} QVQLVESGGGVVQPGKSLRLSCVVSNFIFNKYPMYWVRQAPGKGLEWVAAISADAWHVDYAASVKDRFLISRD NSKNALYLEMNTLRVEDTGIYYCARNIEEFSVPQFDSWSGRSYYHYFGMDVWGQGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVL HEALHSHYTQKSLSLSPGK _{SEQ ID NO: 133 PGT154 (Interface-bNAb20) LC} DIVMTQTPVSLSVSLGQAASISCSSSESLGRGDGRTYLHWYRQKPGQTPQLLMYEVSTRFSGVSDRFAGSGSRT QFTLKISRVEAEDVGVYYCMQSRDFPITFGGGTRVDLKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 134 PGT155 (Interface-bNAb21) CDRH1} EYPMY _{SEQ ID NO: 135 PGT155 (Interface-bNAb21) CDRH2} AISADAWHVDYAGSVRG _{SEQ ID NO: 136 PGT155 (Interface-bNAb21) CDRH3} DGEEHKVPQLHSWSGRNLYHYTGFDV _{SEQ ID NO: 137 PGT155 (Interface-bNAb21) CDRL1} KSSQSVRQSDGKTFLY QVHLVESGGGVVQPGKSLRLSCETSGFIFNEYPMYWIRQAPGKGPEWVAAISADAWHVDYAGSVRGRFTVSRD NSKNSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNLYHYTGFDVWGPGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM HEALHNHYTQKSLSLSPGK QVHLVESGGGVVQPGKSLRLSCETSGFIFNEYPMYWIRQAPGKGPEWVAAISADAWHVDYAGSVRGRFTVSRD NSKNSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNLYHYTGFDVWGPGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVL HEALHSHYTQKSLSLSPGK DIVMTQSPVSLSVTLGQPASMSCKSSQSVRQSDGKTFLYWYRQKPGQSPQLLIYEGSSRFSGVSDRISGSGSGT DFTLRISRVEAEDAGVYFCLQTKDFPLTFGGGTRVDLKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 145 PGT156 (Interface-bNAb22) CDRH1} QYPMY _{SEQ ID NO: 146 PGT156 (Interface-bNAb22) CDRH2} AISADAWHVDYPGSVRG _{SEQ ID NO: 147 PGT156 (Interface-bNAb22) CDRH3} DGEEHKVPQLHSWSGRNLYHYTGFDV _{SEQ ID NO: 148 PGT156 (Interface-bNAb22) CDRL1} KSSQTVRQSDGKTFLY _{SEQ ID NO: 149 PGT156 (Interface-bNAb22) CDRL2} EGSNRFS _{SEQ ID NO: 150 PGT156 (Interface-bNAb22) CDRL3} LQTKDFPLT _{SEQ ID NO: 151 PGT156 (Interface-bNAb22) VH} QVHLVESGGGVVQPGKSLRLSCETSGFIFNQYPMYWVRQAPGKGPEWVAAISADAWHVDYPGSVRGRFTVSR DNSKSSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNLYHYTGFDVWGPGTTVTVSS _{SEQ ID NO: 152 PGT156 (Interface-bNAb22) VL} DIVMTQSPVSLSVTLGQPASMSCKSSQTVRQSDGKTFLYWYRQKAGQSPQLLIYEGSNRFSGVSDRISGSGSGT DFTLRISRVEAEDVGVYFCLQTKDFPLTFGGGTRVDIK _{SEQ ID NO: 153 PGT156 (Interface-bNAb22) HC (no LS)} QVHLVESGGGVVQPGKSLRLSCETSGFIFNQYPMYWVRQAPGKGPEWVAAISADAWHVDYPGSVRGRFTVSR DNSKSSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNLYHYTGFDVWGPGTTVTVSSASTKGPSVFPL APSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV MHEALHNHYTQKSLSLSPGK _{SEQ ID NO: 154 PGT156 (Interface-bNAb22) HC} QVHLVESGGGVVQPGKSLRLSCETSGFIFNQYPMYWVRQAPGKGPEWVAAISADAWHVDYPGSVRGRFTVSR DNSKSSLYLDMKSLKVEDTAIYFCAKDGEEHKVPQLHSWSGRNLYHYTGFDVWGPGTTVTVSSASTKGPSVFPL APSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVN HKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWY VDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPP SRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSV LHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 155 PGT156 (Interface-bNAb22) LC} DIVMTQSPVSLSVTLGQPASMSCKSSQTVRQSDGKTFLYWYRQKAGQSPQLLIYEGSNRFSGVSDRISGSGSGT DFTLRISRVEAEDVGVYFCLQTKDFPLTFGGGTRVDIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 156 PGT157 (Interface-bNAb23) CDRH1} QYPMY _{SEQ ID NO: 157 PGT157 (Interface-bNAb23) CDRH2} AISADAWHVDYAGSVRG _{SEQ ID NO: 158 PGT157 (Interface-bNAb23) CDRH3} DGEEHEVPQLHSWSGRNLYHYTGVDI _{SEQ ID NO: 159 PGT157 (Interface-bNAb23) CDRL1} KSSQSLRQSDGKTFLY _{SEQ ID NO: 160 PGT157 (Interface-bNAb23) CDRL2} EASNRFS _{SEQ ID NO: 161 PGT157 (Interface-bNAb23) CDRL3} MQTKDFPLT _{SEQ ID NO: 162 PGT157 (Interface-bNAb23) VH} EVHLVESGGGVVQPGKSLRLSCVTSGFIFKQYPMYWIRQAPGKGLEWVAAISADAWHVDYAGSVRGRFTVSRD NSKNSLYLDMNSLTVEDTAIYFCAKDGEEHEVPQLHSWSGRNLYHYTGVDIWGPGTTVTVSS _{SEQ ID NO: 163 PGT157 (Interface-bNAb23) VL} DIVMTQTPVSLSVTLGQPASMSCKSSQSLRQSDGKTFLYWYRQKAGQSPQLLISEASNRFSGVSDRFSGSGSGT DFTLKISRVEAEDVGIYFCMQTKDFPLTFGGGTKVDLK _{SEQ ID NO: 164 PGT157 (Interface-bNAb23) HC (no LS)} EVHLVESGGGVVQPGKSLRLSCVTSGFIFKQYPMYWIRQAPGKGLEWVAAISADAWHVDYAGSVRGRFTVSRD NSKNSLYLDMNSLTVEDTAIYFCAKDGEEHEVPQLHSWSGRNLYHYTGVDIWGPGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM HEALHNHYTQKSLSLSPGK _{SEQ ID NO: 165 PGT157 (Interface-bNAb23) HC (LS)} EVHLVESGGGVVQPGKSLRLSCVTSGFIFKQYPMYWIRQAPGKGLEWVAAISADAWHVDYAGSVRGRFTVSRD NSKNSLYLDMNSLTVEDTAIYFCAKDGEEHEVPQLHSWSGRNLYHYTGVDIWGPGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVL HEALHSHYTQKSLSLSPGK _{SEQ ID NO: 166 PGT157 (Interface-bNAb23) LC} DIVMTQTPVSLSVTLGQPASMSCKSSQSLRQSDGKTFLYWYRQKAGQSPQLLISEASNRFSGVSDRFSGSGSGT DFTLKISRVEAEDVGIYFCMQTKDFPLTFGGGTKVDLKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 167 PGT158 (Interface-bNAb24) CDRH1} KYPMY _{SEQ ID NO: 168 PGT158 (Interface-bNAb24) CDRH2} AISADAWHVDYPGSVRG _{SEQ ID NO: 169 PGT158 (Interface-bNAb24) CDRH3} DGEEHEVPQLHSWSGRNLYHYTGVDV _{SEQ ID NO: 170 PGT158 (Interface-bNAb24) CDRL1} KSSQSVRQSDGKTFLY _{SEQ ID NO: 171 PGT158 (Interface-bNAb24) CDRL2} EASKRFS _{SEQ ID NO: 172 PGT158 (Interface-bNAb24) CDRL3} MQTKDFPLT _{SEQ ID NO: 173 PGT158 (Interface-bNAb24) VH} EVRLMESGGGVVQPGKSLRLSCVTSGFIFKKYPMYWIRQAPGKGLEWVAAISADAWHVDYPGSVRGRFTVSRD NSKNSLYLDMNSLTVEDTAIYFCAKDGEEHEVPQLHSWSGRNLYHYTGVDVWGPGTTVTVSS _{SEQ ID NO: 174 PGT158 (Interface-bNAb24) VL} DIVMTQTPVSVSVTLGQPASMSCKSSQSVRQSDGKTFLYWYRQKAGQSPQLLIYEASKRFSGVSDRFSGSGSGT DFTLKISRVGAEDVGVYFCMQTKDFPLTFGGGTKVDLK _{SEQ ID NO: 175 PGT158 (Interface-bNAb24) HC (no LS)} EVRLMESGGGVVQPGKSLRLSCVTSGFIFKKYPMYWIRQAPGKGLEWVAAISADAWHVDYPGSVRGRFTVSRD NSKNSLYLDMNSLTVEDTAIYFCAKDGEEHEVPQLHSWSGRNLYHYTGVDVWGPGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM HEALHNHYTQKSLSLSPGK _{SEQ ID NO: 176 PGT158 (Interface-bNAb24) HC} EVRLMESGGGVVQPGKSLRLSCVTSGFIFKKYPMYWIRQAPGKGLEWVAAISADAWHVDYPGSVRGRFTVSRD NSKNSLYLDMNSLTVEDTAIYFCAKDGEEHEVPQLHSWSGRNLYHYTGVDVWGPGTTVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVL HEALHSHYTQKSLSLSPGK _{SEQ ID NO: 177 PGT158 (Interface-bNAb24) LC} DIVMTQTPVSVSVTLGQPASMSCKSSQSVRQSDGKTFLYWYRQKAGQSPQLLIYEASKRFSGVSDRFSGSGSGT DFTLKISRVGAEDVGVYFCMQTKDFPLTFGGGTKVDLKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 178 8ANC195 (Interface-bNAb25) CDRH1} GLYAVN _{SEQ ID NO: 179 8ANC195 (Interface-bNAb25) CDRH2} QIWRWKSSASHHFRGRVLI _{SEQ ID NO: 180 8ANC195 (Interface-bNAb25) CDRH3} TSTYDKWSGLHHDGVMAFSS _{SEQ ID NO: 181 8ANC195 (Interface-bNAb25) CDRL1} RASQSITGNWVA _{SEQ ID NO: 182 8ANC195 (Interface-bNAb25) CDRL2} RGAALLG _{SEQ ID NO: 183 8ANC195 (Interface-bNAb25) CDRL3} QQYDTYPGT _{SEQ ID NO: 184 8ANC195 (Interface-bNAb25) VH} QIHLVQSGTEVKKPGSSVTVSCKAYGVNTFGLYAVNWVRQAPGQSLEYIGQIWRWKSSASHHFRGRVLISAVDL TGSSPPISSLEIKNLTSDDTAVYFCTTTSTYDKWSGLHHDGVMAFSSWGQGTLISVSA _{SEQ ID NO: 185 8ANC195 (Interface-bNAb25) VL} DIQMTQSPSTLSASIGDTVRISCRASQSITGNWVAWYQQRPGKAPRLLIYRGAALLGGVPSRFSGSAAGTDFTLT IGNLQAEDFGTFYCQQYDTYPGTFGQGTKVEVK _{SEQ ID NO: 186 8ANC195 (Interface-bNAb25) HC (no LS)} QIHLVQSGTEVKKPGSSVTVSCKAYGVNTFGLYAVNWVRQAPGQSLEYIGQIWRWKSSASHHFRGRVLISAVDL TGSSPPISSLEIKNLTSDDTAVYFCTTTSTYDKWSGLHHDGVMAFSSWGQGTLISVSAASTKGPSVFPLAPSSKS TSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNT KVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEV HNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELT KNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEAL HNHYTQKSLSLSPGK _{SEQ ID NO: 187 8ANC195 (Interface-bNAb25) HC} QIHLVQSGTEVKKPGSSVTVSCKAYGVNTFGLYAVNWVRQAPGQSLEYIGQIWRWKSSASHHFRGRVLISAVDL TGSSPPISSLEIKNLTSDDTAVYFCTTTSTYDKWSGLHHDGVMAFSSWGQGTLISVSAASTKGPSVFPLAPSSKS TSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNT KVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEV HNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELT KNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALH SHYTQKSLSLSPGK _{SEQ ID NO: 188 8ANC195 (Interface-bNAb25) LC} DIQMTQSPSTLSASIGDTVRISCRASQSITGNWVAWYQQRPGKAPRLLIYRGAALLGGVPSRFSGSAAGTDFTLT IGNLQAEDFGTFYCQQYDTYPGTFGQGTKVEVKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQW KVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 189 35O22 (Interface-bNAb26) CDRH1} FYHIN _{SEQ ID NO: 190 35O22 (Interface-bNAb26) CDRH2} WISPYSGDKNLAPAFQD _{SEQ ID NO: 191 35O22 (Interface-bNAb26) CDRH3} GLLRDGSSTWLPYL _{SEQ ID NO: 192 35O22 (Interface-bNAb26) CDRL1} TGPNSVCCSHKSIS _{SEQ ID NO: 193 35O22 (Interface-bNAb26) CDRL2} EDNERAP _{SEQ ID NO: 194 35O22 (Interface-bNAb26) CDRL3} CSYTHNSGCV _{SEQ ID NO: 195 35O22 (Interface-bNAb26) VH} QGQLVQSGAELKKPGASVKISCKTSGYRFNFYHINWIRQTAGRGPEWMGWISPYSGDKNLAPAFQDRVIMTTD TEVPVTSFTSTGAAYMEIRNLKFDDTGTYFCAKGLLRDGSSTWLPYLWGQGTLLTVSS _{SEQ ID NO: 196 35O22 (Interface-bNAb26) VL} QSVLTQSASVSGSLGQSVTISCTGPNSVCCSHKSISWYQWPPGRAPTLIIYEDNERAPGISPRFSGYKSYWSAYL TISDLRPEDETTYYCCSYTHNSGCVFGTGTKVSVL _{SEQ ID NO: 197 35O22 (Interface-bNAb26) HC (no LS)} QGQLVQSGAELKKPGASVKISCKTSGYRFNFYHINWIRQTAGRGPEWMGWISPYSGDKNLAPAFQDRVIMTTD TEVPVTSFTSTGAAYMEIRNLKFDDTGTYFCAKGLLRDGSSTWLPYLWGQGTLLTVSSASTKGPSVFPLAPSSKS TSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNT KVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEV HNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELT KNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEAL HNHYTQKSLSLSPGK _{SEQ ID NO: 198 35O22 (Interface-bNAb26) HC (LS)} QGQLVQSGAELKKPGASVKISCKTSGYRFNFYHINWIRQTAGRGPEWMGWISPYSGDKNLAPAFQDRVIMTTD TEVPVTSFTSTGAAYMEIRNLKFDDTGTYFCAKGLLRDGSSTWLPYLWGQGTLLTVSSASTKGPSVFPLAPSSKS TSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNT KVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEV HNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELT KNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALH SHYTQKSLSLSPGK _{SEQ ID NO: 199 35O22 (Interface-bNAb26) LC} QSVLTQSASVSGSLGQSVTISCTGPNSVCCSHKSISWYQWPPGRAPTLIIYEDNERAPGISPRFSGYKSYWSAYL TISDLRPEDETTYYCCSYTHNSGCVFGTGTKVSVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVA WKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS _{SEQ ID NO: 200 ACS202 (Interface-bNAb27) CDRH1} DFGMH _{SEQ ID NO: 201 ACS202 (Interface-bNAb27) CDRH2} VIGGGHGQHQSYSESVKG _{SEQ ID NO: 202 ACS202 (Interface-bNAb27) CDRH3} DRLGRPWNIGGRLVYYYYGMDV _{SEQ ID NO: 203 ACS202 (Interface-bNAb27) CDRL1} QASQDIKKSLN _{SEQ ID NO: 204 ACS202 (Interface-bNAb27) CDRL2} DASILQT _{SEQ ID NO: 205 ACS202 (Interface-bNAb27) CDRL3} QEYENLQFT _{SEQ ID NO: 206 ACS202 (Interface-bNAb27) VH} EVQLVESGGGVVQPGGSLRLSCAASGFAFKDFGMHWVRQAPGKGLEWVAVIGGGHGQHQSYSESVKGRFAIT RDNEKNKLYLHMDRLRTEDTAVYYCAKDRLGRPWNIGGRLVYYYYGMDVWGQGTTATVSS _{SEQ ID NO: 207 ACS202 (Interface-bNAb27) VL} DIRMTQAPVSLSASVGDRVTITCQASQDIKKSLNWYRQKPSKAPELLIHDASILQTGVPSAFTASGSGTHFSFVIN KLQPEDVGTYFCQEYENLQFTFGPGTKVNIK _{SEQ ID NO: 208 ACS202 (Interface-bNAb27) HC (no LS)} EVQLVESGGGVVQPGGSLRLSCAASGFAFKDFGMHWVRQAPGKGLEWVAVIGGGHGQHQSYSESVKGRFAIT RDNEKNKLYLHMDRLRTEDTAVYYCAKDRLGRPWNIGGRLVYYYYGMDVWGQGTTATVSSASTKGPSVFPLAP SSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHK PSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVD GVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR DELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM HEALHNHYTQKSLSLSPGK _{SEQ ID NO: 209 ACS202 (Interface-bNAb27) HC} EVQLVESGGGVVQPGGSLRLSCAASGFAFKDFGMHWVRQAPGKGLEWVAVIGGGHGQHQSYSESVKGRFAIT RDNEKNKLYLHMDRLRTEDTAVYYCAKDRLGRPWNIGGRLVYYYYGMDVWGQGTTATVSSASTKGPSVFPLAP SSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHK PSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVD GVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR DELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLH EALHSHYTQKSLSLSPGK _{SEQ ID NO: 210 ACS202 (Interface-bNAb27) LC} DIRMTQAPVSLSASVGDRVTITCQASQDIKKSLNWYRQKPSKAPELLIHDASILQTGVPSAFTASGSGTHFSFVIN KLQPEDVGTYFCQEYENLQFTFGPGTKVNIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVD NALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 211 LN02 (Interface-bNAb29) CDRH1} RHFWG _{SEQ ID NO: 212 LN02 (Interface-bNAb29) CDRH2} HMHHLGVKYVNPSLKN _{SEQ ID NO: 213 LN02 (Interface-bNAb29) CDRH3} MGARMSDIAFFSFGD _{SEQ ID NO: 214 LN02 (Interface-bNAb29) CDRL1} WGYYMGSKPVN _{SEQ ID NO: 215 LN02 (Interface-bNAb29) CDRL2} YDDERDS _{SEQ ID NO: 216 LN02 (Interface-bNAb29) CDRL3} QVWDSKYEEIY _{SEQ ID NO: 217 LN02 (Interface-bNAb29) VH} QAPLPESGPGVVRPTGTLSLTCTAAYGSISRHFWGWVRQSPQGTLEWIAHMHHLGVKYVNPSLKNRVSISMDT SKNQMSLTLKTVTATDAAKYHCVRMGARMSDIAFFSFGDWGPGSLVTVSS _{SEQ ID NO: 218 LN02 (Interface-bNAb29) VL} SYVLGQSSSMSVAPGQTAKISCWGYYMGSKPVNWYQLKPGRAPSLIISYDDERDSGTPARFSGSHSGSTATLTI SNVVPADEADYFCQVWDSKYEEIYFGGGTALTVL _{SEQ ID NO: 219 LN02 (Interface-bNAb29) HC (no LS)} QAPLPESGPGVVRPTGTLSLTCTAAYGSISRHFWGWVRQSPQGTLEWIAHMHHLGVKYVNPSLKNRVSISMDT SKNQMSLTLKTVTATDAAKYHCVRMGARMSDIAFFSFGDWGPGSLVTVSSASTKGPSVFPLAPSSKSTSGGTAA LGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVE PKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKP REEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLT CLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQK SLSLSPGK _{SEQ ID NO: 220 LN02 (Interface-bNAb29) HC (LS)} QAPLPESGPGVVRPTGTLSLTCTAAYGSISRHFWGWVRQSPQGTLEWIAHMHHLGVKYVNPSLKNRVSISMDT SKNQMSLTLKTVTATDAAKYHCVRMGARMSDIAFFSFGDWGPGSLVTVSSASTKGPSVFPLAPSSKSTSGGTAA LGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVE PKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKP REEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLT CLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKS LSLSPGK _{SEQ ID NO: 221 LN02 (Interface-bNAb29) LC} SYVLGQSSSMSVAPGQTAKISCWGYYMGSKPVNWYQLKPGRAPSLIISYDDERDSGTPARFSGSHSGSTATLTI SNVVPADEADYFCQVWDSKYEEIYFGGGTALTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVA WKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS _{SEQ ID NO: 222 CAP248-2B (Interface-bNAb30) CDRH1} NEDYYWT _{SEQ ID NO: 223 CAP248-2B (Interface-bNAb30) CDRH2} DIYYNSGTTHYNPSLKS _{SEQ ID NO: 224 CAP248-2B (Interface-bNAb30) CDRH3} EASTKITDDGGAFDF _{SEQ ID NO: 225 CAP248-2B (Interface-bNAb30) CDRL1} TGTSSDIGGYKYVS _{SEQ ID NO: 226 CAP248-2B (Interface-bNAb30) CDRL2} DVIKRPS _{SEQ ID NO: 227 CAP248-2B (Interface-bNAb30) CDRL3} SSYTTKKTSFFGPATRAYV _{SEQ ID NO: 228 CAP248-2B (Interface-bNAb30) VH} EVQLQQSGPGLVKPSQTLSLTCNVYGVAISNEDYYWTWIRQHPGKGLEWIGDIYYNSGTTHYNPSLKSRASVSV DLSRNQFTLKVTSVTTADAAVYYCAREASTKITDDGGAFDFWGRGTMVTVSS _{SEQ ID NO: 229 CAP248-2B (Interface-bNAb30) VL} QSALTQPASVSGSPGQSISISCTGTSSDIGGYKYVSWYQQHPGRAPKLIIYDVIKRPSGISDRFSGSKSANTASLT ISGLQAGDEASYYCSSYTTKKTSFFGPATRAYVFGSGTQVTVL _{SEQ ID NO: 230 CAP248-2B (Interface-bNAb30) HC (no LS)} EVQLQQSGPGLVKPSQTLSLTCNVYGVAISNEDYYWTWIRQHPGKGLEWIGDIYYNSGTTHYNPSLKSRASVSV DLSRNQFTLKVTSVTTADAAVYYCAREASTKITDDGGAFDFWGRGTMVTVSSASTKGPSVFPLAPSSKSTSGGT AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKK VEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKT KPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVS LTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT QKSLSLSPGK _{SEQ ID NO: 231 CAP248-2B (Interface-bNAb30) HC} EVQLQQSGPGLVKPSQTLSLTCNVYGVAISNEDYYWTWIRQHPGKGLEWIGDIYYNSGTTHYNPSLKSRASVSV DLSRNQFTLKVTSVTTADAAVYYCAREASTKITDDGGAFDFWGRGTMVTVSSASTKGPSVFPLAPSSKSTSGGT AALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKK VEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKT KPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVS LTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQ KSLSLSPGK _{SEQ ID NO: 232 CAP248-2B (Interface-bNAb30) LC} QSALTQPASVSGSPGQSISISCTGTSSDIGGYKYVSWYQQHPGRAPKLIIYDVIKRPSGISDRFSGSKSANTASLT ISGLQAGDEASYYCSSYTTKKTSFFGPATRAYVFGSGTQVTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDF YPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS _{SEQ ID NO: 233 3BC315 (Interface-bNAb31) CDRH1} DYYMH _{SEQ ID NO: 234 3BC315 (Interface-bNAb31) CDRH2} WVNTNGGFTKYGAKFQG _{SEQ ID NO: 235 3BC315 (Interface-bNAb31) CDRH3} PMRPVSHGIDYSGLFVFQF _{SEQ ID NO: 236 3BC315 (Interface-bNAb31) CDRL1} SGTRSDVGGYDFVS _{SEQ ID NO: 237 3BC315 (Interface-bNAb31) CDRL2} EVTKRPS _{SEQ ID NO: 238 3BC315 (Interface-bNAb31) CDRL3} CSYANYDKLI _{SEQ ID NO: 239 3BC315 (Interface-bNAb31) VH} QVQLVQSGAEMKDPGASVKVSCRASGYKFTDYYMHWVRQAPGQGLEWVGWVNTNGGFTKYGAKFQGRVTVT RDTSTNTVFLELSRLTFGDTAMYFCARPMRPVSHGIDYSGLFVFQFWGRGTMVTVSS _{SEQ ID NO: 240 3BC315 (Interface-bNAb31) VL} QSALTQPASVSASPGQSITISCSGTRSDVGGYDFVSWYQQHPGKVPKLIIYEVTKRPSGIPQRFSGSKSGNTASL TISGLQADDEADYYCCSYANYDKLILGGGTKLTVL _{SEQ ID NO: 241 3BC315 (Interface-bNAb31) HC (no LS)} QVQLVQSGAEMKDPGASVKVSCRASGYKFTDYYMHWVRQAPGQGLEWVGWVNTNGGFTKYGAKFQGRVTVT RDTSTNTVFLELSRLTFGDTAMYFCARPMRPVSHGIDYSGLFVFQFWGRGTMVTVSSASTKGPSVFPLAPSSKST SGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTK VDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVH NAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTK NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALH NHYTQKSLSLSPGK _{SEQ ID NO: 242 3BC315 (Interface-bNAb30) HC} QVQLVQSGAEMKDPGASVKVSCRASGYKFTDYYMHWVRQAPGQGLEWVGWVNTNGGFTKYGAKFQGRVTVT RDTSTNTVFLELSRLTFGDTAMYFCARPMRPVSHGIDYSGLFVFQFWGRGTMVTVSSASTKGPSVFPLAPSSKST SGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTK VDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVH NAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTK NQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHS HYTQKSLSLSPGK _{SEQ ID NO: 243 3BC315 (Interface-bNAb30) LC} QSALTQPASVSASPGQSITISCSGTRSDVGGYDFVSWYQQHPGKVPKLIIYEVTKRPSGIPQRFSGSKSGNTASL TISGLQADDEADYYCCSYANYDKLILGGGTKLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVA WKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS _{SEQ ID NO: 244 CAP256V2LS (Apex-bNAb1) CDRH1} GYGMH _{SEQ ID NO: 245 CAP256V2LS (Apex-bNAb1) CDRH2} SISHDGIKKYHAEKVWG _{SEQ ID NO: 246 CAP256V2LS (Apex-bNAb1) CDRH3} DLREDECEEWWSDYYDFGAQLPCAKSRGGLVGIADN _{SEQ ID NO: 247 CAP256V2LS (Apex-bNAb1) CDRL1} SGNTSNIGNNFVS _{SEQ ID NO: 248 CAP256V2LS (Apex-bNAb1) CDRL2} ETDKRPS _{SEQ ID NO: 249 CAP256V2LS (Apex-bNAb1) CDRL3} ATWAASLSSARV _{SEQ ID NO: 250 CAP256V2LS (Apex-bNAb1) VH} QVQLVESGGGVVQPGTSLRLSCAASQFRFDGYGMHWVRQAPGKGLEWVASISHDGIKKYHAEKVWGRFTISR DNSKNTLYLQMNSLRPEDTALYYCAKDLREDECEEWWSDYYDFGAQLPCAKSRGGLVGIADNWGQGTMVTVS S _{SEQ ID NO: 251 CAP256V2LS (Apex-bNAb1) VL} QSVLTQPPSVSAAPGQKVTISCSGNTSNIGNNFVSWYQQRPGRAPQLLIYETDKRPSGIPDRFSASKSGTSGTLA ITGLQTGDEADYYCATWAASLSSARVFGTGTKVIVL _{SEQ ID NO: 252 CAP256V2LS (Apex-bNAb1) HC (no LS)} QVQLVESGGGVVQPGTSLRLSCAASQFRFDGYGMHWVRQAPGKGLEWVASISHDGIKKYHAEKVWGRFTISR DNSKNTLYLQMNSLRPEDTALYYCAKDLREDECEEWWSDYYDFGAQLPCAKSRGGLVGIADNWGQGTMVTVS SASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSS LGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVS HEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKG QPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSR WQQGNVFSCSVMHEALHNHYTQKSLSLSPGK _{SEQ ID NO: 253 CAP256V2LS (Apex-bNAb1) HC} QVQLVESGGGVVQPGTSLRLSCAASQFRFDGYGMHWVRQAPGKGLEWVASISHDGIKKYHAEKVWGRFTISR DNSKNTLYLQMNSLRPEDTALYYCAKDLREDECEEWWSDYYDFGAQLPCAKSRGGLVGIADNWGQGTMVTVS SASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSS LGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVS HEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKG QPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSR WQQGNVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 254 CAP256V2LS (Apex-bNAb1) LC} QSVLTQPPSVSAAPGQKVTISCSGNTSNIGNNFVSWYQQRPGRAPQLLIYETDKRPSGIPDRFSASKSGTSGTLA ITGLQTGDEADYYCATWAASLSSARVFGTGTKVIVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTV AWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS _{SEQ ID NO: 255 PGDM1400 (Apex-bNAb2) CDRH1} TYDLH _{SEQ ID NO: 256 PGDM1400 (Apex-bNAb2) CDRH2} WISHEGDKKVIVERFKA _{SEQ ID NO: 257 PGDM1400 (Apex-bNAb2) CDRH3} GSKHRLRDYALYDDDGALNWAVDVDYLSNLEF _{SEQ ID NO: 258 PGDM1400 (Apex-bNAb2) CDRL1} KSSHSLIHGDRNNYLA _{SEQ ID NO: 259 PGDM1400 (Apex-bNAb2) CDRL2} LASSRAS _{SEQ ID NO: 260 PGDM1400 (Apex-bNAb2) CDRL3} MQGRESPWT _{SEQ ID NO: 261 PGDM1400 (Apex-bNAb2) VH} QAQLVQSGPEVRKPGTSVKVSCKAPGNTLKTYDLHWVRSVPGQGLQWMGWISHEGDKKVIVERFKAKVTIDW DRSTNTAYLQLSGLTSGDTAVYYCAKGSKHRLRDYALYDDDGALNWAVDVDYLSNLEFWGQGTAVTVSS _{SEQ ID NO: 262 PGDM1400 (Apex-bNAb2) VL} DFVLTQSPHSLSVTPGESASISCKSSHSLIHGDRNNYLAWYVQKPGRSPQLLIYLASSRASGVPDRFSGSGSDKD FTLKISRVETEDVGTYYCMQGRESPWTFGQGTKVDIK _{SEQ ID NO: 263 PGDM1400 (Apex-bNAb2) HC (no LS)} QAQLVQSGPEVRKPGTSVKVSCKAPGNTLKTYDLHWVRSVPGQGLQWMGWISHEGDKKVIVERFKAKVTIDW DRSTNTAYLQLSGLTSGDTAVYYCAKGSKHRLRDYALYDDDGALNWAVDVDYLSNLEFWGQGTAVTVSSASTK GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQT YICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEV KFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQ VYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGN VFSCSVMHEALHNHYTQKSLSLSPGK _{SEQ ID NO: 264 PGDM1400 (Apex-bNAb2) HC (LS)} QAQLVQSGPEVRKPGTSVKVSCKAPGNTLKTYDLHWVRSVPGQGLQWMGWISHEGDKKVIVERFKAKVTIDW DRSTNTAYLQLSGLTSGDTAVYYCAKGSKHRLRDYALYDDDGALNWAVDVDYLSNLEFWGQGTAVTVSSASTK GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQT YICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEV KFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQ VYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGN VFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 265 PGDM1400 (Apex-bNAb2) LC} DFVLTQSPHSLSVTPGESASISCKSSHSLIHGDRNNYLAWYVQKPGRSPQLLIYLASSRASGVPDRFSGSGSDKD FTLKISRVETEDVGTYYCMQGRESPWTFGQGTKVDIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 266 PG9 (Apex-bNAb3) CDRH1} RQGMH _{SEQ ID NO: 267 PG9 (Apex-bNAb3) CDRH2} FIKYDGSEKYHADSVWG _{SEQ ID NO: 268 PG9 (Apex-bNAb3) CDRH3} EAGGPDYRNGYYYYDFYDGYYNYHYMDV _{SEQ ID NO: 269 PG9 (Apex-bNAb3) CDRL1} QGTSNDVGGYESVS _{SEQ ID NO: 270 PG9 (Apex-bNAb3) CDRL2} DVSKRPS _{SEQ ID NO: 271 PG9 (Apex-bNAb3) CDRL3} KSLTSTRRRV _{SEQ ID NO: 272 PG9 (Apex-bNAb3) VH} QRLVESGGGVVQPGSSLRLSCAASGFDFSRQGMHWVRQAPGQGLEWVAFIKYDGSEKYHADSVWGRLSISRD NSKDTLYLQMNSLRVEDTATYFCVREAGGPDYRNGYYYYDFYDGYYNYHYMDVWGKGTTVTVSS _{SEQ ID NO: 273 PG9 (Apex-bNAb3) VL} QSALTQPASVSGSPGQSITISCQGTSNDVGGYESVSWYQQHPGKAPKVVIYDVSKRPSGVSNRFSGSKSGNTAS LTISGLQAEDEGDYYCKSLTSTRRRVFGTGTKLTVL _{SEQ ID NO: 274 PG9 (Apex-bNAb3) HC (no LS)} QRLVESGGGVVQPGSSLRLSCAASGFDFSRQGMHWVRQAPGQGLEWVAFIKYDGSEKYHADSVWGRLSISRD NSKDTLYLQMNSLRVEDTATYFCVREAGGPDYRNGYYYYDFYDGYYNYHYMDVWGKGTTVTVSSASTKGPSVF PLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNV NHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNW YVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLP PSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCS VMHEALHNHYTQKSLSLSPGK _{SEQ ID NO: 275 PG9 (Apex-bNAb3) HC (LS)} QRLVESGGGVVQPGSSLRLSCAASGFDFSRQGMHWVRQAPGQGLEWVAFIKYDGSEKYHADSVWGRLSISRD NSKDTLYLQMNSLRVEDTATYFCVREAGGPDYRNGYYYYDFYDGYYNYHYMDVWGKGTTVTVSSASTKGPSVF PLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNV NHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNW YVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLP PSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCS VLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 276 PG9 (Apex-bNAb3) LC} QSALTQPASVSGSPGQSITISCQGTSNDVGGYESVSWYQQHPGKAPKVVIYDVSKRPSGVSNRFSGSKSGNTAS LTISGLQAEDEGDYYCKSLTSTRRRVFGTGTKLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTV AWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS _{SEQ ID NO: 277 PG16 (Apex-bNAb4) CDRH1} KYGMH _{SEQ ID NO: 278 PG16 (Apex-bNAb4) CDRH2} LISDDGMRKYHSDSMWG _{SEQ ID NO: 279 PG16 (Apex-bNAb4) CDRH3} EAGGPIWHDDVKYYDFNDGYYNYHYMDV _{SEQ ID NO: 280 PG16 (Apex-bNAb4) CDRL1} NGTSSDVGGFDSVS _{SEQ ID NO: 281 PG16 (Apex-bNAb4) CDRL2} DVSHRPS _{SEQ ID NO: 282 PG16 (Apex-bNAb4) CDRL3} SSLTDRSHRI _{SEQ ID NO: 283 PG16 (Apex-bNAb4) VH} QEQLVESGGGVVQPGGSLRLSCLASGFTFHKYGMHWVRQAPGKGLEWVALISDDGMRKYHSDSMWGRVTISR DNSKNTLYLQFSSLKVEDTAMFFCAREAGGPIWHDDVKYYDFNDGYYNYHYMDVWGKGTTVTVSS _{SEQ ID NO: 284 PG16 (Apex-bNAb4) VL} QSALTQPASVSGSPGQTITISCNGTSSDVGGFDSVSWYQQSPGKAPKVMVFDVSHRPSGISNRFSGSKSGNTAS LTISGLHIEDEGDYFCSSLTDRSHRIFGGGTKVTVL _{SEQ ID NO: 285 PG16 (Apex-bNAb4) HC (no LS)} QEQLVESGGGVVQPGGSLRLSCLASGFTFHKYGMHWVRQAPGKGLEWVALISDDGMRKYHSDSMWGRVTISR DNSKNTLYLQFSSLKVEDTAMFFCAREAGGPIWHDDVKYYDFNDGYYNYHYMDVWGKGTTVTVSSASTKGPS VFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYIC NVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKF NWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVY TLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVF SCSVMHEALHNHYTQKSLSLSPGK _{SEQ ID NO: 286 PG16 (Apex-bNAb4) HC} QEQLVESGGGVVQPGGSLRLSCLASGFTFHKYGMHWVRQAPGKGLEWVALISDDGMRKYHSDSMWGRVTISR DNSKNTLYLQFSSLKVEDTAMFFCAREAGGPIWHDDVKYYDFNDGYYNYHYMDVWGKGTTVTVSSASTKGPS VFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYIC NVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKF NWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVY TLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVF SCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 287 PG16 (Apex-bNAb4) LC} QSALTQPASVSGSPGQTITISCNGTSSDVGGFDSVSWYQQSPGKAPKVMVFDVSHRPSGISNRFSGSKSGNTAS LTISGLHIEDEGDYFCSSLTDRSHRIFGGGTKVTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVA WKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS _{SEQ ID NO: 288 PG20 (Apex-bNAb5) CDRH1} SYAFT _{SEQ ID NO: 289 PG20 (Apex-bNAb5) CDRH2} MVTPIFGEAKYSQRFEG _{SEQ ID NO: 290 PG20 (Apex-bNAb5) CDRH3} DRRAVPIATDNWLDP _{SEQ ID NO: 291 PG20 (Apex-bNAb5) CDRL1} RASQTINNYLN _{SEQ ID NO: 292 PG20 (Apex-bNAb5) CDRL2} GASNLQN _{SEQ ID NO: 293 PG20 (Apex-bNAb5) CDRL3} QQSFSTPRT _{SEQ ID NO: 294 PG20 (Apex-bNAb5) VH} QVRLVQSGPEVKKPGSSVTVSCQASGGTFSSYAFTWVRQAPGQGLEWLGMVTPIFGEAKYSQRFEGRVTITADE STSTTSIELRGLTSEDTAIYYCARDRRAVPIATDNWLDPWGQGTLVTVSS _{SEQ ID NO: 295 PG20 (Apex-bNAb5) VL} DIQLTQSPSSLSASVGDRVSITCRASQTINNYLNWYQQTPGKAPKLLIYGASNLQNGVPSRFSGSGSGTDFTLTI SSLQPEDFATYYCQQSFSTPRTFGQGTRLDIK _{SEQ ID NO: 296 PG20 (Apex-bNAb5) HC (no LS)} QVRLVQSGPEVKKPGSSVTVSCQASGGTFSSYAFTWVRQAPGQGLEWLGMVTPIFGEAKYSQRFEGRVTITADE STSTTSIELRGLTSEDTAIYYCARDRRAVPIATDNWLDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAAL GCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEP KSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPR EEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTC LVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKS LSLSPGK _{SEQ ID NO: 297} QVRLVQSGPEVKKPGSSVTVSCQASGGTFSSYAFTWVRQAPGQGLEWLGMVTPIFGEAKYSQRFEGRVTITADE STSTTSIELRGLTSEDTAIYYCARDRRAVPIATDNWLDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAAL GCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEP KSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPR EEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTC LVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSL SLSPGK SYAFS _{SEQ ID NO: 300 PGG14 (Apex-bNAb6) CDRH2} MITPVFGETKYAPRFQG _{SEQ ID NO: 301 PGG14 (Apex-bNAb6) CDRH3} DRRVVPMATDNWLDP C_DRL1 _CDRL2 GASTLQS _{SEQ ID NO: 304 PGG14 (Apex-bNAb6) CDRL3} QQSYSTPRT _{SEQ ID NO: 305 PGG14 (Apex-bNAb6) VH} QVLLVQSGTEVKKPGSSVKVSCQASGGAFSSYAFSWVRQAPGQGLEWMGMITPVFGETKYAPRFQGRLTLTAE ESLSTTYMELRSLTSDDTAFYYCTRDRRVVPMATDNWLDPWGQGTLVTVSS _{SEQ ID NO: 306 PGG14 (Apex-bNAb6) VL} DIQLTQSPSSLSASVGDRVTVTCRASQTIHTYLNWYQQIPGKAPKLLIYGASTLQSGVPSRFSGSGSGTDFTLTIN SLQPEDFATYYCQQSYSTPRTFGQGTRLDIK _{SEQ ID NO: 307 PGG14 (Apex-bNAb6) HC (no LS)} QVLLVQSGTEVKKPGSSVKVSCQASGGAFSSYAFSWVRQAPGQGLEWMGMITPVFGETKYAPRFQGRLTLTAE ESLSTTYMELRSLTSDDTAFYYCTRDRRVVPMATDNWLDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTA ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKV EPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTK PREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSL TCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQ KSLSLSPGK _{SEQ ID NO: 308 PGG14 (Apex-bNAb6) HC} QVLLVQSGTEVKKPGSSVKVSCQASGGAFSSYAFSWVRQAPGQGLEWMGMITPVFGETKYAPRFQGRLTLTAE ESLSTTYMELRSLTSDDTAFYYCTRDRRVVPMATDNWLDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTA ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKV EPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTK PREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSL TCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQK SLSLSPGK _{SEQ ID NO: 309 PGG14 (Apex-bNAb6) LC} DIQLTQSPSSLSASVGDRVTVTCRASQTIHTYLNWYQQIPGKAPKLLIYGASTLQSGVPSRFSGSGSGTDFTLTIN SLQPEDFATYYCQQSYSTPRTFGQGTRLDIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVD NALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 310 PGC14 (Apex-bNAb7) CDRH1} DYYLH _{SEQ ID NO: 311 PGC14 (Apex-bNAb7) CDRH2} LIDPENGEARYAEKFQG _{SEQ ID NO: 312 PGC14 (Apex-bNAb7) CDRH3} GAVGADSGSWFDP _{SEQ ID NO: 313 PGC14 (Apex-bNAb7) CDRL1} SGSKLGDKYVS _{SEQ ID NO: 314 PGC14 (Apex-bNAb7) CDRL2} ENDRRPS _{SEQ ID NO: 315 PGC14 (Apex-bNAb7) CDRL3} QAWETTTTTFVF _{SEQ ID NO: 316 PGC14 (Apex-bNAb7) VH} DGHLVQSGVEVKKTGATVKISCKVSGYSFIDYYLHWVQRAPGKGLEWVGLIDPENGEARYAEKFQGRVTIIADT SIDTGYMEMRSLKSEDTAVYFCAAGAVGADSGSWFDPWGQGTLVTVSS _{SEQ ID NO: 317 PGC14 (Apex-bNAb7) VL} SYELTQPPSVSVSPGQTASITCSGSKLGDKYVSWYQLRPGQSPILVMYENDRRPSGIPERFSGSNSGDTATLTIS GTQALDEADFYCQAWETTTTTFVFFGGGTQLTVL _{SEQ ID NO: 318 PGC14 (Apex-bNAb7) HC (no LS)} DGHLVQSGVEVKKTGATVKISCKVSGYSFIDYYLHWVQRAPGKGLEWVGLIDPENGEARYAEKFQGRVTIIADT SIDTGYMEMRSLKSEDTAVYFCAAGAVGADSGSWFDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALG CLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK SCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPRE EQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCL VKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSL SLSPGK _{SEQ ID NO: 319 PGC14 (Apex-bNAb7) HC (LS)} DGHLVQSGVEVKKTGATVKISCKVSGYSFIDYYLHWVQRAPGKGLEWVGLIDPENGEARYAEKFQGRVTIIADT SIDTGYMEMRSLKSEDTAVYFCAAGAVGADSGSWFDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALG CLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK SCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPRE EQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCL VKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHEALHSHYTQKSLS LSPGK _{SEQ ID NO: 320 PGC14 (Apex-bNAb7) LC} SYELTQPPSVSVSPGQTASITCSGSKLGDKYVSWYQLRPGQSPILVMYENDRRPSGIPERFSGSNSGDTATLTIS GTQALDEADFYCQAWETTTTTFVFFGGGTQLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVA WKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS _{SEQ ID NO: 321 CH01 (Apex-bNAb8) CDRH1} NFGFS _{SEQ ID NO: 322 CH01 (Apex-bNAb8) CDRH2} GLNWNGGDTRYADSVKG _{SEQ ID NO: 323 CH01 (Apex-bNAb8) CDRH3} GTDYTIDDAGIHYQGSGTFWYFDL _{SEQ ID NO: 324 CH01 (Apex-bNAb8) CDRL1} RASHNVHPKYFA _{SEQ ID NO: 325 CH01 (Apex-bNAb8) CDRL2} GGSTRAA _{SEQ ID NO: 326 CH01 (Apex-bNAb8) CDRL3} QQYGGSPYT _{SEQ ID NO: 327 CH01 (Apex-bNAb8) VH} EVQLVESGANVVRPGGSLRLSCKASGFIFENFGFSWVRQAPGKGLQWVAGLNWNGGDTRYADSVKGRFRMSR DNSRNFVYLDMDKVGVDDTAFYYCARGTDYTIDDAGIHYQGSGTFWYFDLWGRGTLVSVSS _{SEQ ID NO: 328 CH01 (Apex-bNAb8) VL} EIVLAQSPGTLSLSPGERATLSCRASHNVHPKYFAWYQQKPGQSPRLLIYGGSTRAAGIPGKFSGSGSGTDFTLTI SRVDPEDFAVYYCQQYGGSPYTFGQGTKVEIK _{SEQ ID NO: 329 CH01 (Apex-bNAb8) HC (no LS)} EVQLVESGANVVRPGGSLRLSCKASGFIFENFGFSWVRQAPGKGLQWVAGLNWNGGDTRYADSVKGRFRMSR DNSRNFVYLDMDKVGVDDTAFYYCARGTDYTIDDAGIHYQGSGTFWYFDLWGRGTLVSVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM HEALHNHYTQKSLSLSPGK _{SEQ ID NO: 330 CH01 (Apex-bNAb8) HC} EVQLVESGANVVRPGGSLRLSCKASGFIFENFGFSWVRQAPGKGLQWVAGLNWNGGDTRYADSVKGRFRMSR DNSRNFVYLDMDKVGVDDTAFYYCARGTDYTIDDAGIHYQGSGTFWYFDLWGRGTLVSVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVL HEALHSHYTQKSLSLSPGK _{SEQ ID NO: 331 CH01 (Apex-bNAb8) LC} EIVLAQSPGTLSLSPGERATLSCRASHNVHPKYFAWYQQKPGQSPRLLIYGGSTRAAGIPGKFSGSGSGTDFTLTI SRVDPEDFAVYYCQQYGGSPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKV DNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 332 CH02 (Apex-bNAb9) CDRH1} NYGLT _{SEQ ID NO: 333 CH02 (Apex-bNAb9) CDRH2} GMNWNGGDTRYADSVRG _{SEQ ID NO: 334 CH02 (Apex-bNAb9) CDRH3} GTDYTIDDQGRFYQGSGTFWYFDF _{SEQ ID NO: 335 CH02 (Apex-bNAb9) CDRL1} RASQNVHPRYFA _{SEQ ID NO: 336 CH02 (Apex-bNAb9) CDRL2} SGSTRAA _{SEQ ID NO: 337 CH02 (Apex-bNAb9) CDRL3} QQYGGSPYT _{SEQ ID NO: 338 CH02 (Apex-bNAb9) VH} EVQLVESGGSVVRPGGSLRLSCRASGFIFENYGLTWVRQVPGKGLHWVSGMNWNGGDTRYADSVRGRFSMSR DNSNNIAYLQMNNLRVEDTALYYCARGTDYTIDDQGRFYQGSGTFWYFDFWGRGTLVTVSS _{SEQ ID NO: 339 CH02 (Apex-bNAb9) VL} EIVLTQSPATLSVSPGERATLSCRASQNVHPRYFAWYQQKRGQSPRLLIHSGSTRAAGIADRFSGGGSGMHFTL TITRVEPEDFAVYFCQQYGGSPYTFGQGTRVELR _{SEQ ID NO: 340 CH02 (Apex-bNAb9) HC (no LS)} EVQLVESGGSVVRPGGSLRLSCRASGFIFENYGLTWVRQVPGKGLHWVSGMNWNGGDTRYADSVRGRFSMSR DNSNNIAYLQMNNLRVEDTALYYCARGTDYTIDDQGRFYQGSGTFWYFDFWGRGTLVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM HEALHNHYTQKSLSLSPGK _{SEQ ID NO: 341 CH02 (Apex-bNAb9) HC} EVQLVESGGSVVRPGGSLRLSCRASGFIFENYGLTWVRQVPGKGLHWVSGMNWNGGDTRYADSVRGRFSMSR DNSNNIAYLQMNNLRVEDTALYYCARGTDYTIDDQGRFYQGSGTFWYFDFWGRGTLVTVSSASTKGPSVFPLA PSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNH KPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPS RDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVL HEALHSHYTQKSLSLSPGK _{SEQ ID NO: 342 CH02 (Apex-bNAb9) LC} EIVLTQSPATLSVSPGERATLSCRASQNVHPRYFAWYQQKRGQSPRLLIHSGSTRAAGIADRFSGGGSGMHFTL TITRVEPEDFAVYFCQQYGGSPYTFGQGTRVELRRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQW KVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 343 CH03 (Apex-bNAb10) CDRH1} NYGLT _{SEQ ID NO: 344 CH03 (Apex-bNAb10) CDRH2} GMNWNGGDTRYADSVRG _{SEQ ID NO: 345 CH03 (Apex-bNAb10) CDRH3} GTDYTIDDQGIFYKGSGTFWYFDL _{SEQ ID NO: 346 CH03 (Apex-bNAb10) CDRL1} RASQSVHPKYFA _{SEQ ID NO: 347 CH03 (Apex-bNAb10) CDRL2} SGSTRAA _{SEQ ID NO: 348 CH03 (Apex-bNAb10) CDRL3} QQYGGSPYT _{SEQ ID NO: 349 CH03 (Apex-bNAb10) VH} EVQLVESGGGVVRPGGSLRLSCAASGFIFENYGLTWVRQVPGKGLHWVSGMNWNGGDTRYADSVRGRFSMSR DNSNNIAYLQMKNLRVDDTALYYCARGTDYTIDDQGIFYKGSGTFWYFDLWGRGTLVTVSS _{SEQ ID NO: 350 CH03 (Apex-bNAb10) VL} EIVLTQSPATLSLSPGERATLSCRASQSVHPKYFAWYQQKPGQSPRLLIYSGSTRAAGIADRFSGGGSGIHFTLTI TRVEPEDFAVYFCQQYGGSPYTFGQGTKVELR _{SEQ ID NO: 351 CH03 (Apex-bNAb10) HC (no LS)} EVQLVESGGGVVRPGGSLRLSCAASGFIFENYGLTWVRQVPGKGLHWVSGMNWNGGDTRYADSVRGRFSMSR DNSNNIAYLQMKNLRVDDTALYYCARGTDYTIDDQGIFYKGSGTFWYFDLWGRGTLVTVSSASTKGPSVFPLAP SSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHK PSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVD GVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR DELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM HEALHNHYTQKSLSLSPGK _{SEQ ID NO: 352 CH03 (Apex-bNAb10) HC (LS)} EVQLVESGGGVVRPGGSLRLSCAASGFIFENYGLTWVRQVPGKGLHWVSGMNWNGGDTRYADSVRGRFSMSR DNSNNIAYLQMKNLRVDDTALYYCARGTDYTIDDQGIFYKGSGTFWYFDLWGRGTLVTVSSASTKGPSVFPLAP SSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHK PSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVD GVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR DELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLH EALHSHYTQKSLSLSPGK _{SEQ ID NO: 353 CH03 (Apex-bNAb10) LC} EIVLTQSPATLSLSPGERATLSCRASQSVHPKYFAWYQQKPGQSPRLLIYSGSTRAAGIADRFSGGGSGIHFTLTI TRVEPEDFAVYFCQQYGGSPYTFGQGTKVELRRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKV DNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 354 CH04 (Apex-bNAb11) CDRH1} NFGFG _{SEQ ID NO: 355 CH04 (Apex-bNAb11) CDRH2} GTNWNGGDSRYGDSVKG _{SEQ ID NO: 356 CH04 (Apex-bNAb11) CDRH3} GTDYTIDDQGIRYQGSGTFWYFDV _{SEQ ID NO: 357 CH04 (Apex-bNAb11) CDRL1} RASQSVHSRYFA _{SEQ ID NO: 358 CH04 (Apex-bNAb11) CDRL2} GGSTRAT _{SEQ ID NO: 359 CH04 (Apex-bNAb11) CDRL3} QQYGRSPYT _{SEQ ID NO: 360 CH04 (Apex-bNAb11) VH} EVQLVESGGGLIRPGGSLRLSCKGSGFIFENFGFGWVRQGPGKGLEWVSGTNWNGGDSRYGDSVKGRFTISRD NSNNFVYLQMNSLRPEDTAIYYCARGTDYTIDDQGIRYQGSGTFWYFDVWGRGTLVTVSS _{SEQ ID NO: 361 CH04 (Apex-bNAb11) VL} EIVLTQSPDTLSLSPGERATLSCRASQSVHSRYFAWYQHKPGQPPRLLIYGGSTRATGIPNRFSAGGSGTQFTLT VNRLEAEDFAVYYCQQYGRSPYTFGQGTKVEIR _{SEQ ID NO: 362 CH04 (Apex-bNAb11) HC (no LS)} EVQLVESGGGLIRPGGSLRLSCKGSGFIFENFGFGWVRQGPGKGLEWVSGTNWNGGDSRYGDSVKGRFTISRD NSNNFVYLQMNSLRPEDTAIYYCARGTDYTIDDQGIRYQGSGTFWYFDVWGRGTLVTVSSASTKGPSVFPLAPS SKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKP SNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDG VEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRD ELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHE ALHNHYTQKSLSLSPGK _{SEQ ID NO: 363 CH04 (Apex-bNAb11) HC (LS)} EVQLVESGGGLIRPGGSLRLSCKGSGFIFENFGFGWVRQGPGKGLEWVSGTNWNGGDSRYGDSVKGRFTISRD NSNNFVYLQMNSLRPEDTAIYYCARGTDYTIDDQGIRYQGSGTFWYFDVWGRGTLVTVSSASTKGPSVFPLAPS SKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKP SNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDG VEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRD ELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVLHE ALHSHYTQKSLSLSPGK _{SEQ ID NO: 364 CH04 (Apex-bNAb11) LC} EIVLTQSPDTLSLSPGERATLSCRASQSVHSRYFAWYQHKPGQPPRLLIYGGSTRATGIPNRFSAGGSGTQFTLT VNRLEAEDFAVYYCQQYGRSPYTFGQGTKVEIRRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWK VDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 365 PGT141 (Apex-bNAb12) CDRH1} KYDVH _{SEQ ID NO: 366 PGT141 (Apex-bNAb12) CDRH2} WMSHEGDKTESAQRFKG _{SEQ ID NO: 367 PGT141 (Apex-bNAb12) CDRH3} GSKHRLRDYVLYDDYGLINYQEWNDYLEFLDV _{SEQ ID NO: 368 PGT141 (Apex-bNAb12) CDRL1} SSTQSLRHSNGANYLA _{SEQ ID NO: 369 PGT141 (Apex-bNAb12) CDRL2} LGSQRAS _{SEQ ID NO: 370 PGT141 (Apex-bNAb12) CDRL3} MQGLNRPWT _{SEQ ID NO: 371 PGT141 (Apex-bNAb12) VH} QVQLVQSGPEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQGLEWVGWMSHEGDKTESAQRFKGRVTFT RDTSASTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLINYQEWNDYLEFLDVWGHGTAVTVSS _{SEQ ID NO: 372 PGT141 (Apex-bNAb12) VL} DTVVTQSPLSLPVTPGEAASMSCSSTQSLRHSNGANYLAWYQHKPGQSPRLLIRLGSQRASGVPDRFSGSGSGT HFTLKISRVEAEDAAIYYCMQGLNRPWTFGKGTKLEIK _{SEQ ID NO: 373 PGT141 (Apex-bNAb12) HC (no LS)} QVQLVQSGPEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQGLEWVGWMSHEGDKTESAQRFKGRVTFT RDTSASTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLINYQEWNDYLEFLDVWGHGTAVTVSSAST KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQ TYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPE VKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREP QVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQG NVFSCSVMHEALHNHYTQKSLSLSPGK _{SEQ ID NO: 374 PGT141 (Apex-bNAb12) HC (LS)} QVQLVQSGPEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQGLEWVGWMSHEGDKTESAQRFKGRVTFT RDTSASTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLINYQEWNDYLEFLDVWGHGTAVTVSSAST KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQ TYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPE VKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREP QVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQG NVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 375 PGT141 (Apex-bNAb12) LC} DTVVTQSPLSLPVTPGEAASMSCSSTQSLRHSNGANYLAWYQHKPGQSPRLLIRLGSQRASGVPDRFSGSGSGT HFTLKISRVEAEDAAIYYCMQGLNRPWTFGKGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 376 PGT142 (Apex-bNAb13) CDRH1} KYDVH _{SEQ ID NO: 377 PGT142 (Apex-bNAb13) CDRH2} WISHERDKTESAQRFKG _{SEQ ID NO: 378 PGT142 (Apex-bNAb13) CDRH3} GSKHRLRDYVLYDDYGLINYQEWNDYLEFLDV _{SEQ ID NO: 379 PGT142 (Apex-bNAb13) CDRL1} SSTQSLRHSNGANYLA _{SEQ ID NO: 380 PGT142 (Apex-bNAb13) CDRL2} LGSQRAS _{SEQ ID NO: 381 PGT142 (Apex-bNAb13) CDRL3} MQGLNRPWT _{SEQ ID NO: 382 PGT142 (Apex-bNAb13) VH} QVQLVQSGPEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQGLEWVGWISHERDKTESAQRFKGRVTFTR DTSATTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLINYQEWNDYLEFLDVWGHGTAVTVSS _{SEQ ID NO: 383 PGT142 (Apex-bNAb13) VL} DTVVTQSPLSLPVTPGEAASMSCSSTQSLRHSNGANYLAWYQHKPGQSPRLLIRLGSQRASGVPDRFSGSGSGT HFTLKISRVEAEDAAIYYCMQGLNRPWTFGKGTKLEIK _{SEQ ID NO: 384 PGT142 (Apex-bNAb13) HC (no LS)} QVQLVQSGPEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQGLEWVGWISHERDKTESAQRFKGRVTFTR DTSATTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLINYQEWNDYLEFLDVWGHGTAVTVSSASTK GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQT YICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEV KFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQ VYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGN VFSCSVMHEALHNHYTQKSLSLSPGK _{SEQ ID NO: 385 PGT142 (Apex-bNAb13) HC} QVQLVQSGPEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQGLEWVGWISHERDKTESAQRFKGRVTFTR DTSATTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLINYQEWNDYLEFLDVWGHGTAVTVSSASTK GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQT YICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEV KFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQ VYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGN VFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 386 PGT142 (Apex-bNAb13) LC} DTVVTQSPLSLPVTPGEAASMSCSSTQSLRHSNGANYLAWYQHKPGQSPRLLIRLGSQRASGVPDRFSGSGSGT HFTLKISRVEAEDAAIYYCMQGLNRPWTFGKGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 387 PGT143 (Apex-bNAb14) CDRH1} KYDVH _{SEQ ID NO: 388 PGT143 (Apex-bNAb14) CDRH2} WMSHEGDKTESAQRFKG _{SEQ ID NO: 389 PGT143 (Apex-bNAb14) CDRH3} GSKHRLRDYVLYDDYGLINYQEWNDYLEFLDV _{SEQ ID NO: 390 PGT143 (Apex-bNAb14) CDRL1} TSTQSLRHSNGANYLA _{SEQ ID NO: 391 PGT143 (Apex-bNAb14) CDRL2} LGSQRAS _{SEQ ID NO: 392 PGT143 (Apex-bNAb14) CDRL3} MQGLNRPWT _{SEQ ID NO: 393 PGT143 (Apex-bNAb14) VH} QVQLEQSGAEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQGLEWVGWMSHEGDKTESAQRFKGRVTFT RDTSASTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLINYQEWNDYLEFLDVWGHGTAVTVSS _{SEQ ID NO: 394 PGT143 (Apex-bNAb14) VL} DTVVTQSPLSLPVTPGEAASMSCTSTQSLRHSNGANYLAWYQHKPGQSPRLLIRLGSQRASGVPDRFSGSGSGT HFTLKISRVEPEDAAIYYCMQGLNRPWTFGKGTKLEIK _{SEQ ID NO: 395 PGT143 (Apex-bNAb14) HC (no LS)} QVQLEQSGAEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQGLEWVGWMSHEGDKTESAQRFKGRVTFT RDTSASTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLINYQEWNDYLEFLDVWGHGTAVTVSSAST KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQ TYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPE VKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREP QVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQG NVFSCSVMHEALHNHYTQKSLSLSPGK _{SEQ ID NO: 396 PGT143 (Apex-bNAb14) HC} QVQLEQSGAEVKKPGSSVKVSCKASGNTFSKYDVHWVRQATGQGLEWVGWMSHEGDKTESAQRFKGRVTFT RDTSASTAYMELRGLTSDDTAIYYCTRGSKHRLRDYVLYDDYGLINYQEWNDYLEFLDVWGHGTAVTVSSAST KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQ TYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPE VKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREP QVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQG NVFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 397 PGT143 (Apex-bNAb14) LC} DTVVTQSPLSLPVTPGEAASMSCTSTQSLRHSNGANYLAWYQHKPGQSPRLLIRLGSQRASGVPDRFSGSGSGT HFTLKISRVEPEDAAIYYCMQGLNRPWTFGKGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 398 PGT144 (Apex-bNAb15) CDRH1} KYDVH _{SEQ ID NO: 399 PGT144 (Apex-bNAb15) CDRH2} WMSHEGDKTESAQRFKG _{SEQ ID NO: 400 PGT144 (Apex-bNAb15) CDRH3} GSKHRLRDYVLYDDYGLINQQEWNDYLEFLDV _{SEQ ID NO: 401 PGT144 (Apex-bNAb15) CDRL1} TSTQSLRHSNGANYLA _{SEQ ID NO: 402 PGT144 (Apex-bNAb15) CDRL2} LGSQRAS _{SEQ ID NO: 403 PGT144 (Apex-bNAb15) CDRL3} MQGLNRPWT _{SEQ ID NO: 404 PGT144 (Apex-bNAb15) VH} QVQLVQSGAEVKKPGSSVKVSCKASGNTFRKYDVHWVRQATGQGLEWVGWMSHEGDKTESAQRFKGRVSFT RDNSASTAYIELRGLTSDDTAIYYCTGGSKHRLRDYVLYDDYGLINQQEWNDYLEFLDVWGHGTAVTVSS _{SEQ ID NO: 405 PGT144 (Apex-bNAb15) VL} DTVVTQSPLSLSVTPGEAASMSCTSTQSLRHSNGANYLAWYQHKPGQSPRLLIRLGSQRASGVPDRFSGSGSGT HFTLKISRVEADDAAIYYCMQGLNRPWTFGKGTKLEIK _{SEQ ID NO: 406 PGT144 (Apex-bNAb15) HC (no LS)} QVQLVQSGAEVKKPGSSVKVSCKASGNTFRKYDVHWVRQATGQGLEWVGWMSHEGDKTESAQRFKGRVSFT RDNSASTAYIELRGLTSDDTAIYYCTGGSKHRLRDYVLYDDYGLINQQEWNDYLEFLDVWGHGTAVTVSSASTK GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQT YICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEV KFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQ VYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGN VFSCSVMHEALHNHYTQKSLSLSPGK _{SEQ ID NO: 407 PGT144 (Apex-bNAb15) HC} QVQLVQSGAEVKKPGSSVKVSCKASGNTFRKYDVHWVRQATGQGLEWVGWMSHEGDKTESAQRFKGRVSFT RDNSASTAYIELRGLTSDDTAIYYCTGGSKHRLRDYVLYDDYGLINQQEWNDYLEFLDVWGHGTAVTVSSASTK GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQT YICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEV KFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQ VYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGN VFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 408 PGT144 (Apex-bNAb15) LC} DTVVTQSPLSLSVTPGEAASMSCTSTQSLRHSNGANYLAWYQHKPGQSPRLLIRLGSQRASGVPDRFSGSGSGT HFTLKISRVEADDAAIYYCMQGLNRPWTFGKGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 409 PGT145 (Apex-bNAb16) CDRH1} NHDVH _{SEQ ID NO: 410 PGT145 (Apex-bNAb16) CDRH2} WMSHEGDKTGLAQKFQG _{SEQ ID NO: 411 PGT145 (Apex-bNAb16) CDRH3} GSKHRLRDYFLYNEYGPNYEEWGDYLATLDV _{SEQ ID NO: 412 PGT145 (Apex-bNAb16) CDRL1} KCSHSLQHSTGANYLA _{SEQ ID NO: 413 PGT145 (Apex-bNAb16) CDRL2} LATHRAS _{SEQ ID NO: 414 PGT145 (Apex-bNAb16) CDRL3} MQGLHSPWT _{SEQ ID NO: 415 PGT145 (Apex-bNAb16) VH} QVQLVQSGAEVKKPGSSVKVSCKASGNSFSNHDVHWVRQATGQGLEWMGWMSHEGDKTGLAQKFQGRVTIT RDSGASTVYMELRGLTADDTAIYYCLTGSKHRLRDYFLYNEYGPNYEEWGDYLATLDVWGHGTAVTVSS _{SEQ ID NO: 416 PGT145 (Apex-bNAb16) VL} EVVITQSPLFLPVTPGEAASLSCKCSHSLQHSTGANYLAWYLQRPGQTPRLLIHLATHRASGVPDRFSGSGSGTD FTLKISRVESDDVGTYYCMQGLHSPWTFGQGTKVEIK _{SEQ ID NO: 417 PGT145 (Apex-bNAb16) HC (no LS)} QVQLVQSGAEVKKPGSSVKVSCKASGNSFSNHDVHWVRQATGQGLEWMGWMSHEGDKTGLAQKFQGRVTIT RDSGASTVYMELRGLTADDTAIYYCLTGSKHRLRDYFLYNEYGPNYEEWGDYLATLDVWGHGTAVTVSSASTK GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQT YICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEV KFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQ VYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGN VFSCSVMHEALHNHYTQKSLSLSPGK _{SEQ ID NO: 418 PGT145 (Apex-bNAb16) HC (LS)} QVQLVQSGAEVKKPGSSVKVSCKASGNSFSNHDVHWVRQATGQGLEWMGWMSHEGDKTGLAQKFQGRVTIT RDSGASTVYMELRGLTADDTAIYYCLTGSKHRLRDYFLYNEYGPNYEEWGDYLATLDVWGHGTAVTVSSASTK GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQT YICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEV KFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQ VYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGN VFSCSVLHEALHSHYTQKSLSLSPGK _{SEQ ID NO: 419 PGT145 (Apex-bNAb16)} LCEVVITQSPLFLPVTPGEAASLSCKCSHSLQHSTGANYLAWYLQRPGQTPRLLIHLATHRASGVPDRFSGSGSG TDFTLKISRVESDDVGTYYCMQGLHSPWTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPRE AKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 420 CAP256V2LS V1/V2 apex bispecific 2 (bispecific1-2)} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSQSVLTQPPSVSAAPGQKVTISCSGNTSNIGNNFVSWYQQRPGR APQLLIYETDKRPSGIPDRFSASKSGTSGTLAITGLQTGDEADYYCATWAASLSSARVFGTGTKVIVLGQPKAAPS VTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHR SYSCQVTHEGSTVEKTVAPTECS _{SEQ ID NO: 421 CAP256V2LS V1/V2 apex bispecific 3 (bispecific1-3)} QVQLVESGGGVVQPGTSLRLSCAASQFRFDGYGMHWVRQAPGKGLEWVASISHDGIKKYHAEKVWGRFTISR DNSKNTLYLQMNSLRPEDTALYYCAKDLREDECEEWWSDYYDFGAQLPCAKSRGGLVGIADNWGQGTMVTVS SASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSS LGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVS HEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKG QPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSR WQQGNVFSCSVLHEALHSHYTQKSLSLSPGKGGGGSKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKIL GNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNLKPEDSDTYICEVEDQKEEVQLVVVC _{SEQ ID NO: 422 CAP256V2LS V1/V2 apex bispecific 4 (bispecific1-4)} QSVLTQPPSVSAAPGQKVTISCSGNTSNIGNNFVSWYQQRPGRAPQLLIYETDKRPSGIPDRFSASKSGTSGTLA ITGLQTGDEADYYCATWAASLSSARVFGTGTKVIVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTV AWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECSGGGGSKK VVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNLKP EDSDTYICEVEDQKEEVQLVVVC _{SEQ ID NO: 423 PGDM1400 V1/V2 apex bispecific 2 (bispecific2-2)} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKNL KPEDSDTYICEVEDQKEEVQLVVVCGGGGSDFVLTQSPHSLSVTPGESASISCKSSHSLIHGDRNNYLAWYVQKP GRSPQLLIYLASSRASGVPDRFSGSGSDKDFTLKISRVETEDVGTYYCMQGRESPWTFGQGTKVDIKRTVAAPSV FIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHK VYACEVTHQGLSSPVTKSFNRGEC _{SEQ ID NO: 424 PGDM1400 V1/V2 apex bispecific 3 (bispecific2-3)} QAQLVQSGPEVRKPGTSVKVSCKAPGNTLKTYDLHWVRSVPGQGLQWMGWISHEGDKKVIVERFKAKVTIDW DRSTNTAYLQLSGLTSGDTAVYYCAKGSKHRLRDYALYDDDGALNWAVDVDYLSNLEFWGQGTAVTVSSASTK GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQT YICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEV KFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQ VYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGN VFSCSVLHEALHSHYTQKSLSLSPGGGGGSKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFL TKGPSKLNDRVDSRRSLWDQGNFPLIIKNLKPEDSDTYICEVEDQKEEVQLVVVC _{SEQ ID NO: 425 PGDM1400 V1/V2 apex bispecific 4 (bispecific2-4)} DFVLTQSPHSLSVTPGESASISCKSSHSLIHGDRNNYLAWYVQKPGRSPQLLIYLASSRASGVPDRFSGSGSDKD FTLKISRVETEDVGTYYCMQGRESPWTFGQGTKVDIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAK VQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECGGGG SKKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQGNFPLIIKN LKPEDSDTYICEVEDQKEEVQLVVVC _{SEQ ID NO: 426 D1m-K8C-G99C_1xG4S_bNAb1-LC} KKVVYGKCGDTVELTCTASQKKNIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRVDSRRSLWDQG NFPLIIKNLKPEDSDTYICEVEDQKEEVQLVVVCGGGGSQSALTQPPSASGSPGQSITISCTGTSNNF VSWYQQHAGKAPKLVIYDVNKRPSGVPDRFSGSKSGNTASLTVSGLQTDDEAVYYCGSLVGNWD VIFGGGTKLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVET TTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS

Claims

CLAIMS 1_{. A multimeric anti-HIV envelope spike complex-binding protein comprising:} _{i. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at least} one heavy chain or light chain, wherein the antibody binds to the V1/V2 loop of a g_{p120 protein or the gp120-gp41 interface region of a gp120 and a gp41 protein;} and i_{i. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached} _{directly or by a linker to the N-terminus or C-terminus of at least one of the heavy} _{chains or light chains of the broadly neutralizing antibody.} _{2. The binding protein of claim 1, wherein the broadly neutralizing antibody binds to at least} one complex N-glycan at the V1/V2 loop of a gp120 protein or the gp120-gp41 interface of a g_{p120 and a gp41 protein.} _{3. A multimeric anti-HIV envelope spike complex-binding protein comprising:} _{i. a broadly neutralizing anti-HIV envelope spike complex antibody, comprising at least} one heavy chain or light chain, wherein the antibody binds to at least one complex N_{-glycan on a gp120 protein or a gp41 protein; and} _{ii. at least one CD4 domain which binds to gp120, wherein the CD4 domain is attached} directly or by a linker to the N-terminus or C-terminus of at least one of the heavy c_{hains or light chains of the broadly neutralizing antibody.} _{4. The binding protein of claim 3, wherein the broadly neutralizing antibody binds to at least} one complex N-glycan at the V1/V2 loop of a gp120 protein or the gp120-gp41 interface of a g_{p120 and a gp41 protein.} _{5. The binding protein of any preceding claim, wherein the binding protein is a bispecific} binding protein. 6_{. The binding protein of any preceding claim, wherein the CD4 domain is attached via a linker} _{to the N-terminus or C-terminus of at least one heavy chain or light chain of the broadly} neutralizing antibody.

_{7. The binding protein of any preceding claim, wherein the binding protein comprises at least} four CD4 domains. _{8. The binding protein of claim 7, wherein the C-terminus of each of the four CD4 domains is} attached by a linker to the N-terminus of the two heavy chains and two light chains of the b_{roadly neutralizing antibody.} _{9. The binding protein of any preceding claim, wherein the CD4 domain is attached via a linker} _{and said linker is selected from one of SEQ ID NOs: 30 to 35.} _{10. The binding protein of any preceding claim, wherein the CD4 domain comprises at least one} _{mutation selected from: L5Y, S23N, A55V, I79P, L96V and/or F98V mutations.} _{11. The binding protein of any preceding claim, wherein the CD4 domain comprises or consists} _{of any one of SEQ ID NO: 4 – 21.} _{12. The binding protein of any preceding claim, wherein the broadly neutralizing antibody} _{comprises CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, CDLR3 as set out in any one row of} Table 3. _{13. The binding protein of any preceding claim, wherein the broadly neutralizing antibody} comprises a heavy chain variable domain and a light chain variable domain pair that is at least 95% identical to any of the variable domain pairs set out in any one row of Table 4. _{14. The binding protein of any preceding claim, wherein the broadly neutralizing antibody} comprises a heavy chain and a light chain pair that is at least 95% identical to any of the chain pairs set out in any one row of Table 4. _{15. The binding protein of any preceding claim, wherein the binding protein comprises or} _{consists of a sequence at least 95% identical to any one of SEQ ID NO: 60-73 or 74-89.} _{16. A pharmaceutical composition comprising the binding protein as defined in any one of the} _{preceding claims and a pharmaceutically acceptable excipient.} _{17. A method of treating or preventing an HIV infection in a human comprising administering to} the human an anti-HIV binding protein according to any one of claims 1 to 15, or a pharmaceutical composition according to claim 16.

_{18. An anti-HIV binding protein according to any one of claims 1 to 15, or a pharmaceutical} composition according to claim 16, for use in treating or preventing an HIV infection in a human. _{19. Use of an anti-HIV binding protein according to any one of claims 1 to 15, or a} pharmaceutical composition according to claim 16, in the manufacture of a medicament for treating or preventing an HIV infection in a human. _{20. The method according to claim 17, protein or composition for use according to claim 18, or} use according to claim 19, wherein HIV viral load in the human is decreased. _{21. A kit comprising in separate containers: an anti-HIV binding protein according to any one of} _{claims 1 to 15 or a pharmaceutical composition according to claim 16, and at least one anti-} viral drug that inhibits cellular entry, replication, or transcription of HIV in a human. _{22. The kit as claimed in claim 21, wherein the antiviral drug is selected from: Nucleoside} Reverse Transcriptase Inhibitors (NRTIs), Non-Nucleoside Reverse Transcriptase Inhibitors (NNRTIs), Protease Inhibitors (PIs), Entry Inhibitors, Integrase Strand Transfer Inhibitors (INSTI), Maturation Inhibitors (MIs), Capsid Inhibitors (CIs) and Nucleoside Reverse Transcriptase Translocation Inhibitors (NRTTIs). _{23. A nucleic acid sequence that encodes an anti-HIV binding protein according to any one of} claims 1 to 15. _{24. An expression vector that comprises the nucleic acid sequence of claim 23.} _{25. A recombinant host cell that comprises the nucleic acid sequence of claim 23 or the} expression vector of claim 24. _{26. A method of producing an anti-HIV binding protein, comprising culturing the host cell as} _{defined in claim 25 under conditions suitable for expression of said nucleic acid sequence or} vector, whereby an anti-HIV binding protein is produced. _{27. The anti-HIV binding protein produced by the method of claim 26.}