WO2024159030A2

WO2024159030A2 - Human papillomavirus, varicella-zoster virus, and rabies virus antigens and uses thereof in cancer immunotherapy

Info

Publication number: WO2024159030A2
Application number: PCT/US2024/012976
Authority: WO
Inventors: Nicolas CUBURU; Lukasz BIALKOWSKI; John SCHILLER; Shiv K. SETHI
Original assignee: US Department of Health and Human Services
Current assignee: US Department of Health and Human Services
Priority date: 2023-01-25
Filing date: 2024-01-25
Publication date: 2024-08-02
Anticipated expiration: 2025-07-25
Also published as: CN120981242A; WO2024159030A3; EP4654991A2

Abstract

Provided herein are varicella-zoster virus vaccine, human papillomavirus vaccine, and Rabies vaccine antigens, compositions thereof, and uses thereof in cancer immunotherapy and cancer treatment.

Description

060734-783069 HUMAN PAPILLOMAVIRUS, VARICELLA-ZOSTER VIRUS, AND RABIES VIRUS ANTIGENS AND USES THEREOF IN CANCER IMMUNOTHERAPY STATEMENT REGARDING FEDERALLY SPONSORED RESEARCH OR DEVELOPMENT [0001] This invention was made in part with Government support under Grant Number ZIA BC 009052 awarded by the National Cancer Institute. The Government has certain rights in this invention. FIELD OF THE INVENTION [0002] Provided herein are human papillomavirus (HPV),varicella-zoster virus (VZV), and Rabies lyssavirus antigen compositions and their use in cancer immunotherapy. REFERENCE TO SEQUENCE LISTING [0003] This application contains a Sequence Listing that has been submitted in XML format via Patent Center and is hereby incorporated by reference in its entirety. The file, created on January 18, 2024, is named SequenceListing_E_199_2022_0_PC_01.xml, and is 4.36 Mb in size. BACKGROUND OF THE INVENTION [0004] Cancer immunotherapy has become a standard of care and first line treatment for many types of cancer including, melanoma, lung and colon cancer. Systemic immunotherapy can lead to remarkable cancer remission but is often associated with high rate of immune-related toxicity or resistance of the tumor microenvironment. Local cancer immunotherapy against solid tumors has emerged as a safer and effective approach to stimulate the tumor immune microenvironment and to promote disseminated anti-tumor immune responses. But most current approaches for in situ tumor therapies focus on activating innate immunity. [0005] There is a need in the art for harnessing preexisting adaptive immune responses using existing vaccines or vaccine-derived antigens to debulk tumor masses and to reprogram the tumor microenvironment. The goal is to promote immediate local immune responses and long- term disseminated anti-tumor responses by repurposing existing subunit vaccines or harnessing preexisting anti-vaccine immunity. 93155272.1 1 060734-783069 SUMMARY OF THE INVENTION [0006] Provided herein is a method of treating a cancer in a subject in need thereof, which may comprise administering to the subject a composition comprising one or more varicella-zoster virus (VZV) antigens from a VZV glycoprotein E. Also provided herein are use of the VZV antigen composition in the manufacture of a medicament for treating the cancer in a subject and the VZV antigen composition for use in treating the cancer in the subject. The subject may have been previously immunized against VZV. The composition may be or may be intended to be administered at the site of the cancer. The cancer may be a solid tumor. The composition may be administered via intratumoral or peritumoral injection. [0007] The VZV antigens may comprise a truncated VZV gE. The truncated VZV gE may comprise the amino acid sequence set forth in SEQ ID NO: 2. The VZV antigens may comprise one or more MHC-I- or MHC-II-restricted peptides from VZV gE, or a combination thereof. The amino acid sequence of VZV gE may be set forth in SEQ ID NO: 1. The VZV antigens may comprise one or more MHC-II-restricted VZV gE peptides, and each VZV gE peptide may independently comprise the amino acid sequence set forth in one of SEQ ID NOs: 3-156. The VZV antigens may also or alternatively comprise one or more MHC-I-restricted VZV gE peptides, and each VZV gE peptide may independently comprise the amino acid sequence set forth in SEQ ID NOs: 157-1387. [0008] Provided herein are a method of treating a cancer in a subject in need thereof, which may comprise administering to the subject a composition comprising one or more human papillomavirus (HPV) antigens from an HPV L1 polypeptide. Also provided herein are use of the HPV antigen composition in the manufacture of a medicament for treating the cancer in a subject and the HPV antigen composition for use in treating the cancer in the subject. The subject may have been previously immunized against HPV. The composition may be or may be intended to be administered at the site of the cancer. The cancer may be a solid tumor. The composition may be administered via intratumoral or peritumoral injection. [0009] The HPV may be type 16 (HPV16) or type 18 (HPV18). The HPV antigens may comprise one or more MHC-I- or MHC-II-restricted peptides of the L1 polypeptide, or a combination thereof. The HPV antigens may comprise one or more MHC-II-restricted HPV L1 peptides. Each HPV L1 peptide may independently comprise an HPV16 peptide comprising the amino acid sequence set forth in one of SEQ ID NOs: 1390-1513 or an HPV18 peptide 93155272.1 2 060734-783069 comprising the amino acid sequence set forth in one of SEQ ID NOs: 1514-1637. The HPV antigens may also or alternatively comprise one or more MHC-I-restricted HPV L1 peptides. Each HPV L1 peptide may independently comprise an HPV16 peptide comprising the amino acid sequence set forth in one of SEQ ID NOs: 1638-2632 or an HPV18 peptide comprising the amino acid sequence set forth in one of SEQ ID NOs: 2633-3631. In one example, each HPV L1 peptide comprises an HPV16 peptide comprising the amino acid sequence set forth in one of SEQ ID NOs: 3632-3645 or an HPV18 peptide comprising the amino acid sequence set forth in one of SEQ ID NOs: 3646-3651. The HPV16 peptide may comprise the amino acid sequence set forth in SEQ ID NO: 1776. [0010] The composition may comprise or may be administered in combination with an adjuvant. The adjuvant may comprise one or more of poly(I:C), poly-ICLC, a 3-O-desacyl-4’- monophosphoryl lipid A (MPL), QS-21, aluminum hydroxide, and aluminum hydroxyphosphate. In one example, the adjuvant comprises poly(I:C). In another, the adjuvant comprises MPL. In a further example, the adjuvant comprises QS21. The adjuvant may comprise MPL and QS-21. The adjuvant may be AS01B. In one example, the adjuvant comprises MPL and aluminium hydroxyphosphate. The adjuvant may be AS04. In another example, the adjuvant comprises poly(I:C) and QS-21. The adjuvant may be MA105, and may be described in WO2023124116 (the contents of which are incorporated herein by reference). [0011] In one example, the adjuvant is AS01B and the VZV antigen comprises the VZV gE polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 2. The VZV antigen and the adjuvant may be from SHINGRIX. The antigen adjuvant may comprise poly(I:C), the VZV antigens may comprise one or more VZV gE peptides, and each VZV gE peptide may comprise the amino acid sequence set forth in one of SEQ ID NOs: 3-156. [0012] In one example, the HPV antigen composition further comprises, is administered in combination with, or is intended to be administered in combination with the truncated VZV gE comprising the amino acid sequence set forth in SEQ ID NO: 2. The subject may have been vaccinated against VZV and HPV. The composition may comprise or may be administered in combination with an adjuvant, which may comprise MPL, QS21, or a combination thereof. The VZV gE composition may be SHINGRIX. [0013] In a further example, the VZV antigen composition further comprises, is administered in combination with, or is intended to be administered in combination with one or more tumor- 93155272.1 3 060734-783069 associated antigens. In one example, the cancer does not express tumor-associated antigens. In another example, the tumor expresses at least one of the tumor-associated antigens. Each tumor- associated antigen may independently be from a tumor-associated protein selected from the group consisting of an E6 oncoprotein and an E7 oncoprotein. Each E6 oncoprotein and E7 oncoprotein may independently be selected from an HPV type selected from the group consisting of HPV16, HPV18, HPV31, HPV45, HPV52, and HPV58. Each E6 and E7 oncoprotein from each of the HPV types may comprise the amino acid sequence set forth in one of SEQ ID NOs: 3652-3663, respectively. Each tumor-associated antigen may be an MHC-I-restricted peptide. Each tumor-associated peptide may comprise the amino acid sequence set forth in one of SEQ ID NOs: 3664-5103. The tumor-associated protein may be the HPV16 E7 oncoprotein. The tumor-associated antigens may comprise a peptide comprising the sequence RAHYNIVTF (SEQ ID NO: 3863). The VZV antigen composition and the tumor-associated antigen may further be administered in combination with or may be intended to be administered in combination with the one or more HPV antigens, and the subject may further have been vaccinated against HPV. In one example, a combination of the truncated VZV gE, the HPV16 L1 peptide comprising the amino acid sequence set forth in SEQ ID NO: 1776, and the tumor- associated antigen comprising the amino acid sequence set forth in SEQ ID NO: 3863 is administered to the subject. [0014] The subject may be human leukocyte antigen (HLA)-A0201 (HLA-A0201)-positive. In one example, the cancer comprises a tumor that does not express E6 and E7 oncoproteins from HPV16 and HPV18. The composition may comprise a truncated VZV gE protein, an HPV16 L1 peptide comprising the sequence set forth in SEQ ID NO: 1960 (ICWGNQLFV), and an HPV18 L1 peptide comprising the sequence set forth in SEQ ID NO: 3649 (NVFPIFLQM). In another example, the cancer comprises a tumor that expresses one or more of E6 and E7 oncoproteins from HPV16 or HPV18. The composition may comprise a truncated VZV gE protein; an HPV16 L1 peptide comprising the sequence set forth in SEQ ID NO: 1960; an HPV18 L1 peptide comprising the sequence set forth in SEQ ID NO: 3649; HPV16 E7 peptides comprising the sequences set forth in SEQ ID NOs: 5235, 3896, and 5236, wherein each HPV16 E7 peptide may comprise one of the sequences; and HPV18 E6 peptides comprising the sequences set forth in SEQ ID NOs: 3930, 3945, and 5237, wherein each HPV18 E6 peptide may comprise one of the sequences. 93155272.1 4 060734-783069 [0015] The composition may be administered or may be intended to be administered 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, or 12 times. Each administration may be performed or may be intended to be performed every 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, or 12 weeks. The cancer may be solid tumor, and the composition may be administered or be intended to be administered as one or more series of injection, each consisting of 6 injections. The series of injections may be repeated or intended to be repeated until the solid tumor shrinks or disappears. [0016] In one example, the cancer is a solid tumor, and the dose of the one or more antigens is determined relative to a volume of the tumor. The dose may be at least 1 μg/cm³. The one or more antigens may be administered or intended to be administered in two or more escalating doses. The dose of the one or more antigens may be determined individually for the subject. The starting dose may be determined by an immune assay on autologous peripheral blood mononuclear cells. The starting dose may be determined by a delayed-type hypersensitivity skin test. Each subsequent dose after an immediately preceding dose may be escalated until an objective is achieved in the subject. The objective may be one or more of an objective clinical response, shrinkage of the cancer, and a substantial toxicity. After the objective is achieved, a subsequent dose of the antigens or peptides may be maintained or decreased relative to a preceding dose, or no additional composition may be administered to the subject. [0017] Provided herein is a method of treating a cancer in a subject in need thereof, which may comprise administering to the subject a composition comprising one or more antigens from a Rabies lyssavirus envelope glycoprotein. Also provided herein are use of the Rabies antigen composition in the manufacture of a medicament for treating the cancer in a subject and the Rabies antigen composition for use in treating the cancer in the subject. The subject may have been previously immunized against Rabies with a Rabies vaccine. The Rabies vaccine may be one or more of NOBIVAC®, VANGUARD®, and IMRAB®. The composition may be or may be intended to be administered at the site of the cancer. The cancer may be a solid tumor. The composition may be administered via intratumoral or peritumoral injection. The subject may be a dog. The one or more antigens from the Rabies envelope glycoprotein may comprise one or more peptides each independently comprising the sequence set forth in one of SEQ ID NOs: 5106- 5234. The composition may comprise peptides comprising the sequences set forth in SEQ ID NOs: 5106-5234, and each peptide may comprise one of the sequences. The composition may 93155272.1 5 060734-783069 comprise or may be administered in combination with an adjuvant. The adjuvant may be a Toll- like Receptor 3 (TLR3) agonist, which may comprise poly(I:C). BRIEF DESCRIPTION OF THE DRAWINGS [0018] The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawing(s) will be provided by the Office by request and payment of the necessary fee. [0019] FIG.1A-C depicts a VZV glycoprotein E (gE) vaccine (SHINGRIX) and a HPV type 16 L1 protein-based vaccine (GARDASIL-9), and a protocol to repurpose the vaccines and harness anti-vaccine immunity for cancer immunotherapy. [0020] FIG.2A-C shows IFN-gamma and TNF-alpha production by CD4 and CD8 T cell after VZV or HPV immunization. [0021] FIG.3A-D shows the broad inflammatory cytokine/chemokine responses induced by VZV and HPV vaccines after prime boost immunization. [0022] FIG.4A-D shows that VZV vaccine intratumoral injection delays tumor growth and promotes long-term survival in vaccinated mice. [0023] FIG.5A-B shows that cured (tumor-free) mice after the primary treatment have acquired long-term anti-tumor immunity and protection against secondary challenge. [0024] FIG.6A-D shows that intratumoral injection of an L1 MHC-I restricted peptide epitope with poly(I:C), but not the intratumoral injection of HPV16 L1-based vaccine, delays tumor growth and improves survival in vaccinated mice. [0025] FIG.7A-C shows recall of L1 specific IFN-gamma producing CD8+ T cells and expansion of anti-tumor E7-specific CD8+ T cells in vaccinated C57BL/6 mice after intratumoral injection with L1 peptide and poly(I:C), but not after intratumoral HPV16 L1-based vaccine injection. [0026] FIG.8A-B shows the effect on tumor growth of VZV vaccine intratumoral injection in combination with the injection of the CTLA-4 immune checkpoint in vaccinated C57BL/6 mice. [0027] FIG.9A-D shows the expansion of anti-tumor E7-specific CD8+ T cells and the expansion of VZV vaccine-specific IFN-gamma producing cells after VZV vaccine intratumoral injection in combination with the CTLA-4 immune checkpoint in vaccinated C57BL/6 mice. 93155272.1 6 060734-783069 [0028] FIG.10A-D shows the multiplex cytokine/chemokine responses in tumor tissues after VZV vaccine intratumoral injection in combination with the injection of the CTLA-4 immune checkpoint in vaccinated C57BL/6 mice. [0029] FIG.11A-C shows the effect on tumor growth of the intratumoral injection of a combination of HPV16 L1 peptide and SHINGRIX after VZV and HPV dual vaccination. [0030] FIG.12A-C shows the effect on tumor growth of intratumoral injections of a combination of HPV16 L1 peptide, SHINGRIX, and E7 peptide after VZV and HPV dual vaccination. [0031] FIG.13 shows the effect on survival of the intratumoral injections of a combination of HPV16 L1 peptide, SHINGRIX, and E7 peptide after VZV and HPV dual vaccination. [0032] FIG.14A-C shows the effect of the intratumoral treatments on circulating lymphocytes. [0033] FIG.15A-C show abscopal effect on tumor growth, in a dual flank tumor model, after the intra-tumoral injections of a combination of HPV16 L1 peptide, SHINGRIX, and HPV16 E7 peptide in mice vaccinated with the VZV and HPV vaccines. FIG.15A shows a schematic of the experimental design and FIG.15B-C show the results in primary injected tumors (FIG.15B) and abscopal non-injected tumors (FIG.15C). [0034] FIG.16A-B show improved survival in a dual flank tumor model after the intra-tumoral injections of a combination of HPV16 L1 peptide, SHINGRIX, and E7 peptide in mice vaccinated with the VZV and HPV vaccines. FIG.16A shows the experimental design and FIG. 16B shows the results. [0035] FIG.17A-B show the induction of tumor cell death on injected tumors after intra-tumoral injections of Shingrix alone or combinations of HPV16 L1 peptide with Shingrix or, HPV16 L1 peptide with VZV gE and polyI:C. FIG.17A shows the experimental design and FIG.17B shows the results. [0036] FIG.18A-B show the modulation of the tumor myeloid infiltrate after intra-tumoral injections of Shingrix alone or combinations of HPV16 L1 peptide with Shingrix or poly(I:C). FIG.18A shows the experimental design and FIG.18B shows the results. [0037] FIG.19A-B show the tumor infiltration by CD8+ T cell after intra-tumoral injections of SHINGRIX alone or combinations of HPV16 L1 peptide with SHINGRIX or, HPV16 L1 peptide with VZV gE and poly(I:C). FIG.19A shows the experimental design and FIG.19B shows the results. 93155272.1 7 060734-783069 [0038] FIG.20A-D show the amplification of Rabies-specific CD4⁺ and CD8⁺ T cells after intratumoral injection of poly(I:C) with an overlapping peptide library covering the Rabies antigen vaccine envelope glycoprotein in two MHC haplotypes (H-2b and H-2d) and in two tumor models: breast cancer (4T1) and HPV-associated (TC1). FIG.20A and 20C show experimental designs and FIG.20B and 20D show the respective results. DETAILED DESCRIPTION [0039] The inventors have discovered that subunit vaccine immunity can be repurposed for cancer immunotherapy, as opposed to relying on general anti-viral immunity. This provides an unexpected advantage in that the number of peptides needed to cover the entire repertoire of possible, or even immunodominant, target antigens is much smaller. In particular, the inventors’ method uses intratumoral injection of peptides from the L1 protein of human papillomavirus type 16 (HPV16) or type 18 HPV18 or antigens of the envelope glycoprotein E (gE) of varicella- zoster virus (VZV, a human alphaherpes virus 3) in subjects previously vaccinated with one or more of HPV and VZV vaccines. [0040] Surprisingly, the inventors discovered further that anti-tumor therapeutic effects are vaccine specific. In VZV-immunized subjects, either a truncated VZV gE polypeptide or MHC- II-restricted VZV peptides provide anti-cancer effects. In contrast, in HPV-immunized subjects, the HPV L1 protein, such as that found in GARDASIL-9, does not exhibit anti-cancer activity, while MHC-I- and/or MHC-II-restricted peptides do. The inventors have also discovered that, surprisingly, further combining a tumor associated peptide such as an HPV E7 peptide with intratumoral injection of VZV vaccine antigens enhances anti-tumor activity. For peptide compositions disclosed herein, anti-cancer effects can be achieved by using experimentally validated peptide epitopes, peptides generated by immunogenicity prediction algorithms, or using an overlapping peptide library that covers the entire sequence of the subunit antigens. [0041] The inventors have further discovered that, surprisingly, Rabies antigens can be injected into tumors of mice previously vaccinated against Rabies lyssavirus to treat cancer. Specifically, antigens from the envelope glycoprotein of Rabies virus (strain Pasteur vaccins) (RABV) amplify the T cell response at the tumors. [0042] Well-established protocols to produce good manufacturing practice (GMP) peptides can be used to generate compositions to reactivate CD8 and CD4 T cells induced by subunit 93155272.1 8 060734-783069 vaccines. Because this strategy is tumor antigen agnostic and requires no molecular profiling of the tumor, it is possible that large cohorts of patients could benefit from this therapy. Repurposing a licensed vaccine for immunotherapy presents the advantage that it could be tested immediately in clinical trial while development of cancer immunotherapies generally requires extensive and costly drug development. An estimated lower cost per patient compared to other biologic therapies suggest that this approach could be used in low resource settings, and thereby help to address the vast inequities in access to cancer therapies in low and high resource settings. 1. Definitions. [0043] The terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting. As used in the specification and the appended claims, the singular forms “a,” “an” and “the” include plural referents unless the context clearly dictates otherwise. [0044] For recitation of numeric ranges herein, each intervening number there between with the same degree of precision is explicitly contemplated. For example, for the range of 6-9, the numbers 7 and 8 are contemplated in addition to 6 and 9, and for the range 6.0-7.0, the numbers 6.0, 6.1, 6.2, 6.3, 6.4, 6.5, 6.6, 6.7, 6.8, 6,9, and 7.0 are explicitly contemplated. 2. Vaccine Antigens [0045] Provided herein are vaccine antigens, which may be from varicella-zoster virus (VZV) or human papillomavirus (HPV). When describing compositions comprising one or more antigens and peptides disclosed herein, one or more antigens and peptides may be combined in a single composition or may be administered in a plurality of separate compositions. a. Varicella-zoster virus [0046] The VZV antigens may comprise one or more antigens from a VZV glycoprotein E (gE) protein. The VZV gE protein may comprise the following sequence: MGTVNKPVVGVLMGFGIITGTLRITNPVRASVLRYDDFHTDEDKLDTNSVYEPYYHSDHAESSWVNRGESSRKAYDH NSPYIWPRNDYDGFLENAHEHHGVYNQGRGIDSGERLMQPTQMSAQEDLGDDTGIHVIPTLNGDDRHKIVNVDQRQY GDVFKGDLNPKPQGQRLIEVSVEENHPFTLRAPIQRIYGVRYTETWSFLPSLTCTGDAAPAIQHICLKHTTCFQDVV VDVDCAENTKEDQLAEISYRFQGKKEADQPWIVVNTSTLFDELELDPPEIEPGVLKVLRTEKQYLGVYIWNMRGSDG TSTYATFLVTWKGDEKTRNPTPAVTPQPRGAEFHMWNYHSHVFSVGDTFSLAMHLQYKIHEAPFDLLLEWLYVPIDP TCQPMRLYSTCLYHPNAPQCLSHMNSGCTFTSPHLAQRVASTVYQNCEHADNYTAYCLGISHMEPSFGLILHDGGTT LKFVDTPESLSGLYVFVVYFNGHVEAVAYTVVSTVDHFVNAIEERGFPPTAGQPPATTKPKEITPVNPGTSPLLRYA AWTGGLAAVVLLCLVIFLICTAKRMRVKAYRVDKSPYNQSMYYAGLPVDDFEDSESTDTEEEFGNAIGGSHGGSSYT VYIDKTR (SEQ ID NO: 1). 93155272.1 9 060734-783069 [0047] The VZV gE protein may be a truncated VZV gE protein. The truncated VZV gE protein may comprise the following sequence: MGTVNKPVVGVLMGFGIITGTLRITNPVRASVLRYDDFHTDEDKLDTNSVYEPYYHSDHAESSWVNRGESSRKAYDH NSPYIWPRNDYDGFLENAHEHHGVYNQGRGIDSGERLMQPTQMSAQEDLGDDTGIHVIPTLNGDDRHKIVNVDQRQY GDVFKGDLNPKPQGQRLIEVSVEENHPFTLRAPIQRIYGVRYTETWSFLPSLTCTGDAAPAIQHICLKHTTCFQDVV VDVDCAENTKEDQLAEISYRFQGKKEADQPWIVVNTSTLFDELELDPPEIEPGVLKVLRTEKQYLGVYIWNMRGSDG TSTYATFLVTWKGDEKTRNPTPAVTPQPRGAEFHMWNYHSHVFSVGDTFSLAMHLQYKIHEAPFDLLLEWLYVPIDP TCQPMRLYSTCLYHPNAPQCLSHMNSGCTFTSPHLAQRVASTVYQNCEHADNYTAYCLGISHMEPSFGLILHDGGTT LKFVDTPESLSGLYVFVVYFNGHVEAVAYTVVSTVDHFVNAIEERGFPPTAGQPPATTKPKEITPVNPGTSPLLRYA AWTGGLA (SEQ ID NO: 2). [0048] In one example, the VZV antigen comprises the VZV gE protein or truncated VZV gE protein, or a protein having a sequence at least 85, 90, 95, 96, 97, 98, or 99% identical thereto. In particular, the VZV antigen may be the truncated VZV gE protein. In a further example, the VZV gE protein is from SHINGRIX (GLAXOSMITHKLINE BIOLOGICALS). [0049] The VZV antigen may comprise one or more peptides from the VZV gE protein, which may be MHC-I- or MHC-II-restricted peptides. In one example, the VZV peptides are MHC-II- restricted. The MHC-II-restricted peptides may be 9-mers or 10-mers and may comprise one or more peptides each independently comprising the sequence set forth in one of SEQ ID NOs: 3- 156, or peptides having a sequence at least 85% or 93% identical thereto. The VZV peptides may comprise 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 or more of the peptides from SEQ ID NOs: 3-156. The VZV peptides may also comprise 1-100, 1-50, 1-25, 1- 10, 5-100, 5-50, 5-25, or 5-10 of the peptides. [0050] The MHC-I-restricted VZV peptides may be 9-mers or 10-mers and may comprise one or more peptides each independently comprising the sequence set forth in one of SEQ ID NOs: 157-772 (9-mers) and 773-1387 (10-mers), or peptides having a sequence at least 88% or 90% identical thereto. The VZV peptides may comprise 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 or more of the peptides from one or more of SEQ ID NOs: 157-1387. The VZV peptides may also comprise all, 1-100, 1-50, 1-25, 1-10, 5-100, 5-50, 5-25, or 5-10 of the peptides. b. Human papillomavirus [0051] The HPV antigen may be from an L1 protein of HPV. The HPV may be type 16 or type 18. The HPV16 L1 protein may comprise the following sequence. 93155272.1 10 060734-783069 MSLWLPSEATVYLPPVPVSKVVSTDEYVARTNIYYHAGTSRLLAVGHPYFPIKKPNNNKILVPKVSGLQYRVFRIHL PDPNKFGFPDTSFYNPDTQRLVWACVGVEVGRGQPLGVGISGHPLLNKLDDTENASAYAANAGVDNRECISMDYKQT QLCLIGCKPPIGEHWGKGSPCTNVAVNPGDCPPLELINTVIQDGDMVDTGFGAMDFTTLQANKSEVPLDICTSICKY PDYIKMVSEPYGDSLFFYLRREQMFVRHLFNRAGTVGENVPDDLYIKGSGSTANLASSNYFPTPSGSMVTSDAQIFN KPYWLQRAQGHNNGICWGNQLFVTVVDTTRSTNMSLCAAISTSETTYKNTNFKEYLRHGEEYDLQFIFQLCKITLTA DVMTYIHSMNSTILEDWNFGLQPPPGGTLEDTYRFVTSQAIACQKHTPPAPKEDPLKKYTFWEVNLKEKFSADLDQF PLGRKFLLQAGLKAKPKFTLGKRKATPTTSSTSTTAKRKKRKL- (SEQ ID NO: 1388). [0052] The HPV18 L1 protein may comprise the following sequence. MALWRPSDNTVYLPPPSVARVVNTDDYVTRTSIFYHAGSSRLLTVGNPYFRVPAGGGNKQDIPKVSAYQYRVFRVQL PDPNKFGLPDTSIYNPETQRLVWACAGVEIGRGQPLGVGLSGHPFYNKLDDTESSHAATSNVSEDVRDNVSVDYKQT QLCILGCAPAIGEHWAKGTACKSRPLSQGDCPPLELKNTVLEDGDMVDTGYGAMDFSTLQDTKCEVPLDICQSICKY PDYLQMSADPYGDSMFFCLRREQLFARHFWNRAGTMGDTVPQSLYIKGTGMRASPGSCVYSPSPSGSIVTSDSQLFN KPYWLHKAQGHNNGVCWHNQLFVTVVDTTRSTNLTICASTQSPVPGQYDATKFKQYSRHVEEYDLQFIFQLCTITLT ADVMSYIHSMNSSILEDWNFGVPPPPTTSLVDTYRFVQSVAITCQKDAAPAENKDPYDKLKFWNVDLKEKFSLDLDQ YPLGRKFLVQAGLRRKPTIGPRKRSAPSATTSSKPAKRVRVRARK (SEQ ID NO: 1389). [0053] The HPV antigen may comprise one or more peptides from the HPV16 L1 or HPV18 L1 protein, which may be MHC-I- or MHC-II-restricted peptides. The MHC-II-restricted HPV peptides may be 15-mers and may comprise one or more peptides each independently comprising the sequence set forth in one of SEQ ID NOs: 1390-1513 (HPV16 L1) and 1514- 1637 (HPV18 L1), or peptides having a sequence at least 85% or 93% identical thereto. The HPV peptides may comprise 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 or more of the peptides from one of SEQ ID NOs: 1390-1637. The HPV peptides may also comprise all, 1-100, 1-50, 1-25, 1-10, 5-100, 5-50, 5-25, or 5-10 of the peptides. [0054] The MHC-I-restricted HPV peptides may comprise one or more peptides each independently comprising the sequence set forth in one of SEQ ID NOs: 1638-2135 (HPV16 L1 9-mer peptides), 2136-2632 (HPV16 L110-mer peptides), 2633-3132 (HPV18 L19-mer peptides), 3133-3631 (HPV18 L110-mer peptides), 3632-3645 (HPV16 L1 MHC-I restricted peptides), and 3646-3651 (HPV18 L1 MHC-I restricted peptides), or more particularly SEQ ID NOs: 3632-3645 or 3646-3651, or peptides having a sequence at least 88% or 90% identical thereto. The HPV peptides may comprise 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 or more of the peptides from one or more of SEQ ID NOs: 1638-3651. The HPV peptides may also comprise all, 1-100, 1-50, 1-25, 1-10, 5-100, 5-50, 5-25, or 5-10 of the peptides. 93155272.1 11 060734-783069 c. VZV and HPV antigen combinations [0055] One or more VZV antigens disclosed herein may be combined with one or more HPV antigens. In one example, the VZV antigens comprise the VZV antigens in SHINGRIX and the HPV antigen comprises one or more MHC-I-restricted HPV peptides. d. Tumor-associated antigen combinations [0056] One or more VZV antigens, HPV antigens, or combinations thereof disclosed herein may be combined with one or more tumor-associated antigens. At least one of or all the tumor- associated antigens may be expressed by a tumor in a subject being treated as described herein. Each tumor-associated antigen may be from at least one of E6 oncoprotein and E7 oncoprotein. Each oncoprotein may independently be from one of HPV16, HPV18, HPV31, HPV45, HPV52, and HPV58. Each of the aforementioned HPV types may be a high-risk HPV type. The amino acid sequences of the E6 and E7 oncoproteins from each of the HPV types are provided below. [0057] HPV16 E6: MHQKRTAMFQDPQERPGKLPQLCTELQTTIHDIILECVYCKQQLLRREVYDFAFRDLCIVYRDGNPYAVCDKCLKFY SKISEYRHYCYSVYGTTLEQQYNKPLCDLLIRCINCQKPLCPEEKQRHLDKKQRFHNIRGRWTGRCMSCCRSSRTRR ETQL (SEQ ID NO: 3652) [0058] HPV16 E7: MHGDTPTLHEYMLDLQPETTDLYCYEQLNDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIR TLEDLLMGTLGIVCPICSQKP (SEQ ID NO: 3653) [0059] HPV18 E6 MARFEDPTRRPYKLPDLCTELNTSLQDIEITCVYCKTVLELTEVFEFAFKDLFVVYRDSIPHAACHKCIDFYSRIRE LRHYSDSVYGDTLEKLTNTGLYNLLIRCLRCQKPLNPAEKLRHLNEKRRFHNIAGHYRGQCHSCCNRARQERLQRRR ETQV (SEQ ID NO: 3654) [0060] HPV18 E7 MHGPKATVQDIVLHLEPQNEIPVDLLCHEQLSDSEEENDEIDGVNHQHLPARRAEPQRHTLLCMCCKCEARIELVVE SSADDLRAFQQLFLNTLSFVCPWCASQQ (SEQ ID NO: 3655) [0061] HPV31 E6 MFKNPAERPRKLHELSSALEIPYDELRLNCVYCKGQLTETEVLDFAFTDLTIVYRDDTPYGVCTKCLRFYSKVSEFR WYRYSVYGTTLEKLTNKGICDLLIRCITCQRPLCPEEKQRHLDKKKRFHNIGGRWTGRCIVCWRRPRTETQV (SEQ ID NO: 3656) [0062] HPV31 E7 MRGETPTLQDYVLDLQPEATDLHCYEQLPDSSDEEDVIDSPAGQAKPDTSNYNIVTFCCQCESTLRLCVQSTQVDIR ILQELLMGSFGIVCPNCSTRL (SEQ ID NO: 3657) [0063] HPV45 E6: 93155272.1 12 060734-783069 MARFDDPTQRPYKLPDLCTELNTSLQDVSIACVYCKATLERTEVYQFAFKDLFIVYRDCIAYAACHKCIDFYSRIRE LRYYSNSVYGETLEKITNTELYNLLIRCLRCQKPLNPAEKRRHLKDKRRFHSIAGQYRGQCNTCCDQARQERLRRRR ETQV (SEQ ID NO: 3658) [0064] HPV45 E7: MHGPRATLQEIVLHLEPQNELDPVDLLCYEQLSESEEENDEADGVSHAQLPARRAEPQRHKILCVCCKCDGRIELTV EISAEDLRTLQQLFLSTLSFVCPWCATNQ (SEQ ID NO: 3659) [0065] HPV52 E6: MFEDPATRPRTLHELCEVLEESVHEIRLQCVQCKKELQRREVYKFLFTDLRIVYRDNNPYGVCIMCLRFLSKISEYR HYQYSLYGKTLEERVKKPLSEITIRCIICQTPLCPEEKERHVNANKRFHNIMGRWTGRCSECWRPRPVTQV(SEQ ID NO: 3660) [0066] HPV52 E7: MRGDKATIKDYILDLQPETTDLHCYEQLGDSSDEEDTDGVDRPDGQAEQATSNYYIVTYCHSCDSTLRLCIHSTATD LRTLQQMLLGTLQVVCPGCARL (SEQ ID NO: 3661) [0067] HPV58 E6: MFQDAEEKPRTLHDLCQALETSVHEIELKCVECKKTLQRSEVYDFTFADLRIVYRDGNPFAVCKVCLRLLSKISEYR HYNYSLYGDTLEQTLKKCLKEILIRCIICQRPLCPQEKKRHVDLNKRFHNISGRWTGRCAVCWRPRRRQTQV (SEQ ID NO: 3662) [0068] HPV58 E7: MRGNNPTLREYILDLHPEPTDLFCYEQLCDSSDEDEIGLDGPDGQAQPATANYYIVTCCYTCGTTVRLCINSTATEV RTLQQLLMGTCTIVCPSCAQQ (SEQ ID NO: 3663) [0069] Each tumor-associated antigen may be an MHC-I-restricted peptide from one of the E6 or E7 proteins described above. Each antigen may be a 9-mer. The tumor-associated antigens may comprise 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 or more peptides each independently comprising the sequence set forth in one of SEQ ID NOs: 3664-3814 (HPV16 E6 peptides), 3815-3905 (HPV16 E7 peptides), 3906-4056 (HPV18 E6 peptides), 4057- 4154 (HPV18 E7 peptides), 4155-4296 (HPV31 E6 peptides), 4297-4387 (HPV31 E7 peptides), 4388-4538 (HPV45 E6 peptides), 4680-4778 (HPV45 E7 peptides), 4539-4679 (HPV52 E6 peptides), 5012-5103 (HPV52 E7 peptides), and 4779-4920 (HPV58 E6 peptides), 4921-5011 (HPV58 E7 peptides). The tumor-associated antigens peptides may also comprise all, 1-100, 1- 50, 1-25, 1-10, 5-100, 5-50, 5-25, or 5-10 of the peptides from one of SEQ ID NOs: 3664-5103. [0070] In one example the tumor-associated antigen is from the HPV16 E7 protein. The E7 antigen may comprise the sequence RAHYNIVTF (SEQ ID NO: 3863). In another example, the E7 antigen comprises an MHC-I-restricted long peptide, which may comprise the sequence QAEPDRAHYNIVTFCCKCD (SEQ ID NO: 5104). The E7 antigen may be combined with the 93155272.1 13 060734-783069 truncated VZV gE protein or SHINGRIX. The E7 antigen may also be combined with the truncated VZV gE protein or SHINGRIX, and the HPV16 L1 antigen AGVDNRECI (SEQ ID NO: 1776). e. Rabies vaccine antigens [0071] Provided herein is a Rabies lyssavirus antigen. The Rabies antigen may be from an envelope glycoprotein, which may be an envelope glycoprotein of Rabies virus. The Rabies virus may be strain Pasteur vaccins (RABV). The envelope glycoprotein may comprise the following sequence. MVPQALLFVPLLVFPLCFGKFPIYTIPDKLGPWSPIDIHHLSCPNNLVVEDEGCTNLSGFSYMELKVGYISAIKMNG FTCTGVVTEAETYTNFVGYVTTTFKRKHFRPTPDACRAAYNWKMAGDPRYEESLHNPYPDYHWLRTVKTTKESLVII SPSVADLDPYDRSLHSRVFPGGNCSGVAVSSTYCSTNHDYTIWMPENPRLGMSCDIFTNSRGKRASKGSETCGFVDE RGLYKSLKGACKLKLCGVLGLRLMDGTWVAMQTSNETKWCPPGQLVNLHDFRSDEIEHLVVEELVKKREECLDALES IMTTKSVSFRRLSHLRKLVPGFGKAYTIFNKTLMEADAHYKSVRTWNEIIPSKGCLRVGGRCHPHVNGVFFNGIILG PDGNVLIPEMQSSLLQQHMELLVSSVIPLMHPLADPSTVFKNGDEAEDFVEVHLPDVHERISGVDLGLPNWGKYVLL SAGALTALMLIIFLMTCWRRVNRSEPTQHNLRGTGREVSVTPQSGKIISSWESYKSGGETGL (SEQ ID NO: 5105). [0072] The Rabies antigen may comprise one or more peptides from the envelope glycoprotein. The Rabies peptides may be MHC-II-restricted peptides. The MHC-II-restricted Rabies peptides may be 15-mers and may comprise one or more peptides each independently comprising the sequence set forth in one of SEQ ID NOs: 5106-5234. The Rabies antigens may comprise 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 or more of the sequences set forth in SEQ ID NOs: 5106-5234. The Rabies peptides may also comprise all, 1-100, 1-50, 1-25, 1-10, 5- 100, 5-50, 5-25, or 5-10 of the sequences from SEQ ID NOs: 5106-5234. 3. Peptide Compositions [0073] Provided herein is a composition comprising one or more antigens disclosed herein. The antigen composition may be a pharmaceutical composition, and may comprise one or more pharmaceutically acceptable excipients. Pharmaceutically acceptable excipients suitable for antigens and peptides are known in the art. The pharmaceutically acceptable excipient may comprise one or more of sodium chloride, potassium chloride, monopotassium phosphate, disodium phosphate, L-histidine, polysorbate 80, sodium borate, yeast protein, sucrose, dioleoyl phosphatidylcholine, potassium dihydrogen phosphate, cholesterol, sodium dihydrogen phosphate dihydrate, and disodium phosphate anhydrous. 93155272.1 14 060734-783069 [0074] The antigen composition may independently comprise about 0.5, 1, 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 200, 300, 400, 500, 600, 700, 800, 900, or 1000 μg of each VZV antigen or HPV antigen, or a range thereof. The antigen composition may comprise about 0.5, 1, 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 200, 300, 400, 500, 600, 700, 800, 900, or 1000 μg of each VZV antigen, or a range therof. The antigen composition may comprise about 0.5, 1, 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 200, 300, 400, 500, 600, 700, 800, 900, or 1000 μg of each HPV antigen, or a range thereof. The antigen composition may also comprise a total of 0.5, 1, 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 200, 300, 400, 500, 600, 700, 800, 900, or 1000 μg of the antigens, or a range thereof. In another example, the antigen composition independently comprises about 0.5, 1, 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 200, 300, 400, 500, 600, 700, 800, 900, or 1000 μg of each Rabies antigen or a range thereof. [0075] The antigen composition may comprise one or more adjuvants, or may be administered or co-administered with one or more adjuvants. The antigen composition and the adjuvant may be combined prior to administration. In one example, the antigens have been lyophilized, and the antigen composition is reconstituted with the adjuvant. [0076] In one example, the adjuvant comprises one or more of poly(I:C) (polyinosinic- polycytidylic acid), poly-ICLC (a complex of carboxymethylcellulose, poly(I:C), and poly-L- lysine double-stranded RNA; e.g., HILTONOL), a Toll-like receptor (TLR) agonist (which may be a TLR3 agonist), a RIG-I-like helicase agonist, a STING agonist, and CpG. In a further example, the adjuvant comprises aluminum hydroxyphosphate. In another example, the adjuvant comprises one or more of a 3-O-desacyl-4’-monophosphoryl lipid A (MPL), which may be from Salmonella minnesota; and, a saponin molecule, which may be QS-21 and which may be purified from a plant extract of Quillaja saponaria Molina. In one example, the adjuvant is a QS-21/MPL adjuvant that comprises the MPL and QS-21. In another example, the adjuvant is an MPL adjuvant comprising the MPL, but not QS-21. The adjuvant may independently comprise about 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 200, 300, 400, 500, 600, 700, 800, 900, or 1000 μg of one or more of MPL and QS-1, or a range thereof. [0077] The adjuvant may comprise a liposomal formulation, which may comprise dioleoyl phophatidylcholine (DOPC), cholesterol, or both. The adjuvant may also comprise a saline 93155272.1 15 060734-783069 solution, which may be phosphate-buffered. In one example, the QS-21/MPL adjuvant is a liposomal formulation comprising the MPL, QS-21, dioleoyl phophatidylcholine (DOPC), and cholesterol in a phosphate-buffered saline solution. The QS-21/MPL adjuvant may independently comprise 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, or 100 μg of QS-21 and MPL, or a range thereof. The QS-21/MPL adjuvant may comprise 50 μg each of QS-21 and MPL. In one example, the adjuvant is AS01B (GLAXOSMITHKLINE BIOLOGICALS). [0078] The MPL adjuvant may comprise an aluminum salt. The aluminum salt may be a hydroxide salt, and may be in a particulate form. The aluminum salt may be aluminum hydroxide or aluminum hydroxyphosphate. The MPL may be adsorbed onto the aluminum salt. The MPL adjuvant may comprise 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, or 100 μg MPL, or a range thereof. The MPL adjuvant may comprise 0.1, 0.2, 0.3, 0.4, 0.5, 0.6, 0.7, 0.8, 0.9, or 1.0 mg aluminum hydroxide, or a range thereof. In one example, the MPL adjuvant comprises 50 μg MPL. In another example, the MPL adjuvant further comprises 0.5 mg aluminum hydroxide. In one example, the MPL adjuvant is AS04 (GLAXOSMITHKLINE). The MPL adjuvant may be combined with the peptide composition prior to administration. In one example, the MPL adjuvant and peptide composition are combined with solution comprising one or more, or all of, sodium chloride, sodium dihydrogen phosphate dihydrate, and water (which may be water for injection). [0079] Each of the aforementioned adjuvants may be used in combination with one or more of the VZV antigens and HPV antigens described herein. In one example, the QS-21/MPL adjuvant is AS01B and is used in combination with the VZV antigens, which may in particular be truncated VZV gE. In a further example, the combination of AS01B and truncated VZV gE are SHINGRIX. In another example, the MPL adjuvant is AS04 and is used in combination the HPV antigens. In a further example, the poly(I:C) adjuvant is used in combination with MHC-I- or MHC-II-restricted peptides of one or more of the VZV peptides and HPV peptides. In another example, the poly(I:C) is used in combination with the one or more Rabies antigens. 4. Cancer immunotherapy [0080] Provided herein are a method of treating a cancer, which may comprise administering an antigen composition disclosed herein to a subject, who may be in need thereof; the antigen composition for use in treating cancer; and use of the antigen composition in the manufacture of 93155272.1 16 060734-783069 a medicament for treating cancer. The subject may be human leukocyte antigen (HLA)-A0201 (HLA-A0201)-positive. For treatments involving VZV and HPV antigens, the subject may be a human. For treatments involving Rabies antigens, the subject may be a dog. The cancer may be a tumor, which may be a solid tumor. The tumor may express one or more of an E6 and E7 oncoprotein from HPV16 or HPV18. The tumor may not express an E6 and E7 oncoprotein from HPV16 and HPV18. The solid tumor may be a squamous cell carcinoma, adenocarcinoma, melanoma, sarcoma, lymphoma, head and neck cancer, cervical cancer, breast cancer, prostate cancer, Merkel cell carcinoma, basal cell carcinoma, skin melanoma, mucosal melanoma, bladder cancer, renal cancer, glioblastoma, or glioma. [0081] The antigen composition may be administered intratumorally or peritumorally. The administration may be via injection, mucosal, or transcutaneous. The antigen composition may be administered as a repeated series of injections, which may present low to no risk of inducing interfering anti-drug antibodies in a subject due to the small size of antigenic peptides. The antigen composition may be administered at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, or 12 times, or 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, or 12 times. The administrations may be performed once every 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, or 12 weeks. In one example, the antigen composition is administered 1-3 times. In one example, the administration is once every two weeks for 3 weeks or 6 weeks. In another example, the administration is once every week for 6 weeks. [0082] The starting dose of the antigen may be determined individually for the subject. The dose may be based on one or more of the subject’s weight, age and sex. The dose may maximize therapeutic index and may minimize toxicity. The dose may be based on one or more of tumor volume, tissue localization, level of preexisting immunity, and the extent of necrosis and immune infiltration. MHC-I-restricted expression may not be limited to the tumor cells, such that the binding of one or more antigens to non-tumor cells may lead to off-target toxicity. Thus, the dose of the antigen may be adjusted over the course of treatment. In one example, if tumors recur after treatment was arrested, an additional antigen composition is administered at the same dose as the dose maintained prior to treatment arrest. [0083] The dose of antigen administered to the subject may be based on tumor volume. The antigen dose may be x, y, z, etc. μg/mm³, or a range thereof. The antigen composition may be administered in a dose-escalated manner, such that a subsequent dose of antigen is increased in comparison to a previous dose. In one example, a low dose of the antigen is administered to the 93155272.1 17 060734-783069 subject. If the dose is well tolerated, then a higher dose of the antigen may subsequently be administered. The antigen composition may be administered by repeated injection following single dose or in a dose escalation protocol. A dose escalation protocol may be used to determine the maximum tolerated (MTR) dose and the objective biological dose (OBD). [0084] In one example, the antigen is tested on autologous peripheral blood mononuclear cells (PBMC) of the subject using an assay to measure immune activation in vitro (cytokine, chemokines, cytotoxic activity) and to determine the minimal effective concentration in vitro (MEC). One or more of the MEC in vitro, magnitude of the immune response, and the tumor volume may be used as a benchmark to determine a first dose of antigen to be administered and subsequent escalation. In another example, the antigen is titrated in a delayed-type hypersensitivity (DTH) skin test to assess immune reactivity (this is an innocuous test used to detect prior or ongoing exposure to tuberculosis for example) to determine the lowest effective dose to use in a first administration. [0085] The objective biological response in the subject may be monitored after each administration, which may be based on one or more of an increased in plasma cytokine, recall of T cells in peripheral blood, and immune activation from tumor biopsies. Clinical response of the subject may be measured after each administration, which may be one or more of tumor volume stabilization or shrinkage in one or more of a treated tumor and an untreated tumor. [0086] In a dose escalation protocol, a subsequent dose may be increased in comparison to an immediately preceding dose until an objective is achieved. The objective may be an objective clinical response, tumor shrinkage, or a substantial toxicity in the subject. After the objective is achieved, an immediately subsequent dose of the antigen may be maintained or decreased relative to a preceding dose, which may be an immediately preceding dose. In one example, no additional antigen composition is administered to the subject after the objective is achieved. a. Cancer treatment in VZV- or HPV-vaccinated subjects [0087] The subject may have been previously vaccinated or infected with a virus. The subject may have been vaccinated against VZV or infected with VZV, and the one or more VZV antigens may be administered to the subject. The subject may have received 1, 2, or 3 previous doses of the vaccine before the VZV antigens are administered. The VZV antigens may be administered at least 1, 2, 3, or 4 weeks after the VZV vaccine was administered. In one example, the subject has been vaccinated with SHINGRIX. The vaccine may have been 93155272.1 18 060734-783069 administered intramuscularly or intratumorally. The VZV antigens may be used in combination with another cancer immunotherapy. The other cancer immunotherapy may be one or more of anti-CTLA-4, PD-1, PD-L1, LAG-3, TIM-3, NKG2A, Gal-9, CD39-CD73 or ICOS-ICOS-L antibodies; a cytokine, which may be IL-15; a small molecule immune modulator; a PARP inhibitor, which may be a Chk1 inhibitor; a CAR T cells; a TCR engineered T cell; or a cancer- associated antigen vaccine. [0088] The subject may have been vaccinated against HPV or infected with HPV, and the HPV antigens may be administered to the subject. The subject may have received 1, 2, or 3 previous doses of the vaccine before the HPV antigens are administered. The HPV antigens may be administered at least 1, 2, 3, or 4 weeks after the HPV vaccine was administered. In one example, the subject has been vaccinated with GARDASIL, GARDASIL-9, or CERVARIX. The vaccine may have been administered intramuscularly or intratumorally. [0089] In one example, a combination of VZV antigens and HPV antigens are administered. The subject may have been previously vaccinated against one or more of VZV and HPV, and the combination of VZV antigens and HPV antigens may be administered to the subject. In a further example, the subject has been previously vaccinated against both VZV and HPV, and a combination of VZV antigens and at least one tumor-associated antigen or a combination of VZV antigens, HPV antigens, and at least one tumor-associated antigen is administered to the subject. The subject may have a cancer associated with HPV16 or HPV18. In one example, the truncated VZV gE protein, the HPV16 L1 antigen AGVDNRECI (SEQ ID NO: 1776), and the HPV16 E7 antigen RAHYNIVTF (SEQ ID NO: 3863) are administered. [0090] In a further example, the truncated VZV gE protein or SHINGRIX in combination with one or more of the HPV16 L1 antigen AGVDNRECI (SEQ ID NO: 1776) and the MHC-II- restricted HPV16 E7 long peptide are administered. The administration may also include AS01_B or poly(I:C). [0091] The subject may have a human leukocyte antigen serotype of HLA-A0201. The HLA- A0201 subject may have an HPV-negative cancer, which may not express an E6 oncoprotein and an E7 oncoprotein from HPV16 or HPV18. SHINGRIX or truncated VZV gE may be administered to the subject in combination with an HPV16 L1 peptide comprising the sequence ICWGNQLFV (SEQ ID NO: 1960) (amino acids 323-331 of HPV16 L1) and an HPV18 L1 93155272.1 19 060734-783069 peptide comprising the sequence NVFPIFLQM (SEQ ID NO: 3649) (amino acids 54-62 of HPV18 L1). [0092] The HLA-A0201-positive subject may have a tumor associated with HPV16 or HPV18, which may express one or more of an E6 oncoprotein and an E7 oncoprotein from HPV16 or HPV18. SHINGRIX or truncated VZV gE may be administered to the subject in combination with an HPV16 L1 peptide comprising the sequence ICWGNQLFV (SEQ ID NO: 1960) and an HPV18 L1 peptide comprising the sequence NVFPIFLQM (SEQ ID NO: 3649), and further in combination with a HPV16 E7 peptides independently comprising the sequences YMLDLQPETT (SEQ ID NO: 5235), LLMGTLGIV (SEQ ID NO: 3896), and TLGIVCPI (SEQ ID NO: 5236) and HPV18 E6 peptides independently comprising the sequences LQDIEITCV (SEQ ID NO: 3930), ELTEVFEFA (SEQ ID NO: 3945), and KLTNTGLYNL (SEQ ID NO: 5237). b. Cancer treatment in Rabies-vaccinated dogs [0093] The subject may be a dog and may have been previously vaccinated with a Rabies vaccine against a Rabies lyssavirus. The Rabies vaccine may comprise one or more of NOBIVAC®, VANGUARD®, and IMRAB®. In one example, all of the one or more Rabies peptides comprising the sequences set forth SEQ ID NOs: 5106-5234 is administered. In another example, at least 10, 20, 30, 40, 50, 60, 70, 80, 90, or 100 of the one or more Rabies antigens is administered. The Rabies antigens may be administered with a TLR3 agonist, which may comprise poly(I:C). [0094] The present invention has multiple aspects, illustrated by the following non-limiting examples. Example 1 HPV and VZV Vaccine Antigens and Cancer Immunotherapy [0095] This example shows that antigens of anti-viral vaccines can be repurposed for local cancer therapy as a safer and off-the-shelf agent, and that selected peptides derived from the vaccine antigens can be used to recall preexisting anti-vaccine T cell responses. A combination with an immune checkpoint blockade antibody (CTLA-4) appears to further improve the treatment efficacy and opens a road map for clinical evaluation. 93155272.1 20 060734-783069 [0096] GARDASIL-9 is a 9-valent HPV prophylactic vaccine for the prevention of cervical cancer and genital warts. GARDASIL-9 (MERCK) was approved in 2014 and includes 9 HPV types, including HPV16, whereas the original HPV vaccine GARDASIL, a 4-valent vaccine, also includes HPV16. CERVARIX (GLAXOSMITHKLINE) is a bivalent HPV vaccine including HPV16 and an adjuvant composed of aluminum hydroxide and a TLR4 agonist, monophosphoryl lipid A (MPL, also referred to as MPLa). All three vaccines confer antibody- mediated protection and induce a strong CD8+ T cells response against the L1 capsid protein. All three vaccines are recommended for 9–26-year-old individuals (FIG.1A). SHINGRIX is a subunit vaccine against shingles recommended for individuals 50-years and older. It is composed of the varicella-zoster antigen ectodomain glycoprotein gE and the adjuvant AS01_B disclosed herein. SHINGRIX elicits antibody-mediated protection and a strong CD4 T cell response in human subjects (FIG.1B). FIG.1C depicts a protocol to repurpose subunit vaccines and to harness anti-vaccine immunity for cancer immunotherapy. Naïve mice were prime/boost immunized with 50 μL of SHINGRIX, GARDASIL OR CERVARIX subunit vaccines. A week following booster immunization, mice were injected subcutaneously with 5x10^5 TC-1 tumor cells that express the oncogenes HaRas and HPV16 E6 and E7 (Lin KY, Guarnieri FG, Staveley- O'Carroll KF, Levitsky HI, August JT, Pardoll DM, Wu TC. Cancer Res.1996 Jan 1;56(1):21- 6.). When tumors reached 50 to 100 mm³ size, the tumors were injected multiple times with either the corresponding vaccine (10 μL) or selected MHC-2 (SHINGRIX) or MHC-1 (GARDASIL-9) restricted epitopes combined with a selected immune modifier (e.g., poly(I:C), agonist for TLR3 and RIG-I and MDA-5). [0097] FIG.2A describes the design of experiments in which C57BL/6 mice were immunized with 50 μL Shingrix or 50 μL of GARDASIL-9 intramuscular (1/10th of a human dose). Two weeks after booster immunization, splenocytes were restimulated with overlapping peptide libraries encompassing the entire sequence of VZV gE (PEPMIX™ VZV gE) or HPV16 L1 capsid protein (PEPMIX™ HPV16 L1) in presence of brefeldin A and monensin. Specific cytokine production by CD4 (FIG.2B) and CD8 T cells (FIG.2C) was assessed by flow cytometry using an intracellular cytokine staining protocol for IFN-gamma and TNF-alpha. [0098] FIG.3A describes the design of experiments in which C57BL/6 mice were immunized with 50 μL Shingrix or 50 μL of Gardasil-9 intramuscular (1/10th of a human dose). Two weeks after booster immunization, splenocytes were restimulated in complete medium alone (FIG.3B) 93155272.1 21 060734-783069 or supplemented with overlapping peptide libraries encompassing the entire sequence of (FIG. 3C) VZV gE (PEPMIX™ VZV gE) or (FIG.3D) HPV16 L1 capsid protein (PEPMIX™ HPV16 L1). Supernatants were harvested after 48hrs culture and analyzed with the LEGENDPLEX™ MU Cytokine Release Syndrome Panel (IFN-γ, IL-10, CCL4, IFN-α, CXCL9, CXCL10, TNF-α, IL-6, VEGF, IL-4, CCL3, CCL2, GM-CSF). Data are shown as a heatmap of the z-score for each analyte. The results demonstrate broad inflammatory cytokine/chemokine responses induced by SHINGRIX and GARDASIL after prime boost immunization. [0099] FIG.4A shows the design of experiments in which C57BL/6 mice were immunized with 50 μL Shingrix intramuscular (1/10th of a human dose). One week after booster immunization, mice were transplanted with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins. When tumors reached a volume of 50 to 100 mm³, they were injected intratumorally with SHINGRIX (10 μL or 1/50th of human dose), or a mixture of an MHC-2 restricted gE peptide epitope (1 μg) with poly(I:C) (50 μg) in 10 μL or saline as a control (10 μL). FIG.4B and C shows that intratumoral injection of SHINGRIX alone improved survival and delayed tumor growth compared to saline alone. Intratumoral injection of a gE minimal peptide epitopes improved survival and delayed tumor growth as well, suggesting that recall of CD4 T cells could contribute to the antitumor response. Mantel–Cox test for survival analysis and Dunn's test for tumor-volume analysis. P values are shown directly in the survival graph and next to the legend for the tumor growth analysis (*P < 0.01). FIG.4D shows that immunization with SHINGRIX induced a robust IgG antibody response against gE in serum of SHINGRIX vaccinated mice (mean endpoint titer as Log10). [0100] FIG.5A shows the design of experiments in which C57BL/6 mice were immunized with 50 μL SHINGRIX intramuscular (1/10th of a human dose). One week after booster immunization, mice were transplanted with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins. When tumors reached a volume of 50 to 100 mm³, they were injected intratumorally with Shingrix (10 μL or 1/50th of human dose), or a mixture of an MHC-II- restricted gE peptide (SRKAYDHNSPYIWPRNDYDG (SEQ ID NO: 156) epitope (1 μg) with poly(I:C) (50 μg) in 10 μL or saline as a control (10 μL). The gE2 peptide was selected from a previous report. FIG.5B shows that complete tumor clearance leads to long protection against secondary challenge with the same TC1 tumor cells injected in the opposite flank from the primary tumor injection site. 93155272.1 22 060734-783069 [0101] FIG.6A shows the design of experiments in which C57BL/6 mice were immunized with 50 μL GARDASIL intramuscular (1/10th of a human dose). One week after booster immunization, mice were transplanted with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins. When tumors reached a volume of 50 to 100 mm³, they were injected intratumorally with GARDASIL (10 μL or 1/50th of human dose), or a mixture of an MHC-I- restricted L1 peptide (AGVDNRECI (SEQ ID NO: 1776)) epitope (1 μg) with poly(I:C) (50 μg) in 10 μL, or saline as a control (10 μL). FIG.6B and C show that intratumoral injection of GARDASIL alone did not improve survival or delayed tumor growth compared to saline alone. In stark contrast, intratumoral injection of L1 minimal peptide epitopes led to complete tumor clearance and long-term remission. Mantel–Cox test for survival analysis and Dunn's test for tumor-volume analysis. P values are shown directly in the survival graph and next to the legend for the tumor growth analysis (****P < 0.0001, **P < 0.01). FIG.6D shows that immunization with SHINGRIX induces a robust IgG antibody response against L1 HPV16 capsid protein in serum of SHINGRIX vaccinated mice (mean endpoint titer as Log10). [0102] FIG.7A shows the design of experiments in which C57BL/6 mice were immunized with 50μL GARDASIL intramuscular (1/10th of a human dose). One week after booster immunization, mice were transplanted with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins. When tumors reached a volume of 50 to 100 mm³, they were injected intratumorally with GARDASIL (10 μL or 1/50th of human dose), or a mixture of an MHC-I- restricted L1 peptide epitope (1 μg) with poly(I:C) (50 μg) in 10μL, or saline as a control (10 μL). FIG.7B shows IFN-gamma production by CD8+ T cells purified from blood samples collected 24hrs after the last intratumoral injection. Blood samples were incubated in presence of purified antigen presenting cells and a protein transport inhibitor cocktail (Brefeldin A and Monensin) with the overlapping HPV 16 L1 peptide library PEPMIX JPT for 8hrs. Cells were stained with a cocktail of antibodies containing anti CD4, CD8, CD3, CD44 for surface staining. After fixation and permeabilization cells were incubated with a cocktail of including IFN- gamma, IL-2 and TNF-alpha for intracellular staining in presence of permeabilization buffer (BD). GARDASIL intratumoral injection did not significantly increase the frequency of CD8+ T cells against the L1 antigen. However, intratumoral injection of the minimal MHC-I-restricted L1 epitope with poly(I:C) led to the expansion of L1-specific IFN-gamma producing CD8+ T cells of mice. FIG.7C shows the CD8 + T cell response, which was performed by flow 93155272.1 23 060734-783069 cytometry using an MHC-1 multimer probe that detects HPV16 E7 CD8+ T cells specific to the TC-1 tumor. The intratumoral injection of L1 peptide with poly(I:C) caused the increase in E7- specific CD8+ T cells compared to saline treated group whereas the intratumoral injection of GARDASIL did not. Data are shown as individual values and mean ± SEM (n = 9–10). Statistical significance was assessed by one-way ANOVA followed by Tukey’s test for multiple comparison analysis. ***P < 0.001, **P < 0.01, *P < 0.05, ns, not significant. [0103] FIG.8A shows the design of experiments in which C57BL/6 mice were immunized with 50 μL SHINGRIX intramuscular (1/10th of a human dose). One week after booster immunization, mice were transplanted with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins. When tumors reached a volume of 50 to 100 mm³, they were injected intratumorally with SHINGRIX (10 μL or 1/50th of human dose) alone, or in combination with intraperitoneal injection of 200 μg of a CTLA-4 blocking monoclonal antibody (Clone 9D9, BIOXCELL). Mice were treated twice a week for 3 weeks for a total of 6 injections. FIG.8B shows that intratumoral injection of SHINGRIX improved survival compared to mice treated with saline, unvaccinated. Intratumoral injection of SHINGRIX in combination with CTLA-4 further improved survival compared to CTLA-4 alone or saline treated mice suggesting the cooperation between SHINGRIX and CTLA-4 antibodies. Statistical significance was assessed by Mantel–Cox test for survival analysis and Dunn's test for tumor-volume analysis. P values are shown directly in the survival graph and next to the legend for the tumor growth analysis (****P < 0.0001, ***P < 0.001, n.s.: not significant). [0104] FIG.9A shows the design of experiments in which C57BL/6 mice were immunized with 50 μL Shingrix intramuscular (1/10th of a human dose). One week after booster immunization, mice were transplanted with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins. When tumors reached a volume of 50 to 100 mm³, they were injected intratumorally with SHINGRIX (10 μL or 1/50th of human dose) alone, or in combination with intraperitoneal injection of 200 μg of a CTLA-4 blocking monoclonal antibody (Clone 9D9, BIOXCELL). Mice were treated twice a week for 3 weeks for a total of 6 injections. FIG.9B shows the expansion of anti-tumor E7-specific CD8+ T cells in tumors, and FIG.9C shows the expansion in draining lymph nodes. FIG.9D shows SHINGRIX-specific IFN-gamma producing cells in spleen measured by mouse IFN-gamma ELISPOT and expressed as spot forming units (DIACLONE). Data are shown as individual values and mean ± SEM (n = 10-12). Statistical 93155272.1 24 060734-783069 significance was assessed by one-way ANOVA followed by Tukey’s test for multiple comparison analysis. ***P < 0.001, **P < 0.01, *P < 0.05, ns, not significant. [0105] FIG.10A shows the design of experiments in which C57BL/6 mice were immunized with 50 μL SHINGRIX intramuscular (1/10th of a human dose). One week after booster immunization, mice were transplanted with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins. When tumors reached a volume of 50 to 100 mm³, they were injected intratumorally with SHINGRIX (10 μL or 1/50th of human dose) alone, or in combination with intraperitoneal injection of 200 μg of a CTLA-4 blocking monoclonal antibody (Clone 9D9, BIOXCELL). Mice were treated twice a week for 3 weeks for a total of 6 injections. Tumor tissues were collected 36hrs after the last of 3 consecutive intratumoral injections. Tumor lysates were obtained by freeze thaw cycle and mechanical tissue disruption (TISSUE LYZER, QUIAGEN) in presence of benzonase and protease cocktail inhibitors. Tissue lysates were analyzed with the LEGENDPLEX™ MU Cytokine Release Syndrome Panel (IFN-γ, IL-10, CCL4, IFN-α, CXCL9, CXCL10, TNF-α, IL-6, VEGF, IL-4, CCL3, CCL2, GM-CSF). In FIG. 10B, data are shown as a heatmap of the z-score for each analyte and in FIG.10C-D as individual values and mean ± SEM (n = 5-7). Statistical significance was assessed by one-way ANOVA followed by Tukey’s test for multiple comparison analysis. ***P < 0.001, **P < 0.01, *P < 0.05, ns, not significant. [0106] FIG.11A shows the design of experiments in which C57BL/6 mice were immunized simultaneously with 50 μL SHINGRIX and GARDASIL-9 intramuscular (1/10th of a human dose). One week after booster immunization, mice were transplanted with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins. When tumors reached a volume of 50 to 100 mm³, they were injected intratumorally twice a week for 3 weeks for total of 6 injections with SHINGRIX (10 μL or 1/50th of human dose), together with MHC-I-restricted HPV16 L1 peptide epitope (1 μg), SHINGRIX alone, HPV16 L1 peptide alone, HPV16 L1 with poly(I:C), VZV gE protein with poly(I:C), VZV gE protein (1 μg) with poly(I:C) and HPV16 L1, or saline as a control. FIG.11B shows mean tumor volume measurements until all mice in the control group (saline treated) reached an experimental humane endpoint. FIG.11C shows individual tumor volume measurements until all mice reached an experimental humane endpoint. The tumor volume measurements show that intratumoral injection of SHINGRIX together with L1 peptides significantly delayed tumor growth and improved survival compared to saline, HPV16 93155272.1 25 060734-783069 L1 peptides or SHINGRIX, given separately. Statistical analysis was performed using Dunn’s test for tumor-volume for SHINGRIX + HPV16 L1 peptide group compared to all other experimental treatment groups (groups n=6-7). P values are shown next to the legend in the mean tumor growth graph (*P < 0.05, ***P < 0.001). [0107] The experiments described above showed that SHINGRIX, a VZV vaccine containing the glycoprotein E (gE) antigen combined with the adjuvant AS01B, and GARDASIL-9, an HPV vaccine containing the L1 virus-like particles combined with alum induce CD4 and CD8 T cell responses, respectively (FIG.2B). In addition, SHINGRIX works at least partly as a standalone therapy or in combination with a second approved drug, anti-CTLA4 monoclonal antibodies (Ipilimumab). Intratumoral injection of SHINGRIX alone or with CTLA-4, delayed tumor growth in prevaccinated mice and led to complete regression in some cases. Such an anti-tumor response was associated with the induction of CD8+ T cell responses against the HPV16 E7 tumor antigen and to the immune activation of the tumor immune microenvironment. The injection of vaccine derived epitopes such as a selected MHC-II-restricted gE minimal peptide epitope combined with poly(I:C) also led to durable remission, which underscores the importance to harness preexisting anti VZV gE CD4 T cells. [0108] The experiment also showed that in contrast to SHINGRIX, GARDASIL-9 intratumoral injection alone in vaccinated mice did not delay tumor growth or cause tumor rejection. This suggests that the virus-like particle antigens are inefficiently cross-presented in the MHC class I by the tumor cells. In contrast, injection of GARDASIL-derived peptide epitopes had an unexpectedly strong anti-tumor activity. Indeed, the injection of selected MHC-I-restricted L1 minimal peptide epitopes led to complete and durable remission suggesting efficient tumor control by L1-specific CD8 T cells. In addition, the injection of L1 minimal MHC-1 restricted peptide epitopes led to expansion of L1-specifiic interferon gamma producing CD8+ T cells and elicited anti-tumor response against a tumor antigen HPV16 E7. The combination of SHINGRIX and an HPV16 L1 MHC-I-restricted peptide led to tumor control suggesting that the addition of an MHC-I-restricted peptide to an existing vaccine can lead to a composition with dramatically improved anti-cancer properties. 93155272.1 26 060734-783069 Example 2 Combining a Tumor-Associated Antigen with VZV or HPV Vaccine Antigens Effectively Treat Tumors in Immunized Subjects [0109] This example demonstrates that intratumoral injection of a tumor-associated antigen with a VZV vaccine antigen enhances anti-tumor activity of the VZV vaccine antigen alone. In particular, dual vaccination with a VZV gE vaccine (SHINGRIX) and HPV16 L1 protein-based vaccine (GARDASIL-9), followed by intratumoral injection with either a combination of SHINGRIX and a tumor-associated MHC-I-restricted HPV16 E7 peptide or a combination of SHINGRIX, an MHC-I-restricted HPV16 L1 peptide, and the tumor-associated E7 peptide, results in potent anti-tumor activity. [0110] FIG.12A shows the design of experiments in which C57BL/6 mice were immunized simultaneously with 50 μL SHINGRIX and GARDASIL-9 intramuscular (1/10th of a human dose). Five days after booster immunization, mice were transplanted subcutaneously with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins. When tumors reached a volume of 50 to 100 mm³, they were injected intratumorally with SHINGRIX (20 μL or 1/25th of human dose), together with MHC-I-restricted E7 peptide epitope (2.5 μg) (RAHYNIVTF; SEQ ID NO: 3863), with MHC-1 restricted HPV16 L1 peptide epitope (1 μg) (AGVDNRECI; SEQ ID NO: 1776), with both the E7 peptide epitope and the L1 peptide epitope or SHINGRIX alone or E7 peptide alone or saline as a control. FIG.12B shows mean tumor volume measurements up until day 35 of the experiment. FIG.12C shows individual tumor volume measurements up until day 35. The tumor volume measurements show that intratumoral injection of SHINGRIX together with either E7 peptide, L1 peptide, or especially, both peptides, significantly delayed tumor growth and improved survival compared to saline, E7 peptide or SHINGRIX, given separately. The number of tumor-free mice at day 35 is listed for each group. Statistical analysis was performed using a multiple-comparison Ordinary one-way ANOVA test for tumor-volume (groups n=10). P values are shown next to the legend in the mean tumor growth graph (*P < 0.05, ***P < 0.001). [0111] FIG.13 shows the survival (complementing the tumor growth charts in FIG.12) of C57BL/6 mice treated with the different experimental treatments. The mice were immunized simultaneously with 50 μL SHINGRIX and GARDASIL-9 intramuscular (1/10th of a human dose). Five days after booster immunization, mice were transplanted subcutaneously with 93155272.1 27 060734-783069 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins. When tumors reached a volume of 50 to 100 mm³, they were injected intratumorally with SHINGRIX (20 μL or 1/25th of human dose), together with MHC-I-restricted E7 peptide epitope (2.5 μg), with MHC-1 restricted HPV16 L1 peptide epitope (1 μg), with both the E7 peptide epitope and the L1 peptide epitope or Shingrix alone or E7 peptide alone or saline as a control. The survival curve shows that while intratumoral injection of SHINGRIX alone prolongs survival, intratumoral injection of SHINGRIX together with either E7 peptide, L1 peptide, or especially, both peptides, substantially prolongs survival compared to saline, E7 peptide or SHINGRIX alone, given separately. Statistical analysis was performed using a Log-rank (Mantel-Cox) test, comparing each experimental group with the saline treatment (groups n=10). P values are shown next to the legend in the mean tumor growth graph (*P < 0.05, ***P < 0.001). [0112] FIG.14 shows the effect on circulating lymphocytes of the intratumoral injections, after the fifth intratumoral injection was administered. FIG.14A shows the relative activity of CD4+ T-Cells and CD8+ T-Cells in each treatment group as measured by expression of the CD44 marker and lack of expression of the CD62L marker. FIG.14B shows the specificity of CD4+ T- Cells to the gE protein (a primary component of the VZV vaccine the mice received). Peripheral blood mononuclear cells (PBMCs) collected from mice were co-cultured with antigen-presenting cells and re-stimulated with an overlapping library of gE peptides for 12 hours before measuring the production of interferon-gamma with an intracellular staining. FIG.14C shows the percentage of CD8+ T-Cells that are specific to either L1 (a protein the mice were immunized against, and a peptide received in two treatment groups) and E7 (the driving antigen of the TC-1 tumor model, and a peptide received in three treatment groups). The figure shows that intratumoral injection of SHINGRIX together with either E7 peptide, L1 peptide, or especially, both peptides, significantly increases the proportion of both activated CD4+ T-Cells as well as activated CD8+ T-Cells, and increases the proportion of T-Cells specific to each antigen (gE, L1, and E7) in the blood. (groups n=8-10). P values are shown next to the legend in the mean tumor growth graph (*P < 0.05, ***P < 0.001). 93155272.1 28 060734-783069 Example 3 VZV and HPV Antigens Have Abscopal Effects on HPV16 E6- and E7-Positive Tumor Growth and Improve Survival in Immunized Subjects [0113] This example demonstrates that SHINGRIX (or truncated VZV gE protein) with a HPV16 E7 tumor peptide epitope alone or together with the HPV16 L1 vaccine peptide epitope leads to an abscopal effect on a non-injected secondary tumor in a dual flank model. The combination of SHINGRIX with the HPV16 E7 peptide and the HPV16 L1 peptide epitope leads to the most pronounced effects on the primary injected tumor and the secondary non-injected tumor. This example also demonstrates that SHINGRIX alone; SHINGRIX with a HPV16 L1 peptide; or poly(I:C), VZV gE protein, and a HPV16 L1 peptide injected in a primary tumor profoundly alters the myeloid infiltrate compartment and promotes the recruitment of vaccine- specific and tumor-specific CD8+ T cells. [0114] FIG.15A shows the design of an experiment in which C57BL/6 mice were immunized simultaneously with 50 μl SHINGRIX and GARDASIL-9 intramuscular (1/10th of a human dose). Five days after booster immunization, mice were transplanted subcutaneously on the right flank with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins (primary tumor). Five days after primary tumor implantation, 5x10^5 TC-1 tumor cells were injected on the left flank (secondary tumor). When primary tumors reached a volume of 50 to 100 mm³, mice were randomized and the primary tumor was injected intratumorally with saline as a control or SHINGRIX (20 μL or 1/25th of human dose) or with the adjuvant AS01B (20 μL or 1/25th of human dose) together with the MHC-I restricted E7 long peptide (QAEPDRAHYNIVTFCCKCD; SEQ ID NO: 5104) epitope (2.5 μg), with MHC-I-restricted HPV16 L1 minimal peptide (AGVDNRECI; SEQ ID NO: 1776) (1 μg) or with both the E7 and the L1 peptide epitopes. FIG.15B shows individual injected primary tumor volume measurements for each treatment group. FIG.15C shows individual non-injected secondary tumor volume measurements for each treatment group. The tumor volume measurements show abscopal effect such that intra-tumoral injection of SHINGRIX together with L1 peptide significantly delayed growth of the primary tumor in the SHINGRIX and L1 and of the secondary non injected tumor compared to saline. The combination of AS01B or SHINGRIX with E7 peptide led to complete clearance of secondary abscopal tumor, but SHINGRIX with E7 led significantly better control of the primary injected tumor. The combination of SHINGRIX 93155272.1 29 060734-783069 with L1 and E7 led to complete clearance of both primary and secondary tumors. The number of tumor-free mice at day 95 is listed for each group. Statistical analysis was performed using a multiple-comparison Ordinary one-way Anova test for tumor-volume (groups n=10). [0115] FIG.16A shows the experimental design which follows the schedule utilized in FIG.15. FIG.16B shows that intratumoral injection of the primary tumor with SHINGRIX and L1 significantly increased survival (median survival, MS = 35 days) of mice compared to saline treated control (MS = 25 days). Mice treated with SHINGRIX and E7, AS01_B and E7, or SHINGRIX with L1 and E7 did not reach median survival (MS= N/a) with 90% to 100% survival at day 95. Statistical analysis was performed using a Log-rank (Mantel-Cox) test, comparing each experimental group with the saline treatment (groups n=10). P values are shown next to the legend in the mean tumor growth graph (*P < 0.05, ***P < 0.001). [0116] FIG.17A shows the design of an experiment in a single tumor challenge model in which C57BL/6 mice were immunized simultaneously with 50 μl SHINGRIX and GARDASIL-9 intramuscular (1/10th of a human dose). Five days after booster immunization, mice were transplanted subcutaneously with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins. When tumors reached a volume of 50 to 100 mm³, mice were randomized and each tumor was injected intratumorally with either saline as a control or SHINGRIX (20 μL or 1/25th of human dose) alone or in combination with the MHC-I-restricted restricted HPV16 L1 minimal peptide (AGVDNRECI; SEQ ID NO: 1776) (1 μg), or with polyI:C (50 μg) in combination with VZV glycoprotein E (gE: 2 μg) and HPV16 L1 minimal peptide (AGVDNRECI; SEQ ID NO: 1776) (1 μg). FIG.17B shows the viability of tumor cells 36 hrs after the last of three consecutive intratumoral treatments. Briefly, tumor masses were harvested and single cell suspension were obtained after mechanical and enzymatic dispersion. Single suspensions were stained with a mixture of antibodies to discriminate immune cells and tumor cells. Cells were labelled with a fluorescent vital dye to measure cellular viability in the single cell suspension. FIG.17B shows treatment with SHINGRIX alone increased tumor cell cytotoxicity (reduction in CD45 negative cells viability). Groups treated with SHINGRIX and the MHC-I-restricted peptide epitope HPV16 L1 or with a combination of poly(I:C), VZV gE and the MHC-I-restricted peptide epitope HPV16 L1 displayed a more pronounced reduction in tumor cell viability. Data are shown as individual values and mean ± SEM (n = 5). Statistical 93155272.1 30 060734-783069 significance was assessed by one-way ANOVA for multiple comparison analysis relative to saline control group. *P < 0.05, ***P < 0.001. [0117] FIG.18A shows the design of an experiment in a single tumor challenge model in which C57BL/6 mice were immunized simultaneously with 50 μl SHINGRIX and GARDASIL-9 intramuscular (1/10th of a human dose). Five days after booster immunization, mice were transplanted subcutaneously with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins. When tumors reached a volume of 50 to 100 mm³, mice were randomized and each tumor was injected intratumorally with either saline as a control or Shingrix (20 μL or 1/25th of human dose) alone or in combination with the MHC-I-restricted restricted HPV16 L1 minimal peptide (AGVDNRECI; SEQ ID NO: 1776) epitope (1 μg), or with poly(I:C) (50 μg) in combination with VZV gE (gE: 2 μg) and HPV16 L1 minimal peptide (AGVDNRECI; SEQ ID NO: 1776) (1 μg). FIG.18B shows the analysis of the myeloid cell infiltrate at 36 hrs after the last of three consecutive intratumoral treatments. Briefly, tumor masses were harvested and single cell suspension were obtained after mechanical and enzymatic dispersion. Single suspensions were stained with a mixture of antibodies to discriminate immune cells and tumor cells. Cells were labelled with a fluorescent vital dye to exclude dead cells from the analysis. The markers used to define each immune cell population were as follow: leucocytes (CD45⁺), neutrophils (CD45⁺CD11b⁺F4/80-Ly6G⁺), monocytes (CD45⁺CD11b⁺F4/80-Ly6C^highLy6G-), tumor macrophages (CD45⁺CD11b⁺F4/80⁺Ly6C-Ly6G-), intermediate monocytes (CD45⁺CD11b⁺F4/80-Ly6C^dimLy6G-). FIG.18B shows that intratumoral treatment with SHINGRIX alone induced the recruitment of neutrophils and reduction and macrophage which was statistically significant. SHINGRIX alone treatment also led to an increased monocytes infiltration albeit not statistically significant. Intratumoral treatment with SHINGRIX and the MHC-I-restricted peptide epitope HPV16 L1 or with a combination of poly(I:C), gE and the MHC-I-restricted peptide epitope HPV16 L1 led to the most pronounced increase in neutrophil infiltration and a reduction in the infiltration by tumor macrophages and intermediate monocytes. Data are shown as individual percentage within live cells or CD45⁺ cells populations as indicated on the Y-axis and mean ± SEM (n = 5). Statistical significance was assessed by one-way ANOVA for multiple comparison analysis relative to saline control group. *P < 0.05 , ***P < 0.001. 93155272.1 31 060734-783069 [0118] FIG.19A shows the design of an experiment in a single tumor challenge model in which C57BL/6 mice were immunized simultaneously with 50 μl SHINGRIX and GARDASIL-9 intramuscular (1/10th of a human dose). Five days after booster immunization, mice were transplanted subcutaneously with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins. When tumors reached a volume of 50 to 100 mm³, mice were randomized and each tumor was injected intratumorally with either saline as a control or SHINGRIX (20 μL or 1/25th of human dose) alone or in combination with the MHC-I-restricted restricted HPV16 L1 minimal peptide (AGVDNRECI; SEQ ID NO: 1776) epitope (1 μg), or with polyI:C (50 μg) in combination with VZV glycoprotein E (gE: 2 μg) and HPV16 L1 minimal peptide (AGVDNRECI; SEQ ID NO: 1776) (1 μg). FIG.19B shows the analysis of the CD8⁺ T cell infiltrate at 36 hrs after the last of three consecutive intratumoral treatments. Briefly, tumor masses were harvested and single cell suspension were obtained after mechanical and enzymatic dispersion. Single suspensions were stained with a mixture of antibodies to discriminate immune cells and tumor cells. Cells were labelled with a fluorescent vital dye to exclude dead cells from the analysis. CD8⁺ T cells specific to MHC-I-restricted GARDASIL-derived HPV16 L1 epitope (AGVDNRECI; SEQ ID NO: 1776) and the tumor-associated MHC-I-restricted HPV16 E7 peptide (RAHYNIVTF; SEQ ID NO: 3863) were detected using fluorescently labeled MHC-I Dextramer and a mixture of antibodies to detect CD8⁺ T cells. FIG.19B shows that intratumoral treatment with SHINGRIX in combination with the MHC-I-restricted HPV16 L1 minimal peptide epitope, or a combination of poly(I:C) with VZV gE and the HPV16 L1 minimal peptide led to significantly increased tumor infiltration by total CD8⁺ T cells, HPV16 L1-specific CD8⁺ T cells and a more modest increase in infiltration by HPV16 E7 tumor-specific CD8⁺ T cells. SHINGRIX treatment alone led to the increased infiltration by HPV16 E7 tumor-specific CD8⁺ T cells only, but not total CD8⁺ T cells or HPV16 L1-specific CD8⁺ T cells. Data are shown as individual percentage of dextramer+ within CD8+ T cells as indicated on the Y-axis and mean ± SEM (n = 5). Statistical significance was assessed by one-way ANOVA for multiple comparison analysis relative to saline control group. *P < 0.05, **P < 0.01, ***P < 0.001. 93155272.1 32 060734-783069 Example 4 Rabies Virus Antigens Have Anti-Tumor Potential in Subjects Previously Vaccinated Against Rabies [0119] This example demonstrates that intratumoral injection of an overlapping peptide library derived from a Rabies virus envelope glycoprotein in two mouse strains harboring different tumor types and vaccinated against rabies amplifies both CD8⁺ and CD4⁺ T cells against the Rabies envelope glycoprotein. This discovery shows that (1) a peptide library can be utilized without prior knowledge of the immunogenic epitope contained within a given antigen; (2) the formulation remains active in different tumor types; and (3) the formulation is effective to recall both CD8⁺ and CD4⁺ T cell responses. [0120] FIG.20A describes the design of an experiment in a single tumor challenge model in which BALB/c mice were immunized with the commercial veterinary rabies vaccines NOBIVAC and VANGUARD (50 μL per vaccine, 1/25th of a veterinary dose) three times one week apart. Five days after the third immunization, mice were transplanted subcutaneously with 5x10^5 TC-1 tumor cells expressing the HPV16 E6 and E7 oncoproteins in the vaccinated C57BL/6 mice. When tumors reached a volume of 50 to 100 mm³, mice were randomized and each tumor was injected intratumorally three times with either saline or a combination of poly(I:C) (50 μg) with the overlapping peptide library from rabies glycoprotein composed of 129 15-mers with an 11 amino acid overlap (0.5 μg each peptide). Ten days after the last intramural injection, T cell responses specific of the rabies envelope glycoprotein were analyzed after in vitro restimulation of splenocyte with the overlapping envelope glycoprotein peptide library. Cytokine production was measured after intracellular staining by flow cytometry. FIG.20B shows the amplification of CD4⁺ and CD8⁺ T cell responses measured by intracellular cytokine staining to detect IFN-gamma and TNF-alpha production by T cells. FIG.20B shows that the injection of tumors with an overlapping peptide library comprising 129 individual peptides and poly(I:C) boosts the CD4 and CD8 T cell responses against the Rabies vaccine envelope glycoprotein antigen. [0121] FIG.20C describes the design of an experiment in a single tumor challenge model in which C57BL/6 mice were immunized with the commercial veterinary rabies vaccines NOBIVAC and VANGUARD (50 μL per vaccine, 1/25th of a veterinary dose) three times one week apart. Five days after the third immunization, mice were transplanted subcutaneously with 93155272.1 33 060734-783069 1x10^6 breast cancer cells 4T1 in the vaccinated BALB/c mice. When tumors reached a volume of 50 to 100 mm³, mice were randomized and each tumor was injected intratumorally three times with either saline or a combination of poly(I:C) (50 μg) with the overlapping peptide library from Rabies envelope glycoprotein composed of 12915-mers with an 11 amino acid overlap (0.5 μg each peptide). Ten days after the last intramural injection T cell responses specific of the rabies envelope glycoprotein were analyzed after in vitro restimulation of splenocyte with the overlapping envelope glycoprotein peptide library. Cytokine production was measured after intracellular staining by flow cytometry. FIG.20D shows the amplification of CD4⁺ and CD8⁺ T cell responses measured by intracellular cytokine staining to detect IFN-gamma and TNF-alpha production by T cells. FIG.20D shows that the injection of tumors with an overlapping peptide library comprising 129 individual peptides and poly(I:C) boosts the CD4 and CD8 T cell responses against the rabies vaccine envelope glycoprotein antigen. 93155272.1 34

Claims

060734-783069 CLAIMS What is claimed is: 1. A method of treating a cancer in a subject in need thereof, comprising administering to the subject a composition comprising one or more varicella-zoster virus (VZV) antigens from a VZV glycoprotein E (gE) protein, wherein the subject has been previously immunized against VZV, and wherein the composition is administered at the site of the cancer. 2. The method of claim 1, wherein the cancer is a solid tumor. 3. The method of claim 2, wherein the composition is administered via intratumoral or peritumoral injection. 4. The method of claim 1, wherein the VZV antigens comprise a truncated VZV gE protein. 5. The method of claim 4, wherein the truncated VZV gE protein comprises the amino acid sequence set forth in SEQ ID NO: 2. 6. The method of claim 1, wherein the VZV antigens comprise one or more MHC-I- or MHC-II-restricted peptides from VZV gE. 7. The method of claim 6, wherein the amino acid sequence of the VZV gE is set forth in SEQ ID NO: 1. 8. The method of claim 7, wherein the VZV antigens comprise one or more MHC- II-restricted VZV gE peptides, and wherein each VZV gE peptide independently comprises the amino acid sequence set forth in one of SEQ ID NOs: 3-156. 93155272.1 35 060734-783069 9. The method of claim 1, wherein the composition comprises or is administered in combination with an adjuvant. 10. The method of claim 9, wherein the adjuvant comprises one or more of poly(I:C), poly-ICLC, a 3-O-desacyl-4’-monophosphoryl lipid A (MPL), QS-21, aluminum hydroxide, and aluminum hydroxyphosphate. 11. The method of claim 10, wherein the adjuvant comprises MPL and QS-21. 12. The method of claim 11, wherein the adjuvant is AS01B. 13. The method of claim 12, wherein the VZV antigen comprises the truncated VZV gE polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 2. 14. The method of claim 13, wherein the VZV antigen and the adjuvant are contained in SHINGRIX. 15. The method of claim 10, wherein the adjuvant comprises poly(I:C), wherein the VZV antigens comprise one or more VZV gE peptides, and wherein each VZV gE peptide independently comprises the amino acid sequence set forth in one of SEQ ID NOs: 3-156. 16. The method of claim 1, wherein the composition is administered 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, or 12 times, wherein each administration is performed every 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, or 12 weeks. 17. The method of claim 16, wherein the cancer is a solid tumor, wherein the composition is administered as one or more series of injections each consisting of 6 injections, and wherein the series of injections is repeated until the solid tumor shrinks or disappears. 93155272.1 36 060734-783069 18. A method of treating a cancer in a subject in need thereof, comprising administering to the subject a composition comprising one or more human papillomavirus (HPV) antigens from an HPV L1 polypeptide, wherein the subject has been previously immunized against HPV, and wherein the composition is administered at the site of the cancer. 19. The method of claim 18, wherein the cancer is a tumor. 20. The method of claim 19, wherein the composition is administered via intratumoral or peritumoral injection. 21. The method of claim 18, wherein the HPV is type 16 (HPV16) or 18 (HPV18). 22. The method of claim 21, wherein the HPV antigens comprise one or more MHC- I- or MHC-II-restricted peptides of the HPV L1 polypeptide. 23. The method of claim 22, wherein the HPV antigens comprise one or more MHC- II-restricted HPV L1 peptides, and wherein each HPV L1 peptide independently comprises an HPV16 peptide comprising the amino acid sequence set forth in one of SEQ ID NOs: 1390-1513 or an HPV18 peptide comprising the amino acid sequence set forth in one of SEQ ID NOs: 1514-1637. 24. The method of claim 22, wherein the HPV antigens comprise one or more MHC- I-restricted HPV L1 peptides, and wherein each HPV L1 peptide independently comprises a HPV16 peptide comprising the amino acid sequence set forth in one of SEQ ID NOs: 1638-2632 or 3632-3645 or a HPV18 peptide comprising the amino acid sequence set forth in one of SEQ ID NOs: 2633-3631 or 3646-3651. 93155272.1 37 060734-783069 25. The method of claim 24, wherein the HPV antigens comprise the MHC-I- restricted HPV16 L1 peptide comprising the amino acid sequence set forth in SEQ ID NO: 1776. 26. The method of claim 18-24, wherein the composition comprises or is administered in combination with an adjuvant. 27. The method of claim 26, wherein the adjuvant comprises one or more of poly(I:C), poly-ICLC, a 3-O-desacyl-4’-monophosphoryl lipid A (MPL), QS-21, aluminum hydroxide, and aluminum hydroxyphosphate. 28. The method of claim 27, wherein the adjuvant comprises poly(I:C). 29. The method of claim 27, wherein the adjuvant comprises MPL. 30. The method of claim 29, wherein the adjuvant further comprises QS21. 31. The method of claim 30, wherein the composition comprises the truncated VZV gE protein comprising the amino acid sequence set forth in SEQ ID NO: 2. 32. The method of claim 31, wherein the composition is SHINGRIX. 33. The method of claim 29, wherein the adjuvant further comprises aluminum hydroxyphosphate. 34. The method of claim 33, wherein the adjuvant is AS04. 35. The method of claim 18, wherein the composition is administered 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, or 12 times, wherein each administration is performed every 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, or 12 weeks. 93155272.1 38 060734-783069 36. The method of claim any one of claims 1-35, wherein the cancer is a solid tumor, and wherein the dose of the one or more antigens is determined relative to tumor volume. 37. The method of claim 36, wherein the dose is at least 1 μg/cm³. 38. The method of claim any one of claims 1-37, wherein the one or more antigens are administered in two or more escalating doses. 39. The method of claim 38, wherein the dose of the one or more antigens is determined individually for the subject. 40. The method of claim 38 or 39, wherein the starting dose of the one or more antigens is determined by an immune assay on autologous peripheral blood mononuclear cells. 41. The method of claim 38 or 39, wherein the starting dose of the one or more antigens is determined by a delayed-type hypersensitivity skin test. 42. The method of claim of claim 38, wherein each subsequent dose after an immediately preceding dose is escalated until an objective is achieved in the subject, wherein the objective is selected from the group consisting of: an objective clinical response in the subject, shrinkage of the cancer, and a substantial toxicity in the subject. 43. The method of claim 42, wherein after the objective is achieved, a subsequent dose of the antigens or peptides is maintained or decreased relative to a preceding dose; or no additional composition is administered to the subject. 44. A method of treating a cancer in a subject in need thereof, comprising administering to the subject a composition comprising one or more tumor-associated antigens 93155272.1 39 060734-783069 and one or more varicella-zoster virus (VZV) antigens from a VZV glycoprotein E (gE) protein, wherein the subject has been previously immunized against VZV, and wherein the composition is administered at the site of the cancer. 45. The method of claim 44, wherein the composition further comprises one or more human papillomavirus (HPV) antigens from an HPV L1 polypeptide, and wherein the subject has further been previously vaccinated against HPV. 46. The method of claim 44, wherein the cancer is a tumor. 47. The method of claim 44, wherein the composition is administered via intratumoral or peritumoral injection. 48. The method of claim 45, wherein the HPV is type 16 (HPV16) or 18 (HPV18). 49. The method of claim 48, wherein the HPV antigens comprise one or more MHC- I- or MHC-II-restricted peptides of the HPV L1 polypeptide. 50. The method of claim 49, wherein the HPV antigens comprise one or more MHC- II-restricted HPV L1 peptides, and wherein each HPV L1 peptide independently comprises an HPV16 peptide comprising the amino acid sequence set forth in one of SEQ ID NOs: 1390-1513 or an HPV18 peptide comprising the amino acid sequence set forth in one of SEQ ID NOs: 1514-1637. 51. The method of claim 49, wherein the HPV antigens comprise one or more MHC- I-restricted HPV L1 peptides, and wherein each HPV L1 peptide independently comprises a HPV16 peptide comprising the amino acid sequence set forth in one of SEQ ID NOs: 1638-2632 93155272.1 40 060734-783069 or 3632-3645 or a HPV18 peptide comprising the amino acid sequence set forth in one of SEQ ID NOs: 2633-3631 or 3646-3651. 52. The method of claim 51, wherein the HPV antigens comprise the MHC-I- restricted HPV16 L1 peptide comprising the amino acid sequence set forth in SEQ ID NO: 1776. 53. The method of claim 44, wherein the VZV antigens comprise a truncated VZV gE protein. 54. The method of claim 53, wherein the truncated VZV gE protein comprises the amino acid sequence set forth in SEQ ID NO: 2. 55. The method of claim 44, wherein the VZV antigens comprise one or more MHC- I- or MHC-II-restricted peptides from VZV gE. 56. The method of claim 55, wherein the amino acid sequence of the VZV gE is set forth in SEQ ID NO: 1. 57. The method of claim 56, wherein the VZV antigens comprise one or more MHC- II-restricted VZV gE peptides, and wherein each VZV gE peptide independently comprises the amino acid sequence set forth in one of SEQ ID NOs: 3-156. 58. The method of claim 48, wherein the subject is human leukocyte antigen (HLA)- A0201 (HLA-A0201)-positive; wherein the cancer comprises a tumor that does not express E6 or E7 oncoproteins from HPV16 and HPV18; and wherein the composition comprises a truncated VZV gE protein, an HPV16 L1 peptide comprising the sequence set forth in SEQ ID NO: 1960, and an HPV18 L1 peptide comprising the sequence set forth in SEQ ID NO: 3649. 93155272.1 41 060734-783069 59. The method of claim 44, wherein the tumor expresses at least one of the tumor- associated antigens. 60. The method of claim 59, wherein the subject is human leukocyte antigen (HLA)- A0201 (HLA-A0201)-positive; wherein the cancer comprises a tumor that expresses one or more of E6 and E7 oncoproteins from one of HPV16 and HPV18; and wherein the composition comprises: a truncated VZV gE protein; an HPV16 L1 peptide comprising the sequence set forth in SEQ ID NO: 1960; an HPV18 L1 peptide comprising the sequence set forth in SEQ ID NO: 3649; HPV16 E7 peptides comprising the sequences set forth in SEQ ID NOs: 5235, 3896, and 5236, wherein each HPV16 E7 peptide comprises one of the sequences; and HPV18 E6 peptides comprising the sequences set forth in SEQ ID NOs: 3930, 3945, and 5237, wherein each HPV18 E6 peptide comprises one of the sequences. 61. The method of claim 44, wherein each tumor-associated antigen is independently from a tumor-associated protein selected from the group consisting of HPV16 E6 oncoprotein, HPV16 E7 oncoprotein, HPV18 E6 oncoprotein, HPV18 E7 oncoprotein, HPV31 E6 oncoprotein, HPV31 E7 oncoprotein, HPV45 E6 oncoprotein, HPV45 E7 oncoprotein, HPV52 E6 oncoprotein, HPV52 E7 oncoprotein, HPV58 E6 oncoprotein, and HPV58 E7 oncoprotein. 62. The method of claim 61, wherein each tumor-associated protein comprises the sequence set forth in any one of SEQ ID NOs: 3652-3663, respectively. 63. The method of claim 61, wherein each tumor-associated antigen is an MHC-I- restricted peptide. 93155272.1 42 060734-783069 64. The method of claim 63, wherein each tumor-associated MHC-I-restricted peptide comprises the amino acid sequence set forth in one of SEQ ID NOs: 3664-5103. 65. The method of claim 61, wherein the tumor-associated protein is HPV16 E7 oncoprotein. 66. The method of claim 65, wherein the tumor-associated antigens comprise an MHC-I-restricted peptide comprising the amino acid sequence RAHYNIVTF (SEQ ID NO: 3863) or QAEPDRAHYNIVTFCCKCD (SEQ ID NO: 5104). 67. The method of claim 66, wherein the HPV antigens comprise the MHC-I- restricted HPV16 L1 peptide comprising the amino acid sequence set forth in SEQ ID NO: 1776 and the VZV antigens comprise the truncated VZV gE comprising the amino acid sequence set forth in SEQ ID NO: 2. 68. The method of any one of claims 44-67, wherein the composition comprises or is administered in combination with an adjuvant. 69. The method of claim 68, wherein the adjuvant comprises one or more of poly(I:C), poly-ICLC, a 3-O-desacyl-4’-monophosphoryl lipid A (MPL), QS-21, aluminum hydroxide, and aluminum hydroxyphosphate. 70. The method of claim 69, wherein the adjuvant comprises poly(I:C). 71. The method of claim 69, wherein the adjuvant comprises MPL. 72. The method of claim 71, wherein the adjuvant further comprises QS21. 73. The method of claim 69, wherein the adjuvant comprises AS01B. 93155272.1 43 060734-783069 74. The method of claim 73, wherein the composition comprises the truncated VZV gE protein comprising the amino acid sequence set forth in SEQ ID NO: 2. 75. The method of claim 74, wherein the composition is SHINGRIX. 76. The method of claim 75, wherein the adjuvant further comprises aluminum hydroxyphosphate. 77. The method of claim 76, wherein the adjuvant is AS04. 78. The method of claim any one of claims 44-77, wherein the composition is administered 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, or 12 times, wherein each administration is performed every 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, or 12 weeks. 79. The method of claim any one of claims 44-78, wherein the cancer is a solid tumor, and wherein the dose of the one or more antigens is determined relative to tumor volume. 80. The method of claim 79, wherein the dose is at least 1 μg/cm³. 81. The method of claim any one of claims 44-80, wherein the one or more antigens are administered in two or more escalating doses. 82. The method of claim 81, wherein the dose of the one or more antigens is determined individually for the subject. 83. The method of claim 81 or 82, wherein the starting dose of the one or more antigens is determined by an immune assay on autologous peripheral blood mononuclear cells. 93155272.1 44 060734-783069 84. The method of claim 81 or 82, wherein the starting dose of the one or more antigens is determined by a delayed-type hypersensitivity skin test. 85. The method of claim of claim 81, wherein each subsequent dose after an immediately preceding dose is escalated until an objective is achieved in the subject, wherein the objective is selected from the group consisting of: an objective clinical response in the subject, shrinkage of the cancer, and a substantial toxicity in the subject. 86. The method of claim 85, wherein after the objective is achieved, a subsequent dose of the antigens or peptides is maintained or decreased relative to a preceding dose; or no additional composition is administered to the subject. 87. A method of treating a cancer in a dog in need thereof, comprising one or more peptides each independently comprising the sequence set forth in one of SEQ ID NOs: 5106- 5234; wherein the dog has been previously immunized against a Rabies virus with a Rabies vaccine; and wherein the composition is administered at the site of the cancer. 88. The method of claim 87, wherein the composition comprises peptides comprising the sequences set forth in SEQ ID NOs: 5106-5234, wherein each peptide comprises one of the sequences. 89. The method of claim 87, wherein the composition comprises is or administered in combination with an adjuvant. 90. The method of claim 89, wherein the adjuvant comprises a Toll-like Receptor 3 (TLR3) agonist. 93155272.1 45 060734-783069 91. The method of claim 90, wherein the TLR3 agonist comprises poly(I:C). 92. The method of claim 87, wherein the cancer is a solid tumor. 93. The method of claim 87, wherein the Rabies vaccine comprises one or more of NOBIVAC®, VANGUARD®, and IMRAB®. 93155272.1 46