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WO2003040335A3 - Genie de peptides leader pour la secretion de proteines recombinees dans des bacteries - Google Patents

Genie de peptides leader pour la secretion de proteines recombinees dans des bacteries Download PDF

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Publication number
WO2003040335A3
WO2003040335A3 PCT/US2002/035618 US0235618W WO03040335A3 WO 2003040335 A3 WO2003040335 A3 WO 2003040335A3 US 0235618 W US0235618 W US 0235618W WO 03040335 A3 WO03040335 A3 WO 03040335A3
Authority
WO
WIPO (PCT)
Prior art keywords
leader peptides
export
proteins
folded
cytoplasm
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/US2002/035618
Other languages
English (en)
Other versions
WO2003040335A2 (fr
Inventor
George Georgiou
Matthew Delisa
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Research Development Foundation
Original Assignee
Research Development Foundation
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Research Development Foundation filed Critical Research Development Foundation
Priority to CA002465724A priority Critical patent/CA2465724A1/fr
Priority to JP2003542582A priority patent/JP2005522188A/ja
Priority to AU2002360348A priority patent/AU2002360348B8/en
Priority to EP02795597A priority patent/EP1451367A4/fr
Publication of WO2003040335A2 publication Critical patent/WO2003040335A2/fr
Publication of WO2003040335A3 publication Critical patent/WO2003040335A3/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00—Preparation of peptides or proteins
    • C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
    • C07K14/43595—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from coelenteratae, e.g. medusae
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
    • C12N15/1034—Isolating an individual clone by screening libraries
    • C12N15/1051—Gene trapping, e.g. exon-, intron-, IRES-, signal sequence-trap cloning, trap vectors
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
    • C12N15/62—DNA sequences coding for fusion proteins
    • C12N15/625—DNA sequences coding for fusion proteins containing a sequence coding for a signal sequence
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
    • C07K2319/034—Fusion polypeptide containing a localisation/targetting motif containing a motif for targeting to the periplasmic space of Gram negative bacteria as a soluble protein, i.e. signal sequence should be cleaved
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/60—Fusion polypeptide containing spectroscopic/fluorescent detection, e.g. green fluorescent protein [GFP]
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/61—Fusion polypeptide containing an enzyme fusion for detection (lacZ, luciferase)
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/95—Fusion polypeptide containing a motif/fusion for degradation (ubiquitin fusions, PEST sequence)

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Molecular Biology (AREA)
  • Biomedical Technology (AREA)
  • Biotechnology (AREA)
  • General Engineering & Computer Science (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • General Health & Medical Sciences (AREA)
  • Biochemistry (AREA)
  • Biophysics (AREA)
  • Microbiology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Plant Pathology (AREA)
  • Physics & Mathematics (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Crystallography & Structural Chemistry (AREA)
  • Bioinformatics & Computational Biology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Tropical Medicine & Parasitology (AREA)
  • Toxicology (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Medicinal Chemistry (AREA)
  • Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Peptides Or Proteins (AREA)

Abstract

L'invention concerne des procédés d'isolement de peptides leader pouvant diriger l'exportation de protéines hétérologues à partir du cytoplasme bactérien. Lesdits procédés se fondent sur le criblage de bibliothèques de peptides leader putatifs ou de mutants de peptides leader pour des séquences qui permettent une exportation rapide et peuvent ainsi empêcher la dégradation d'une protéine reporter à durée de vie courte dans le cytoplasme. Lesdits peptides leader mutants identifiés dans la présente invention peuvent conférer de manière significative des niveaux d'états stables d'exportation plus élevés non seulement pour une protéine reporter à durée de vie courte mais aussi pour d'autres protéines stables à durée de vie longue. Lesdits peptides leader peuvent être utilisés pour diriger ou augmenter la sécrétion des protéines. L'invention concerne de plus des procédés d'exportation de protéines pliées de manière cytoplasmique par l'intermédiaire d'une voie Tat. Des protéines présentant des liaisons disulfure sont pliées en premier à l'intérieur du cytoplasme dans des souches mutantes appropriées oxydantes. Lesdites protéines pré-pliées de manière cytoplasmique qui contiennent des liaisons disulfure sont alors exportées par l'intermédiaire de la voie Tat.
PCT/US2002/035618 2001-11-05 2002-11-05 Genie de peptides leader pour la secretion de proteines recombinees dans des bacteries Ceased WO2003040335A2 (fr)

Priority Applications (4)

Application Number Priority Date Filing Date Title
CA002465724A CA2465724A1 (fr) 2001-11-05 2002-11-05 Genie de peptides leader pour la secretion de proteines recombinees dans des bacteries
JP2003542582A JP2005522188A (ja) 2001-11-05 2002-11-05 バクテリア内での遺伝子組み換え体蛋白質の分泌を促進するためのリーダー・ペプチド及びその単離方法
AU2002360348A AU2002360348B8 (en) 2001-11-05 2002-11-05 Engineering of leader peptides for the secretion of recombinant proteins in bacteria
EP02795597A EP1451367A4 (fr) 2001-11-05 2002-11-05 Genie de peptides leader pour la secretion de proteines recombinees dans des bacteries

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
US33745201P 2001-11-05 2001-11-05
US60/337,452 2001-11-05
US60/ 2002-09-13

Publications (2)

Publication Number Publication Date
WO2003040335A2 WO2003040335A2 (fr) 2003-05-15
WO2003040335A3 true WO2003040335A3 (fr) 2003-12-31

Family

ID=23320598

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/US2002/035618 Ceased WO2003040335A2 (fr) 2001-11-05 2002-11-05 Genie de peptides leader pour la secretion de proteines recombinees dans des bacteries

Country Status (3)

Country Link
EP (1) EP1451367A4 (fr)
CN (1) CN100564540C (fr)
WO (1) WO2003040335A2 (fr)

Families Citing this family (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20130045871A1 (en) * 2010-03-18 2013-02-21 Cornell University Engineering correctly folded antibodies using inner membrane display of twin-arginine translocation intermediates
CN103797122A (zh) * 2011-04-08 2014-05-14 安瑟生物科技私人有限公司 用于大肠杆菌中异源蛋白质生产的新的表达和分泌载体系统
KR101470595B1 (ko) 2012-08-01 2014-12-10 대구가톨릭대학교산학협력단 세포외로 분비되는 녹색형광단백질, 이를 코딩하는 유전자 및 이 유전자 발현을 위한 벡터
CN102851270A (zh) * 2012-08-03 2013-01-02 江南大学 一种杂交链霉菌胰蛋白酶酶原及其应用
GB201713732D0 (en) * 2017-08-25 2017-10-11 Alta Innovations Ltd Tat expression system
CN109575116B (zh) * 2018-11-09 2022-04-22 广东海洋大学 一种线粒体定位导肽及其发现方法与应用
CN110616227A (zh) * 2019-09-30 2019-12-27 天津科技大学 一种来源于黄粉虫的抗冻蛋白的基因、重组表达载体、工程菌株和应用

Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20020110860A1 (en) * 2000-09-18 2002-08-15 Sierd Bron Twin-arginine translocation in Bacillus
US20020182672A1 (en) * 2000-10-10 2002-12-05 Marc Kolkman Enhanced secretion of a polypeptide by a microorganism

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1999045136A1 (fr) * 1998-03-05 1999-09-10 University Of British Columbia Procedes d'analyse d'inhibiteurs de secretion de type iii
EP1068339B1 (fr) * 1998-04-01 2008-07-23 The Governors of the University of Alberta Compositions et methodes de secretion proteique

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20020110860A1 (en) * 2000-09-18 2002-08-15 Sierd Bron Twin-arginine translocation in Bacillus
US20020182672A1 (en) * 2000-10-10 2002-12-05 Marc Kolkman Enhanced secretion of a polypeptide by a microorganism

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
DELISA M.P. ET AL.: "Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway", PROC. NATL. ACAD. SCI. USA, vol. 100, no. 10, 13 May 2003 (2003-05-13), pages 6115 - 6120, XP002970386 *
DELISA M.P.: "Genetic analysis of the twin arginine translocator secretion pathway in bacteria", THE JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 277, no. 33, 16 August 2002 (2002-08-16), pages 29825 - 29831, XP002970385 *
See also references of EP1451367A4 *

Also Published As

Publication number Publication date
CN1788092A (zh) 2006-06-14
EP1451367A4 (fr) 2006-06-14
CN100564540C (zh) 2009-12-02
EP1451367A2 (fr) 2004-09-01
WO2003040335A2 (fr) 2003-05-15

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