WO2003057897A3 - Recombinant protein expression - Google Patents

Recombinant protein expression Download PDF

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Publication number
WO2003057897A3
WO2003057897A3 PCT/IB2003/000299 IB0300299W WO03057897A3 WO 2003057897 A3 WO2003057897 A3 WO 2003057897A3 IB 0300299 W IB0300299 W IB 0300299W WO 03057897 A3 WO03057897 A3 WO 03057897A3
Authority
WO
WIPO (PCT)
Prior art keywords
recombinant protein
interest
protein
methods
expression
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/IB2003/000299
Other languages
French (fr)
Other versions
WO2003057897A2 (en
Inventor
Marco Ario De
Arie Geerlof
Bernd Bukau
Elke Deuerling
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.)
Europaisches Laboratorium fuer Molekularbiologie EMBL
Original Assignee
Europaisches Laboratorium fuer Molekularbiologie EMBL
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
Priority claimed from GBGB0200250.9A external-priority patent/GB0200250D0/en
Priority claimed from GBGB0209013.2A external-priority patent/GB0209013D0/en
Application filed by Europaisches Laboratorium fuer Molekularbiologie EMBL filed Critical Europaisches Laboratorium fuer Molekularbiologie EMBL
Priority to CA002471178A priority Critical patent/CA2471178A1/en
Priority to EP03700428A priority patent/EP1468105A2/en
Priority to AU2003201727A priority patent/AU2003201727A1/en
Priority to US10/500,883 priority patent/US20050064545A1/en
Publication of WO2003057897A2 publication Critical patent/WO2003057897A2/en
Publication of WO2003057897A3 publication Critical patent/WO2003057897A3/en
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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Classifications

    • 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
    • C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • C12N15/67—General methods for enhancing the expression
    • 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
    • C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • 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

Landscapes

  • Life Sciences & Earth Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Engineering & Computer Science (AREA)
  • Organic Chemistry (AREA)
  • Chemical & Material Sciences (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Biotechnology (AREA)
  • General Engineering & Computer Science (AREA)
  • Biomedical Technology (AREA)
  • Microbiology (AREA)
  • Molecular Biology (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Plant Pathology (AREA)
  • Biophysics (AREA)
  • Physics & Mathematics (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)

Abstract

There are provided methods for the expression of a recombinant protein of interest, said methods comprising, in additional to various additional steps: a) culturing a host cell which expresses: i) one or more genes encoding the recombinant protein(s) of interest; ii) at least two genes encoding proteins selected from the group consisting of the chaperone proteins GroEL, GRoES, Dnak, DnaJ, GRpe, ClpB and their homologs (for example, Hsp104, Ydj1 and Ssal in yeast); under conditions suitable for protein expression; and separating said recombinant protein of interest from the host cell culture. Also provided are methods for increasing the degree of refolding of a recombinant protein of interest by ading a composition containing a chaperone protein to a preparation of the recombinant protein of interest in vitro.
PCT/IB2003/000299 2002-01-07 2003-01-07 Recombinant protein expression Ceased WO2003057897A2 (en)

Priority Applications (4)

Application Number Priority Date Filing Date Title
CA002471178A CA2471178A1 (en) 2002-01-07 2003-01-07 Recombinant protein expression
EP03700428A EP1468105A2 (en) 2002-01-07 2003-01-07 Recombinant protein expression
AU2003201727A AU2003201727A1 (en) 2002-01-07 2003-01-07 Recombinant protein expression
US10/500,883 US20050064545A1 (en) 2002-01-07 2003-01-07 Recombinant protein expression

Applications Claiming Priority (4)

Application Number Priority Date Filing Date Title
GB0200250.9 2002-01-07
GBGB0200250.9A GB0200250D0 (en) 2002-01-07 2002-01-07 Recombinant protein expression
GBGB0209013.2A GB0209013D0 (en) 2002-04-19 2002-04-19 Recombinant protein expression
GB0209013.2 2002-04-19

Publications (2)

Publication Number Publication Date
WO2003057897A2 WO2003057897A2 (en) 2003-07-17
WO2003057897A3 true WO2003057897A3 (en) 2003-11-27

Family

ID=26246917

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/IB2003/000299 Ceased WO2003057897A2 (en) 2002-01-07 2003-01-07 Recombinant protein expression

Country Status (5)

Country Link
US (1) US20050064545A1 (en)
EP (1) EP1468105A2 (en)
AU (1) AU2003201727A1 (en)
CA (1) CA2471178A1 (en)
WO (1) WO2003057897A2 (en)

Families Citing this family (20)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
KR100516389B1 (en) * 2003-09-08 2005-09-23 한국과학기술원 Composition for Protecting Proteins Degradation Comprising Small Heat Shock Proteins(sHSPs) and Method of Two-Dimensional Gel Electrophoresis Using the sHSPs
GB0329681D0 (en) * 2003-12-23 2004-01-28 Delta Biotechnology Ltd Gene expression technique
DK2330200T3 (en) * 2004-12-23 2017-07-24 Albumedix As GENE EXPRESSION TECHNIQUE
GB0512707D0 (en) * 2005-06-22 2005-07-27 Delta Biotechnology Ltd Gene expression technique
US20080268488A1 (en) * 2005-11-10 2008-10-30 Sturgess Michael A Screening Method for Dnak Inhibitors
US8722348B2 (en) 2008-05-28 2014-05-13 Wayne State University Method and composition for a protein transduction technology and its applications
DE102008035152A1 (en) * 2008-07-28 2010-02-04 Evocatal Gmbh Chaperone toolbox
EP2258854A1 (en) 2009-05-20 2010-12-08 FH Campus Wien Eukaryotic host cell comprising an expression enhancer
KR20130094313A (en) * 2010-08-24 2013-08-23 노스-웨스트 유니버시티 Recombinant therapeutic glycine n-acyltransferase
CN102533835A (en) * 2010-08-31 2012-07-04 上海交通大学 Plasmid for heterologous protein solubility expression and preparation and application method thereof
GB201101794D0 (en) 2011-02-02 2011-03-16 Fermentas Uab Protein production
PT2705143T (en) 2011-05-02 2021-04-07 Univ Wayne State A protein-induced pluripotent cell technology uses thereof
CN102925475B (en) * 2012-11-22 2014-07-09 江南大学 Novel method for realizing secreting expression of exogenous protein by using novel transfer signal
US10076574B2 (en) 2013-10-25 2018-09-18 Wayne State University Methods, systems and compositions relating to cell conversion via protein-induced in-vivo cell reprogramming
WO2017215790A1 (en) * 2016-06-17 2017-12-21 National Hellenic Research Foundation Systems for recombinant protein production
KR102185312B1 (en) * 2017-10-25 2020-12-02 재단법인 지능형 바이오 시스템 설계 및 합성 연구단 A composition for solubilization of target proteins and use thereof
US10829731B2 (en) 2018-01-25 2020-11-10 Alliance For Sustainable Energy, Llc Biocatalysts for conversion of thermochemical waste streams
CN111936629B (en) * 2018-03-29 2025-03-28 弗门尼舍有限公司 Method for producing vanillin
CN118652908A (en) * 2024-06-03 2024-09-17 南京工业大学 A co-expression method for combining homologous chaperone elements and improving soluble expression of plastic degrading enzymes
CN118652907A (en) * 2024-06-03 2024-09-17 南京工业大学 Homologous chaperone elements and their application in improving soluble expression of PET plastic degrading enzyme

Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0885967A2 (en) * 1997-06-20 1998-12-23 Hsp Research Institute, Inc. Chaperone expression plasmids
WO2000071723A2 (en) * 1999-05-21 2000-11-30 Roche Diagnostics Gmbh Methods for regulating protein conformation using molecular chaperones

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0885967A2 (en) * 1997-06-20 1998-12-23 Hsp Research Institute, Inc. Chaperone expression plasmids
WO2000071723A2 (en) * 1999-05-21 2000-11-30 Roche Diagnostics Gmbh Methods for regulating protein conformation using molecular chaperones

Non-Patent Citations (6)

* Cited by examiner, † Cited by third party
Title
AMREIN KURT E ET AL: "Purification and characterization of recombinant human p50-csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL.", PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES, vol. 92, no. 4, 1995, 1995, pages 1048 - 1052, XP002241051, ISSN: 0027-8424 *
BEN-ZVI ANAT PERES ET AL: "Review: Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones.", JOURNAL OF STRUCTURAL BIOLOGY, vol. 135, no. 2, August 2001 (2001-08-01), pages 84 - 93, XP002241053, ISSN: 1047-8477 *
CARRIO M M ET AL: "Protein aggregation as bacterial inclusion bodies is reversible", FEBS LETTERS, ELSEVIER SCIENCE PUBLISHERS, AMSTERDAM, NL, vol. 489, no. 1, 26 January 2001 (2001-01-26), pages 29 - 33, XP004239392, ISSN: 0014-5793 *
MOGK A ET AL: "Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB", EMBO JOURNAL, OXFORD UNIVERSITY PRESS, SURREY, GB, vol. 18, no. 24, 15 December 1999 (1999-12-15), pages 6934 - 6949, XP002148774, ISSN: 0261-4189 *
THOMAS JEFFREY G ET AL: "ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells.", MOLECULAR MICROBIOLOGY, vol. 36, no. 6, June 2000 (2000-06-01), pages 1360 - 1370, XP002241052, ISSN: 0950-382X *
VEINGER LEA ET AL: "The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network.", JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 273, no. 18, 1 May 1998 (1998-05-01), pages 11032 - 11037, XP002241887, ISSN: 0021-9258 *

Also Published As

Publication number Publication date
WO2003057897A2 (en) 2003-07-17
US20050064545A1 (en) 2005-03-24
CA2471178A1 (en) 2003-07-17
AU2003201727A1 (en) 2003-07-24
EP1468105A2 (en) 2004-10-20

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