CA2313248C - Process for the production of naturally folded and secreted proteins by co-secretion of molecular chaperones - Google Patents

Process for the production of naturally folded and secreted proteins by co-secretion of molecular chaperones Download PDF

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Publication number
CA2313248C
CA2313248C CA2313248A CA2313248A CA2313248C CA 2313248 C CA2313248 C CA 2313248C CA 2313248 A CA2313248 A CA 2313248A CA 2313248 A CA2313248 A CA 2313248A CA 2313248 C CA2313248 C CA 2313248C
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CA
Canada
Prior art keywords
gly
ala
ser
leu
glu
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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.)
Expired - Lifetime
Application number
CA2313248A
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English (en)
French (fr)
Other versions
CA2313248A1 (en
Inventor
Dorothee Ambrosius
Rainer Rudolph
Jorg Schaffner
Elisabeth Schwarz
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F Hoffmann La Roche AG
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F Hoffmann La Roche AG
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Publication date
Application filed by F Hoffmann La Roche AG filed Critical F Hoffmann La Roche AG
Publication of CA2313248A1 publication Critical patent/CA2313248A1/en
Application granted granted Critical
Publication of CA2313248C publication Critical patent/CA2313248C/en
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Expired - Lifetime 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
    • 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
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424—Serine endopeptidases (3.4.21)
    • C12N9/6456—Plasminogen activators
    • C12N9/6459—Plasminogen activators t-plasminogen activator (3.4.21.68), i.e. tPA
    • 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
    • C12N1/00—Microorganisms; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
    • C12N1/20—Bacteria; Culture media therefor
    • 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
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/21—Serine endopeptidases (3.4.21)
    • C12Y304/21069—Protein C activated (3.4.21.69)
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
    • C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence

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  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Genetics & Genomics (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • General Engineering & Computer Science (AREA)
  • Biotechnology (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Biomedical Technology (AREA)
  • Microbiology (AREA)
  • Molecular Biology (AREA)
  • Medicinal Chemistry (AREA)
  • Virology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Tropical Medicine & Parasitology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Physics & Mathematics (AREA)
  • Biophysics (AREA)
  • Plant Pathology (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Peptides Or Proteins (AREA)
  • Enzymes And Modification Thereof (AREA)
CA2313248A 1999-07-29 2000-07-26 Process for the production of naturally folded and secreted proteins by co-secretion of molecular chaperones Expired - Lifetime CA2313248C (en)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
EP99114811A EP1077263A1 (de) 1999-07-29 1999-07-29 Verfahren zur Herstellung von natürlich gefalteten und sekretierten Proteinen durch Co-Sekretion von Chaperonen
EP99114811.5 1999-07-29

Publications (2)

Publication Number Publication Date
CA2313248A1 CA2313248A1 (en) 2001-01-29
CA2313248C true CA2313248C (en) 2010-05-25

Family

ID=8238680

Family Applications (1)

Application Number Title Priority Date Filing Date
CA2313248A Expired - Lifetime CA2313248C (en) 1999-07-29 2000-07-26 Process for the production of naturally folded and secreted proteins by co-secretion of molecular chaperones

Country Status (13)

Country Link
US (1) US6455279B1 (https=)
EP (2) EP1077263A1 (https=)
JP (1) JP2001061487A (https=)
KR (1) KR100378325B1 (https=)
CN (1) CN1231595C (https=)
AT (1) ATE299942T1 (https=)
CA (1) CA2313248C (https=)
DE (1) DE60021318T2 (https=)
DK (1) DK1077262T3 (https=)
ES (1) ES2247990T3 (https=)
IN (1) IN190327B (https=)
JO (1) JO2309B1 (https=)
MX (1) MXPA00007339A (https=)

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AU6124201A (en) * 2000-05-03 2001-11-12 Expressive Constructs Inc A method and device for improving protein stability and solubility
US6955910B2 (en) 2000-11-14 2005-10-18 Boehringer Ingelheim International Gmbh Method for large scale production of recombinant DNA-derived TPA or K2S molecules
GB0027779D0 (en) * 2000-11-14 2000-12-27 Boehringer Ingelheim Int Methods for large scale production of recombinant dna-derived tpa or k2s molecules
US7087412B2 (en) 2000-11-14 2006-08-08 Boehringer Ingelheim International Gmbh Methods for large scale protein production in prokaryotes
US6979556B2 (en) * 2000-12-14 2005-12-27 Genentech, Inc. Separate-cistron contructs for secretion of aglycosylated antibodies from prokaryotes
US7094757B2 (en) 2001-06-22 2006-08-22 Roche Diagnostics Corporation Complexes comprising a prion protein and a peptidyl prolyl isomerase chaperone, and method for producing and using them
US6962982B2 (en) 2001-06-22 2005-11-08 Roche Diagnostics Corporation Soluble complexes of target proteins and peptidyl prolyl isomerase chaperones and methods of making and using them
DK1402015T3 (da) * 2001-06-22 2011-12-05 Hoffmann La Roche Opløseligt kompleks omfattende et retroviralt overfladeglycoprotein og FkpA eller SlyD
US7094884B2 (en) 2001-06-22 2006-08-22 Roche Diagnostics Corporation Soluble complexes of amylod β peptide and peptidyl prolyl isomerase chaperone and methods of making and using them
KR100441755B1 (ko) * 2001-07-24 2004-08-02 재단법인서울대학교산학협력재단 분자 샤페론을 핵 내부로 이동시키는 방법
KR100968664B1 (ko) * 2001-08-27 2010-07-06 제넨테크, 인크. 항체 발현 및 조립을 위한 시스템
DE10145694A1 (de) * 2001-09-17 2003-04-03 Roche Diagnostics Gmbh Verfahren zur Erhöhung der Löslichkeit, der Expressionsrate und der Aktivität von Proteinen während der rekombinanten Herstellung
WO2004042017A2 (en) * 2002-10-31 2004-05-21 Genentech, Inc. Methods and compositions for increasing antibody production
CA2513113A1 (en) * 2003-01-23 2004-08-05 Genentech, Inc. Methods for producing humanized antibodies and improving yield of antibodies or antigen binding fragments in cell culture
EP1624886A2 (en) * 2003-05-12 2006-02-15 Expressive Constructs, Inc. Methods for increasing cell and tissue viability
AU2004273791A1 (en) * 2003-09-05 2005-03-31 Genentech, Inc. Antibodies with altered effector functions
GB0329681D0 (en) * 2003-12-23 2004-01-28 Delta Biotechnology Ltd Gene expression technique
EP1789446A2 (en) * 2004-09-02 2007-05-30 Genentech, Inc. Heteromultimeric molecules
DK2330200T3 (en) * 2004-12-23 2017-07-24 Albumedix As GENE EXPRESSION TECHNIQUE
DE112005003589T5 (de) * 2005-05-23 2008-04-17 Korea Advanced Institute Of Science & Technology Verfahren zum Herstellen eines Zielproteins unter Verwendung der sHSPs
GB0512707D0 (en) * 2005-06-22 2005-07-27 Delta Biotechnology Ltd Gene expression technique
WO2008067547A2 (en) 2006-11-30 2008-06-05 Research Development Foundation Improved immunoglobulin libraries
CN101294164B (zh) * 2007-04-23 2013-01-16 南京大学 重组人中期因子(rh-Midkine)的表达及其单克隆抗体的制备和应用
AU2008247819B2 (en) 2007-05-01 2013-02-14 Research Development Foundation Immunoglobulin Fc libraries
CN101307310B (zh) * 2007-05-15 2012-08-08 康泰生医科技股份有限公司 具有提高产率及免疫原性的重组蛋白质表达系统
CA2766065C (en) * 2009-06-30 2020-07-21 Research Development Foundation Immunoglobulin fc polypeptides
AU2012214643B2 (en) 2011-02-07 2016-12-15 Research Development Foundation Engineered immunoglobulin Fc polypeptides
WO2014054744A1 (ja) * 2012-10-03 2014-04-10 協和発酵キリン株式会社 培養液にアミノ酸を添加することによるポリペプチドの還元防止方法
JP6345688B2 (ja) 2012-12-05 2018-06-20 ソラ・バイオサイエンシズ・エルエルシー タンパク質発現増強ポリペプチド
JP6724023B2 (ja) 2015-02-09 2020-07-15 リサーチ ディベロップメント ファウンデーション 改善された補体活性化を示す操作された免疫グロブリンｆｃポリペプチド
CN105296653B (zh) * 2015-11-26 2018-07-06 天津师范大学 采用荧光RT-PCR技术检测周氏啮小蜂Hsp83基因表达的方法
CN105296651B (zh) * 2015-11-26 2018-07-06 天津师范大学 采用荧光RT-PCR技术检测周氏啮小蜂Hsp90基因表达的方法
CN105296652B (zh) * 2015-11-26 2018-07-06 天津师范大学 采用荧光RT-PCR技术检测周氏啮小蜂Hsp40基因表达的方法
CN105296654B (zh) * 2015-11-26 2018-07-06 天津师范大学 采用荧光RT-PCR技术检测周氏啮小蜂Hsp60基因表达的方法
CN110734480B (zh) * 2019-11-07 2021-08-24 中国科学院遗传与发育生物学研究所 大肠杆菌分子伴侣GroEL/ES在协助合成植物Rubisco中的应用
US10973908B1 (en) 2020-05-14 2021-04-13 David Gordon Bermudes Expression of SARS-CoV-2 spike protein receptor binding domain in attenuated salmonella as a vaccine
US12537071B1 (en) 2020-07-22 2026-01-27 David Gordon Bermudes Bacteria having boolean control pathways expressing therapeutic proteins including immunotherapeutic cytotoxins
CN112239760B (zh) * 2020-09-18 2022-02-11 深圳科兴药业有限公司 高效表达重组hGH的重组工程菌及构建方法和应用
CN112940955B (zh) * 2021-04-18 2022-10-18 江南大学 一种高效合成乳铁蛋白的毕赤酵母及其构建方法与应用

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Also Published As

Publication number Publication date
US6455279B1 (en) 2002-09-24
IN190327B (https=) 2003-07-19
DK1077262T3 (da) 2005-11-07
ES2247990T3 (es) 2006-03-16
CA2313248A1 (en) 2001-01-29
DE60021318D1 (de) 2005-08-25
CN1231595C (zh) 2005-12-14
EP1077262B1 (en) 2005-07-20
KR20010049895A (ko) 2001-06-15
DE60021318T2 (de) 2006-05-24
ATE299942T1 (de) 2005-08-15
MXPA00007339A (es) 2002-08-06
EP1077262A1 (en) 2001-02-21
EP1077263A1 (de) 2001-02-21
KR100378325B1 (ko) 2003-03-29
JO2309B1 (en) 2005-09-12
JP2001061487A (ja) 2001-03-13
CN1283702A (zh) 2001-02-14

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Effective date: 20200727