WO2007086879A2 - Method of expressing proteins with disulfide bridges - Google Patents

Method of expressing proteins with disulfide bridges Download PDF

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Publication number
WO2007086879A2
WO2007086879A2 PCT/US2006/004413 US2006004413W WO2007086879A2 WO 2007086879 A2 WO2007086879 A2 WO 2007086879A2 US 2006004413 W US2006004413 W US 2006004413W WO 2007086879 A2 WO2007086879 A2 WO 2007086879A2
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WO
WIPO (PCT)
Prior art keywords
disintegrin
protein
domain
sequence
thioredoxin
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/US2006/004413
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English (en)
French (fr)
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WO2007086879A3 (en
Inventor
Radu Minea
Frances Markland
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University of Southern California USC
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University of Southern California USC
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Application filed by University of Southern California USC filed Critical University of Southern California USC
Priority to CA002597647A priority Critical patent/CA2597647A1/en
Priority to EP13157149.9A priority patent/EP2634252B1/en
Priority to AU2006336468A priority patent/AU2006336468B2/en
Priority to JP2007556197A priority patent/JP2008536479A/ja
Priority to EP06849695A priority patent/EP1856255A4/en
Publication of WO2007086879A2 publication Critical patent/WO2007086879A2/en
Anticipated expiration legal-status Critical
Publication of WO2007086879A3 publication Critical patent/WO2007086879A3/en
Ceased legal-status Critical Current

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    • 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
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P35/00—Antineoplastic agents
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P35/00—Antineoplastic agents
    • A61P35/04—Antineoplastic agents specific for metastasis
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P7/00—Drugs for disorders of the blood or the extracellular fluid
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P7/00—Drugs for disorders of the blood or the extracellular fluid
    • A61P7/02—Antithrombotic agents; Anticoagulants; Platelet aggregation inhibitors
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
    • C07K14/24—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
    • C07K14/245—Escherichia (G)
    • 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
    • C12N9/6402—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals
    • C12N9/6418—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals from snakes
    • 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
    • C12N9/90—Isomerases (5.)
    • 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
    • C07K2319/00—Fusion polypeptide
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/20—Fusion polypeptide containing a tag with affinity for a non-protein ligand
    • C07K2319/21—Fusion polypeptide containing a tag with affinity for a non-protein ligand containing a His-tag
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/50—Fusion polypeptide containing protease site
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/90—Fusion polypeptide containing a motif for post-translational modification

Definitions

  • CN also has the ability to directly engage tumor cells and suppress their growth in a cytostatic manner (Trikha, De Clerck et al. 1994; Trikha, Rote et al. 1994; Schmitmeier, Markland et al. 2000).
  • the antitumoral activity of CN is based on its high affinity interaction with integrins ⁇ 5 ⁇ l, ⁇ v ⁇ 3 and ⁇ v ⁇ 5 on both cancer cells and newly growing vascular endothelial cells (Trikha, De Clerck et al.
  • FIG. 18B shows a mutated CN gene sequence after replacing all CGG and most ACA rarely used codons. The ACA codons left unreplaced are highlighted in bold.
  • FIG. 19 is a map of the pCDFDuet- 1 vector (from Novagen) .
  • bacterial host cells may be engineered to cytoplasmically express a disulfide isomerase normally targeted to the periplasmic space of the host.
  • the disulfide isomerase is DsbC.
  • DsbC disulfide isomerase
  • DsbC is specifically activated by the periplasmic N-terminal domain (DsbD ⁇ -domain) of the transmembrane electron transporter DsbD.
  • DsbA and DsbC the formation of protein disulfide bonds is catalyzed by DsbA and DsbC.
  • the oxidation pathway consists of DsbA, a powerful oxidase (the most oxidizing protein known) and its modulator, DsbB, that couples DsbA with the respiratory chain (in aerobic conditions) or with the anaerobic electron acceptors (in anaerobic conditions).
  • HPLC purified rCN and VN were recognized by a polyclonal antisera raised against native CN in both ELISA and Western blotting assays (data not shown).
  • Biological activity of liposome encapsulated CN was evaluated as previously described (Swenson, Costa et al. 2004). Briefly, three groups of five nude mice had MDA-MB-435 human mammary carcinoma cells implanted in the mammary fat pad. Two weeks following implantation, small tumors were palpable and treatment was commenced. Animals were treated with LCN or LVN (105 ⁇ g, twice weekly, i.v. administration); a PBS treated control was included. A significant inhibitory effect on tumor growth by LVN was observed (FIG. 12). The functional activity of VN was indicated by its in vivo cancer therapeutic effect, which was found to be similar to native CN.
  • FIG. 15A shows a big peak of 13507.0, for CN representing the dimer, and two smaller peaks probably CN from which a single amino acid has been cleaved.
  • FIG. 15B shows a single peak of 7146.0, for VN, confirming that it is a monomer.
  • Trxback Trx reverse external primer introducing the BgIII restriction site and designed for inserting the 3' end of the active site mutants into pET32a vector: 5'TACCCAGATCTGGGCTGTCCATGTGCTS' (SEQ ID NO: 24)
  • DsbCGFfor - active site mutated DsbC (CGFC) overlap extension forward primer: 5'TTTACTGATATTACCTGTGGTTTCTGCCACAAACTGCATGAGS' (SEQ ID NO: 36)

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  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Zoology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Wood Science & Technology (AREA)
  • Genetics & Genomics (AREA)
  • Medicinal Chemistry (AREA)
  • Biochemistry (AREA)
  • Molecular Biology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Microbiology (AREA)
  • General Engineering & Computer Science (AREA)
  • Biotechnology (AREA)
  • Animal Behavior & Ethology (AREA)
  • Veterinary Medicine (AREA)
  • Public Health (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Biomedical Technology (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Biophysics (AREA)
  • Marine Sciences & Fisheries (AREA)
  • Diabetes (AREA)
  • Hematology (AREA)
  • Immunology (AREA)
  • Epidemiology (AREA)
  • Oncology (AREA)
  • Peptides Or Proteins (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
PCT/US2006/004413 2005-02-11 2006-02-09 Method of expressing proteins with disulfide bridges Ceased WO2007086879A2 (en)

Priority Applications (5)

Application Number Priority Date Filing Date Title
CA002597647A CA2597647A1 (en) 2005-02-11 2006-02-09 Method of expressing proteins with disulfide bridges
EP13157149.9A EP2634252B1 (en) 2005-02-11 2006-02-09 Method of expressing proteins with disulfide bridges
AU2006336468A AU2006336468B2 (en) 2005-02-11 2006-02-09 Method of expressing proteins with disulfide bridges
JP2007556197A JP2008536479A (ja) 2005-02-11 2006-02-09 ジスルフィド架橋を有するタンパク質の発現法
EP06849695A EP1856255A4 (en) 2005-02-11 2006-02-09 PROCESS FOR EXPRESSING PROTEINS VIA DISULPHIDE BRIDGES

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US65252905P 2005-02-11 2005-02-11
US60/652,529 2005-02-11

Publications (2)

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WO2007086879A2 true WO2007086879A2 (en) 2007-08-02
WO2007086879A3 WO2007086879A3 (en) 2009-06-11

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PCT/US2006/004413 Ceased WO2007086879A2 (en) 2005-02-11 2006-02-09 Method of expressing proteins with disulfide bridges

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US (4) US7754850B2 (https=)
EP (2) EP2634252B1 (https=)
JP (1) JP2008536479A (https=)
CN (1) CN101535492A (https=)
AU (1) AU2006336468B2 (https=)
CA (1) CA2597647A1 (https=)
WO (1) WO2007086879A2 (https=)

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CN108864291A (zh) * 2011-11-23 2018-11-23 拜奥文斯瑞有限公司 重组蛋白及其治疗用途
EP3505532A4 (en) * 2016-08-25 2020-04-22 Nexgen Biotechnologies, Inc. SCORPION POISON FUSION PROTEIN WITH IMPROVED EFFECT IN THE PROLIFERATION OF SKIN CELLS AND COSMETIC COMPOSITION, THEREFORE AS AN ACTIVE SUBSTANCE TO REDUCE SKIN WRINKLES, TO IMPROVE THE SKIN ELASTICITY AND TO PREVENT THE AGE

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EP2634252A2 (en) 2013-09-04
EP2634252B1 (en) 2018-12-19
JP2008536479A (ja) 2008-09-11
EP1856255A4 (en) 2010-01-27
US20120301453A1 (en) 2012-11-29
CN101535492A (zh) 2009-09-16
US7754850B2 (en) 2010-07-13
US8685668B2 (en) 2014-04-01
US8110542B2 (en) 2012-02-07
EP1856255A2 (en) 2007-11-21
AU2006336468A2 (en) 2010-04-29
US20130345399A1 (en) 2013-12-26
AU2006336468B2 (en) 2012-04-12
WO2007086879A3 (en) 2009-06-11
US20110097388A1 (en) 2011-04-28
US8338365B2 (en) 2012-12-25
US20060246541A1 (en) 2006-11-02
CA2597647A1 (en) 2007-08-02
EP2634252A3 (en) 2013-11-13
AU2006336468A1 (en) 2007-08-02

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