Methods and compositions for increasing antibody production

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...

Reexamination Certificate

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Reexamination Certificate

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07608429

ABSTRACT:
The invention provides methods and compositions for improved expression and production of recombinant antibodies in host cell expression systems. In particular, prokaryotic expression and production of antibodies with modified hinge cysteine residues are provided. The invention further provides compositions, kits and articles of manufacture for practicing methods of the present invention.

REFERENCES:
patent: 4816567 (1989-03-01), Cabilly et al.
patent: 5264365 (1993-11-01), Georgiou et al.
patent: 5264586 (1993-11-01), Nicolaou et al.
patent: 5348876 (1994-09-01), Michaelsen et al.
patent: 5500362 (1996-03-01), Robinson et al.
patent: 5508192 (1996-04-01), Georgiou et al.
patent: 5585097 (1996-12-01), Bolt et al.
patent: 5624821 (1997-04-01), Winter et al.
patent: 5639635 (1997-06-01), Joly et al.
patent: 5648237 (1997-07-01), Carter
patent: 5648260 (1997-07-01), Winter et al.
patent: 5677425 (1997-10-01), Bodmer et al.
patent: 5731168 (1998-03-01), Carter et al.
patent: 5807706 (1998-09-01), Carter et al.
patent: 5821333 (1998-10-01), Carter et al.
patent: 5821337 (1998-10-01), Carter et al.
patent: 5840523 (1998-11-01), Simmons et al.
patent: 5854027 (1998-12-01), Steipe et al.
patent: 5892019 (1999-04-01), Schlom et al.
patent: 6027888 (2000-02-01), Georgiuo et al.
patent: 6083715 (2000-07-01), Georgiuo et al.
patent: 6165745 (2000-12-01), Ward et al.
patent: 6331415 (2001-12-01), Cabilly et al.
patent: 6455279 (2002-09-01), Ambrosius et al.
patent: 6602688 (2003-08-01), Opper et al.
patent: 2003/0118592 (2003-06-01), Ledbetter et al.
patent: 2005/0048572 (2005-03-01), Reilly et al.
patent: 2005/0152894 (2005-07-01), Krummen et al.
patent: WO 89/01974 (1989-03-01), None
patent: WO 92/22583 (1992-12-01), None
patent: WO 94/29531 (1994-12-01), None
patent: WO 95/14779 (1995-06-01), None
patent: WO 99/25378 (1999-05-01), None
patent: WO 99/51642 (1999-10-01), None
patent: WO 99/64460 (1999-12-01), None
patent: WO-2001/075076 (2001-10-01), None
patent: WO-2002/026998 (2002-04-01), None
patent: WO 02/056910 (2002-07-01), None
patent: WO 02/061090 (2002-08-01), None
patent: WO-2002/094949 (2002-11-01), None
patent: WO 03/074569 (2003-09-01), None
patent: WO 2004/042017 (2004-05-01), None
patent: WO 2005/027966 (2005-03-01), None
Kurokawa et al. The Journal of Biological Chemistry. 2001. 276;17;14393-14399.
Adlersberg, “The Immunoglobulin Hinge (Interdomain) Region”,Ric.Clin. Lab., 6(3):191-205 (1976).
Arie et al., “Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm ofEscherichia coli”, Molecular Microbiology, 39(1):199-210 (2001).
Armour et al., “Recombinant human IgG molecules lacking Fcγ receptor I binding and monocyte triggering activities”,Eur. J. Immunol., 29:2613-2624 (1999).
Barbas et al., “In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity”,Proc. Nat. Acad. Sci. USA, 91:3809-3813 (1994).
Bloom et al., “Intrachain disulfide bond in the core hinge region of human IgG4”,Protein Science, 6:407-415 (1997).
Bothmann et al., “The PeriplasmicEscherichia coliPeptidylprolylcis,trans-Isomerase FkpA”,Journal of Biological Chemistry, 275(22):17100-17105 (2000).
Brekke et al., “Activation of complement by an IgG molecule without a genetic hinge”,Nature, 363:628-630 (1993).
Capel et al., “Heterogeneity of Human IgG Fc Receptors”,Immunomethods, 4:25-34 (1994).
Carter et al., “High LevelEscherichia coliExpression and Production of a Bivalent Humanized Antibody Fragment”,Bio/Technology, 10:163-167 (1992).
Carter et al., “Humanization of an anti-p185HER2antibody for human cancer therapy”,Proc. Natl. Acad. Sci. USA, 89:4285-4289 (1992).
Chamow et al., “A Humanized, Bispecific Immunoadhesin-Antibody that Retargets CD3+Effectors to Kill HIV-1-Infected Cells”,J. Immunol., 153:4268-4280 (1994).
Chang et al., “High-level secretion of human growth hormone byEscherichia coli”, Gene, 55:189-196 (1987).
Chen et al., “Selection and Analysis of an Optimized Anti-VEGF Antibody: Crystal Structure of an Affinity-matured Fab in Complex with Antigen”,J. Mol. Biol., 293:865-881 (1999).
Chen et al., “Chaperone Activity of DsbC”,Journal of Biological Chemistry, 274(28):19601-19605 (1999).
Chothia et al., “Canonical Structures for the Hypervariable Regions”,J. Mol. Biol., 196:901-917 (1987).
Clynes et al., “Fc receptors are required in passive and active immunity to melanoma”,Proc. Natl. Acad. Sci. USA, 95:652-656 (1998).
Daëron et al., “Fc Receptor Biology”,Annu. Rev. Immunol, 15:203-234 (1997).
de Haas et al., “Fcγ receptors of phagocytes”,J. Lab. Clin. Med., 126:330-341 (1995).
Duncan et al., “The binding site for Clq on IgG”,Nature, 232:738-740 (1988).
Friend et al., “Phase I Study of an Engineered Aglycosylated Humanized CD3 Antibody in Renal Transplant Rejection”,Transplatation, 68:1632-1637 (1999).
Guyer et al., “Immunoglobulin Binding by Mouse Intestinal Epithelial Cell Receptors”,J. Immunol., 117:587-593 (1976).
Hara et al., “Overproduction of Penicillin-Binding Protein 7 Suppresses Thermosensitive Growth Defect at Low Osmolarity due to ansprMutation ofEscherichia coli”, Microbial Drug Resistance, 2(1):63-72 (1996).
Hawkins et al., “Selection of Phage Antibodies by Binding Affinity: Mimicking Affinity Maturation”,J. Mol. Biol., 226:889-896 (1992).
Humphreys et al., “Formation of dimeric Fabs inEscherichia coli: effect of hinge size and isotype, presence of interchain disulphide bond, Fab′ expression levels, tail piece sequences and growth conditions”,J. Immunol. Methods, 209:193-202 (1997).
Isaacs et al., “A therapeutic human IgG4 monoclonal antibody that depletes target cells in humans”,Clin. Exp. Immunol., 106:427-433 (1996).
Jackson et al., “In Vitro Antibody Maturation: Improvement of a High Affinity, Neutralizing Antibody Against IL-1β”,J. Immunol., 154(7):3310-3319 (1995).
Joly et al., “Overexpression ofEscherichia colioxidoreductases increases recombinant insulin-like growth factor-I accumulation”,Proc. Natl. Acad. Sci. USA, 95:2773-2777 (1998).
Jones et al., “Replacing the complementarity-determining regions in a human antibody with those from a mouse”,Nature, 321:522-525 (1986).
Kelley et al., “Analysis of the Factor VIIa Binding Site on Human Tissue Factor: Effects of Tissue Factor Mutations on the Kinetics and Thermodynamics of Binding”,Biochemistry, 10383-10392 (1995).
Kikuchi et al., “The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) ofEscherichia coli”, Nucleic Acids Res., 9:5671-5678 (1981).
Kim et al., “Localization of the site of the murine IgG1 molecule that is involved in binding to the murine intestinal Fc receptor”,J. Immunol., 24:2429-2434 (1994).
Kim et al., “Evidence that the Hinge Region Plays a Role in Maintaining Serum Levels of the Murine IgG1 Molecule”,Mol. Immunol., 32(7):467-475 (1995).
Kipriyanov et al., “Generation of Recombinant Antibodies”,Mol. Biotech., 12:173-201 (1999).
Lee et al., “Characterization of the Gene Encoding Heat-Stable Toxin II and Preliminary Molecular Epidemiological Studies of EnterotoxigenicEscherichia coliHeat-Stable Toxin II Producers”,Infect. Immun., 42(1):264-268 (1983).
Marks et al., “By-Passing Immunization: Building High Affinity Human Antibodies by Chain Shuffling”,Bio/Technology, 10:779-783 (1992).
Merchant et al., “An efficient route to human bispecific IgG”,Nat. Biotech., 16:677-681 (1998).
Morrison et al., “Chimeric human antibody molecules: Mouse antigen-binding domains with human constant region dimmers”,Proc. N

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