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
2006-03-28
2006-03-28
Ungar, Susan (Department: 1642)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
C435S069700, C435S070100, C435S070210, C435S173300, C435S972000, C530S389100, C530S387300
Reexamination Certificate
active
07018809
ABSTRACT:
Methods for the high yield production of antibody Fv-containing polypeptides, especially Fab′ and F(ab′)2antibody fragments are provided. Expression of heavy and light chain Fv in a microbial secretory system is followed by recovery of Fv from the periplasm under conditions that maintain a cysteine residue as a free thiol. The free thiol is reacted with free thiol of an antibody fragment of the same or differing specificity, or with agents such as diagnostic labels or therapeutic moieties. The products offer advantages of homogeneity and purity not available through the use of known methods for preparing such derivatives.
REFERENCES:
patent: 4444878 (1984-04-01), Paulus et al.
patent: 4642334 (1987-02-01), Moore et al.
patent: 4816567 (1989-03-01), Cabilly et al.
patent: 4946778 (1990-08-01), Ladner et al.
patent: 5219996 (1993-06-01), Bodmer et al.
patent: 5274119 (1993-12-01), Frasier et al.
patent: 5618920 (1997-04-01), Robinson et al.
patent: 5648237 (1997-07-01), Carter
patent: 5698417 (1997-12-01), Robinson et al.
patent: 5698435 (1997-12-01), Robinson et al.
patent: A-27617/88 (1989-06-01), None
patent: B-57621/90 (1991-01-01), None
patent: 136907 (1985-04-01), None
patent: 0338745 (1989-10-01), None
patent: 459 577 (1991-12-01), None
patent: WO 89/01783 (1989-03-01), None
patent: WO 89/01974 (1989-03-01), None
patent: WO 89/06692 (1989-07-01), None
patent: WO 92/01059 (1992-01-01), None
patent: WO 92/10209 (1992-06-01), None
patent: WO 92/22324 (1992-12-01), None
patent: WO 93/12220 (1993-06-01), None
del Rosario RB, et al, 1990, Bioconjugate Chemsitry, 1(1): 51-59.
Gillies, S et al. Human Alatihod. & Hybridousas 1(1):47-54, 1990.
Spiegelberg, HL. Biochem. 10:2157-2163, 1975.
Rodrigues, M. L. et al. J. Immunol. 151:6954-6961, 1993.
Sambrook et al. Molecular Cloning. Cold Spring Haron Lab. Press. Cold Spring Harbor. pp. 17.31-17.33, 1989.
Tgo et al. Journal of Immunology p. 2595 vol. 143, 1989.
Hashida et al. Journal of Applied Biochem. 6 56-63 (1984).
Johnston et al. Immunochemistry 1982 Blackwell Scientific Publication.
Voet et al., “Protein Isolation”Biochemistry,John Wiley and Sons, Inc. pp. 76-77 (1990).
Better and Horwitz, “Expression of engineered antibodies and antibody fragments in microorganisms”Methods in Enzymology178:476-496 (1989).
Better et al., “Escherichia colisecretion of an active chimeric antibody fragment”Science240:1041-1043 (1988).
Better et al., “Potent anti-CD5 ricin A chain immunoconjugates from bacterially produced Fab' and F(ab')2”Proc. Natl. Acad. Sci. USA90:457-461 (1993).
Better et al., “Production and Scale Up of Chimeric Fab Fragments from Bacteria”Advances in Gene Technology: The Molecular Biology of Immune Diseases&the Immune Response(ICSU Short Rpts.), Streilein et al., eds. vol. 10:105 (1990).
Bird et al., “Single-chain antigen-binding proteins”Science242:423-426 (1988).
Boss et al., “Assembly of functional antibodies from immunoglobulin heavy and light chains synthesised inE. coli” Nucleic Acids Research12(9):3791-3806 (1984).
Brennan et al., “Preparation of bispecific antibodies by chemical recombination of monoclonal immunoglobulin G1fragments”Science229:81-83 (1985).
Burgess et al., “Possible Dissociation of the Heparin-binding and Mitogenic Activities of Heparin binding (Acidic Fibroblast) Growth Factor-1 from Its Receptor-binding Activities by Site-directed Mutagenesis of a Single Lysine Residue”Journal of Cell Biology111:2129-2138 (1990).
Cabilly et al., “Generation of antibody activity from immunoglobulin polypeptide chains produced inEscherichia coli” Proc. Natl. Acad. Sci. USA81:3273-3277 (1984).
Cabilly, Shmuel, “Growth at sub-optimal temperatures allows the production of functional, antigen-binding Fab fragments inEscherichia coli” Gene85:553-557 (1989).
Carter et al., “High levelescherichia coliexpression and production of a bivalent humanized antibody fragment”Bio/Technology10:163-167 (1992).
Carter et al., “Humanization of an anti-p185HER2antibody for human cancer therapy”Proc. Natl. Acad. Sci.89:4285-4289 (1992).
Carter, P. and Wells, J.A., “Engineering enzyme specificity by “substrate-assisted catalysis””Science237:394-399 (1987).
Chothia, Cyrus, “Domain association in immunoglobulin molecules: The packing of variable domains”J. Mol. Biol.186:651-663 (1985).
Condra et al., “Bacterial expression of antibody fragments that block human rhinovirus infection of cultured cells”Journal of Biological Chemistry265(4):2292-2295 (1990).
Cumber et al., “Comparative stabilities in vitro and in vivo of a recombinant mouse antibody FvCys fragment and a bisFvCys conjugate”J. Immunol.,149(1):120-126 (1992).
Fanger et al., “Bispecific antibodies and targeted cellular cytotoxicity”Immunology Today12(2):51-54 (1991).
Fendly et al., “Characterization of murine monoclonal antibodies reactive to either the human epidermal growth factor receptor or HEM2
eu gene product”Cancer Research50(5):1550-1558 (Mar. 1, 1990).
Gavit et al., “Purification of a Mouse-Human Chimeric Fab Secreted fromE. coli” BioPharmpp. 28-29, 32-34, 58 (1992).
Gilles et al., “Antigen binding and biological activities of engineered mutant chimeric antibodies with human tumor specificities”Hum. Antibod. Hybridomas1(1):47-54 (1990).
Glennie et al., “Preparation and Performance of Bispecific F(ab'γ)2Antibody Containing Thioether-Linked Fab'γ Fragments”J. Immunol.139(7):2367-2375 (1987).
Glennie M.J. et al., “Bispecific F(ab'γ)2antibody for the delivery of saporin in the treatment of lymphoma”J. Immunol.141(10):3662-3670 (1988).
Glockshuber et al., “A Comparison of Strategies to Stabilize Immunoglobulin Fv-Fragements”Biochemistsry29:1362-1367 (1990).
Hammerling et al., “Use of hybrid antibody with anti-γG and anti-ferritin specificities in locating cell surface antigens by electron microscopy”Journal of Experimental Medicine128:1461-1469 (1968).
Hasemann and Capra, “High-level production of a functional immunoglobulin heterodimer in a baculovirus expression system”Proc. Natl. Acad. Sci. USA87:3942-3946 (1990).
Horwitz et al., “Secretion of functional antibody and Fab fragment from yeast cells”Proc. Natl. Acad. Sci. USA85:8678-8682 (1988).
Hudziak et al., “p185HER2Monoclonal Antibody Has Antiproliferative Effects In Vitro and Sensitizes Human Breast Tumor Cells to Tumor Necrosis Factor”Molecular&Cellular Biology9(3):1165-1172 (1989).
Huse et al., “Generation of a large combinatorial library of the immunoglobulin repertoire in phage lambda”Science246:1275-1281 (1989).
Huston et al., “Protein engineering of antibody binding sites: Recovery of specific activity in an anti-digoxin single-chain Fv analogue produced inEscherichia coli” Proc. Natl Acad. Sci. USA85:5879-5883 (1988).
Kabat et al.Sequences of Proteins of Immunological Interest,Bethesda, MD:National Institutes of Health pp. iii-xxvii, 41-176 (1987).
King et al., “Tumor Localization of Engineered Antibody Fragments”Antibody. Immunoconjugates.&Radiopharmaceuticals5(2):159-170 (1992).
Lazar et al., “Transforming Growth Factor α: Mutation of Aspartic Acid 47 and Leucine 48 Results in Different Biological Activities”Molecular&Cellular Biology8(3):1247-1252 (1988).
Liu et al., “Heteroantibody duplexes target cells for lysis by cytotoxic T lymphocytes”Proc. Natl. Acad. Sci. USA82:8648-8652 (1985).
Lupu et al., “Direct interaction of a ligand for the erB2 oncogene product with the EGF receptor and p185erbB2”Science249(4976):1552-1555 (Sep. 28, 1990).
Lyons et al., “Site-specific attachment to recombinant antibodies via introduced surface cysteine residues”Protein E
Davis Minh-Tam
Genentech Inc.
Ungar Susan
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