Antibody peg positional isomers, compositions comprising...

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Blood proteins or globulins – e.g. – proteoglycans – platelet...

Reexamination Certificate

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C424S133100, C424S180100

Reexamination Certificate

active

07601817

ABSTRACT:
The present invention relates to recombinant protein PEG positional isomers. More specifically, it relates to PEG positional isomers of an antibody having specificity for antigenic determinants of human tumor necrosis factor alpha (TNFα). More specifically, it relates to PEG positional isomers of CDP870. The present invention also relates to compositions comprising the PEG positional isomers and therapeutic uses of the composition for treating a disease medicated by TNFα including acute and chronic immune and immunoregulatory disorders and rheumatoid-or osteo-arthritis.

REFERENCES:
patent: 5643575 (1997-07-01), Martinez et al.
patent: 5919452 (1999-07-01), Le et al.
patent: 5919455 (1999-07-01), Greenwald et al.
patent: 5932462 (1999-08-01), Harris et al.
patent: 6113906 (2000-09-01), Greenwald et al.
patent: 0 239 400 (1987-09-01), None
patent: 0 392 745 (1990-10-01), None
patent: 2 246 570 (1992-02-01), None
patent: 2 297 145 (1996-07-01), None
patent: WO 86/01533 (1986-03-01), None
patent: WO 89/01476 (1989-02-01), None
patent: WO 90/00195 (1990-01-01), None
patent: WO 90/07861 (1990-07-01), None
patent: WO 91/09967 (1991-07-01), None
patent: WO 92/11383 (1992-07-01), None
patent: WO 92/22583 (1992-12-01), None
patent: WO 93/06231 (1993-04-01), None
patent: WO 98/20734 (1998-05-01), None
patent: WO 98/25971 (1998-06-01), None
patent: WO 01/04585 (2001-01-01), None
patent: WO 01/94585 (2001-12-01), None
Monkarsh et al. Anal. Biochem. vol. 247, p. 434-440, 1997.
Adorini, L. and Sinigaglia, F., “Pathogenesis and immunotherapy of autoimmune diseases,”Trends in Immunology Today, 18(5):209-211, (1997).
Bodmer, M. et al., “Preclinical review of anti-tumor necrosis factor monoclonal antibodies,”Critical Care Medicine, 21(10):S441-S446, (1993).
Crameri, A., et al., “DNA shuffling of a family of genes from diverse species accelerates directed evolution,”Nature, 391(6664):288-291, (Jan. 1988).
Feldman, M., et al., “Anti-TNFα Therapy Is Useful in rheumatoid Arthritis and Crohn's Disease: Analysis of the Mechanism of Action Predicts Utility in Other Diseases,”Transplantation Proceedings, 30:4126-4127. (1998).
Feldmann, M., et al., “Anti-Tumor Necrosis Factor-α Therapy of Rheumatoid Arthritis,”Advances in Immunology, 64:283-350, (1997).
Fendly, B.M., et al., “Murine Monoclonal Antibodies Defining Neutralizing Epitopes on Tumor Necrosis Factor,”Hybridoma, 6(4):359-370. (1987).
Flanagan, J.G. and Rabbitts, T.H., “Arrangement of human immunoglobulin heavy chain constant region genes implies evolutionary duplication of a segment containing γ, ε and α genes,”Nature, 300(5894):709-713, (Dec. 1982).
Genebank Accession No. J00241, version J00241.1 GI:185938, “Human Ig germline kappa-L chain, C region (inv3 allele),” accessed by PTO on Apr. 6, 2002, (Jan. 5, 1995).
Hieter, P.A., et al., “Cloned Human and Mouse Kappa Immunoglobulin Constant and J Region Genes Conserve Homology in Functional Segments,”Cell, 22(Part 1):197-207, (Nov. 1980).
Keffer, J., et al., “Transgenic mice expressing human tumour necrosis factor: a predictive genetic model of arthritis,”The EMBO Journal, 10(13):4025-4031, (1991).
Kirschenbaum, L., et al., “Antibodies to TNF-α: Too little, too late?,”Critical Care Medicine, 26(10):1625-1626, (1998).
Low, N.M., et al., “Mimicking Somatic Hypermutation: Affinity Maturation of Antibodies Displayed on Bacteriophage Using a Bacterial Mutator Strain,”J. Mol. Biol., 260:359-368, (1996).
Marks, J.D., et al.. “By-Passing Immunization: Building High Affinity Human Antibodies By Chain Shuffling,”Bio/Technology, 10:779-783, (Jul. 1992).
Meager, A., et al., “Preparation and Characterization of Monoclonal Antibodies Directed Against Antigenic Determinants of Recombinant Human Tumour Necrosis Factor (rTNF).”Hybridoma, 6(3):305-311, (1987).
McKown, K.M., et al., “Lack of Efficacy of Oral Bovine Type II Collagen Added to Existing Therapy in Rheumatoid Arthritis,”Arthritis and Rheumatism, 42(6):1204-1208, (Jun. 1999).
Patten, P.A., et al., “Applications of DNA shuffling to pharmaceuticals and vaccines,”Current Opinion in Biotechnology, 87:724-733, (1997).
Rankin, E.C.C., et al., “The Therapeutic Effects of an Engineered Human Anti-Tumour Necrosis Factor Alpha Antibody (CDP571) in Rheumatoid Arthritis,”British Journal of Rheumatology, 34:334-342, (1995).
Riechmann, L., et al., “Reshaping human antibodies for therapy,”Nature, 332:323-327, (Mar. 1988).
Russell, W.K. et al., “Proteolysis in Mixed Organic-Aqueous Solvent Systems: Applications for Peptide Mass Mapping Using Mass Spectrometry,”Anal. Chem., 73:2682-2685, (2001).
Shimamoto, Y., et al., “Monoclonal antibodies against human recombinant tumor necrosis factor: prevention of endotoxic shock,”Immunology Letters, 17:311-318, (1988).
Stephens, S., et al., “Comprehensive pharmacokinetics of a humanized antibody and analysis of residual anti-idiotypic responses,”Immunology, 85:668-674, (1995).
Thompson, J., et al., “Affinity Maturation of a High-affinity Human Monoclonal Antibody Against the Third Hypervariable Loop of Human Immunodeficiency Virus: Use of Phage Display to Improve Affinity and Broaden Strain Reactivity,”J. Mol. Biol., 256:77-88. (1996).
Tracey, K.J., et al., “Shock and Tissue Injury Induced by Recombinant Human Cachectin,”Science, 234:470-474, (1985).
Vaughan, T., et al., “Human antibodies by design,”Nature Biotechnology, 16:535-539, (Jun. 1998).
Verhoeyen, M., et al., “Reshaping Human Antibodies: Grafting an Antilysozyme Activity,”Science, 239:1534-1536, (Mar. 25, 1988).
Wherry, J.C., “Tumor necrosis factor and the therapeutic potential of anti-tumor necrosis factor antibodies,”Critical Care Medicine, 21(10):S436-S440, (Oct. 1993).
Williams, R.O., et al., “Anti-tumor necrosis factor ameliorates joint disease in murine collagen-induced arthritis,”Proc. Natl. Acad. Sci. USA, 89:9784-9788, (Oct. 1992).
Wu, T.T. and Kabat, E.A., “An Analysis of the Sequences of the Variable Regions of Bence Jones Proteins and Myeloma Light Chains and Their Implications for Antibody Complementarity,”J. Exp. Med., 132:211-250, (1970).
Yang, W.P., et al., “CDR Walking Mutagenesis for the Affinity Maturation of a Potent Human Anti-HIV-1 Antibody into the Picomolar Range,”J. Mol. Biol., 254:392-403. (1995).
PCT International Search Report dated May 25, 2004 for International Application No. PCT/US03/16619, International Filing Date: May 28, 2003.
M. Aslam and A. Dent, “Bioconjugation Protein Coupling Techniques for the Biomedical Sciences,” Grove Publishers, New York (1998).
J. Milton Harris (ed.), “Poly(ethyleneglycol) Chemistry, Biotechnical and Biomedical Applications,” Plenum Press, New York (1992).
J. Milton Harris and S. Zalipsky (eds.), “Poly(ethyleneglycol) Chemistry and Biological Applications,” American Chemical Society, Washington, D.C. (1997).
Kabat, et al., “In Sequences of Proteins of Immunological Interest,” U.S. Department of Health and Human Services, NIH, USA, (1987).
Remington's Pharmaceutical Sciences, Mack Publishing Company, New Jersey (1991).

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