Single chain antibody against mutant p53

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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C530S387100, C530S387300, C530S387900, C530S388800, C530S388850

Reexamination Certificate

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10247488

ABSTRACT:
More than 90% of mutations found in the p53 protein produce a conformational change in p53 which results in the exposure of an epitope, which is otherwise hidden in the hydrophobic core of the molecule. A single chain antibody (scFv) which specifically recognizes this common mutant epitope in mutant p53 but not in wild type p53 is disclosed. Also described are a DNA molecule encoding the scFv, pharmaceutical compositions comprising the antibody and methods of treatment using the pharmaceutical compositions.

REFERENCES:
patent: 4816567 (1989-03-01), Cabilly et al.
patent: 5091513 (1992-02-01), Huston et al.
patent: 5258498 (1993-11-01), Huston et al.
patent: 5618920 (1997-04-01), Robinson et al.
patent: 5756669 (1998-05-01), Bischoff et al.
patent: 6630584 (2003-10-01), Solomon et al.
patent: 2002/0155114 (2002-10-01), Marks et al.
Rudikoff et al (Proc. Natl. Acad. Sci. USA 1982 vol. 79 p. 1979).
Burgess et al, Journal of Cell Biology vol. 111 Nov. 1990 2129-2138.
Lazar et al Molecular and Cellular Biology Mar. 1988 vol. 8 No. 3 1247-1252.
Schwartz et al, Proc Natl Acad Sci USA vol. 84:6408-6411 (1987).
Lin et al Biochemistry USA vol. 14:1559-1563 (1975).
Acland et al., Nature vol. 343:662-665 (1990).
Ibragimova and Eade (Biophysical Journal, Oct. 1999, vol. 77, pp. 2191-2198).
Orlandi et al (Proc. Natl. Acad. Sci. USA, 86:3833-3837, 1989).
Marasco, W.A., “Intracellular antibodies (intrabodies) as research reagents and therapeutic molecules for gene therapy”,Immunotechnology, vol. 1, pp. 1-19, (1995).
Jannot, C.B., et al., “Characterization of scFv-421, a Single-Chain Antibody Targeted to p53”,Biochemical and Biophysical Research Comm., vol. 230, No. 2, pp. 242-246, (1997).
Yewdell, J.W., et al., “Monoclonal Antibody Analysis of p53 Expression in Normal and Transformed Cells”,Journal of Virology, vol. 59, No. 2, pp. 444-452, (Aug. 1986).
Harlow, E., et al., “Monoclonal Antibodies Specific for Simian Virus 40 Tumor Antigens”,Journal of Virology, Vo. 39, No. 3, pp. 861-869, (Sep. 1981).
Gannon, J.V., et al., “Activating mutations in p53 produce a common conformational effect. A monoclonal antibody specific for the mutant form”,The EMBO Journal, vol. 9, No. 5, pp. 1595-1602, (1990).
Gamble, J., et al., “Evidence that Immunological Variants of p53 Represent Alternative Protein Conformations”,Virology, vol. 162, pp. 452-458, (1988).
Stephen, C.W., et al., “Mutant Conformation of p53 Precise Epitope Mapping Using a Filamentous Phage Epitope Library”,J. Mol. Biol. vol. 225, pp. 577-583, (1992).
Cohen, P.A., et al., “Characterization of a new intrabody directed against the N-terminal region of human p53”,Oncogene, vol. 17, pp. 2445-2456, (1998).
Milner, J., et al., “A new anti-p53 monoclonal antibody, previously reported to be directed against the large T antigen of simian virus 40”,Oncogene, vol. 1, pp. 453-455, (1987).
Bowie et al., Science, vol. 247, pp. 1306-1310, 1990.
Burgess et al., Journal of Cell Biology, vol. 111, pp. 2129-2138, 1990.
Lazar et al., Molecular and Cell Biology, vol. 8, pp. 1247-1252, 1988.
Bork, Genome Research, vol. 10, pp. 398-400, 2000.
Jones et al., Advanced Drug Delivery Reviews, vol. 31, pp. 153-170, 1998.
Anderson, Nature, vol. 392, pp. 25-30, 1998.
Verma et al., Nature, vol. 389, pp. 239-242, 1997.
Ross et al., Human Gene Therapy, vol. 7, pp. 1781-1790, 1996.
Cohen et al., Science, vol. 265, pp. 1371-1371, 1994.
Cohen et al. “Characterization of A New Intrabody Directed Against the N-Terminal Region of Human P53”, Oncogene, 17(19): 2445-2456, 1998. Abstract, p. 2452, col. 1; Claims: 1-29.
Caron de Fromentel et al. “Restoration of Transcriptional Activity of P53 Mutants in Human Tumour Cells by Intracellular Expression of Anti-P53 Single Chain Fv Fragments”, Oncogene, 18(2): 551-557, 1999. Abstract, p. 556, Fig.6; Claims: 1-29.
Jannot et al. “Characterization of SCFV-421, A Single-Chain Antibody Targeted to P53”, Biochemical and Biophysical Research Communications, 230(2): 242-246, 1997. Abstract, p. 245, col. 1-2; Claims: 1-29.
Govorko et al. “Single-Chain Antibody Against the Common Epitope of Mutant P53: Isolation and Intracytosolic Expression in Mammalian Cells”, Journal of Immunological Methods, 258(1-2): 169-181, 2001. Abstract. p. 179, col. 2; Claims: 1-29.
Fischer-Fantuzzi et al. “Cell-Dependent Efficiency of Reiterated Nuclear Signals in A Mutant Simian Virus 40 Oncoprotein Targeted to the Nucleus”, Mol. Cell Biol., 8(12): 5495-5503, 1988. Abstract.
Pavlinkova et al. “Effects of Humanization and Gene Shuffling on Immunogenicity and Antigen Binding of Anti-TAG-72 Single-Chain Fvs”, Int. J. Cancer, 94(5): 717-726, 2001. Abstract.
Cheson “Rituximab: Clinical Development and Future Directions”, Expert. Opin. Biol. Ther., 2(1): 97-110, 2002. Abstract.
Grillo-Lopez et al. “Monoclonal Antibodies: A New Era in the Treatment of Non-Hodgkin's Lymphoma”, Curr. Pharm. Biotechnol., 2(4): 301-311, 2001. Abstract.
Kashmiri et al. “Development of A Minimally Immunogenic Variant of Humanized Anti-Carcinoma Monoclonal Antibody CC49”, Crit. Rev. Oncol. Hematol., 38(1): 3-16, 2001. Abstract.
Keating et al. “Emerging Information on the Use of Rituximab in Chronic Lymphocytic Leukemia”, Semin. Oncol., 29(1 Suppl.2): 70-74, 2002. Abstract.
Hortobagyi “Overview of Treatment Results With Trastuzumab (Herceptin) in Metastatic Breast Cancer”, Semin. Oncol., 28(6 Suppl.18): 43-47, 2001. Abstract).
Munro et al. “A C-Terminal Signal Prevents Sectetion of Luminal ER Proteins”, Cell, 48(5): 899-907, 1987. Abstract.
Silver “How Proteins Enter the Nucleus”, Cell, 64(3): 489-497, 1991. Abstract.
Wu et al. “Humanization of A Murine Monoclonal Antibody by Simultaneous Optimization of Framework and CDR Residues”, J. Mol. Biol., 294(1): 151-162, 1999. Abstract.
Barbas et al. “Selection and Evolution of High-Affinity Human Anti-Viral Antibodies”, TIBTECH, 14: 230-234, 1996.
Brown et al. “Tolerance to Single, But Not Multiple, Amino Acid Replacements in Antibody VH CDR2. A Means of Minimizing B Cells Wastage From Somatic Hypermutation?”, The Journal of Immunology, 156: 3285-3291, 1996. Abstract.
Nishimiya et al. “Thermodynamic Consequences of Grafting Enhanced Affinity Toward the Mutated Antigen Onto An Antibody. The Case of Anti-Lysozyme Antibody, HyHEL-10”, The Journal of Biological Chemistry, 275(17): 12813-12820, 2000.
Gamble et al. “Evidence That Immunological Variants of P53 Represent Alternative Protein Conformations”, Virology, 162(2): 452-458, 1988. Abstract.
Gannon et al. “Activating Mutations in P53 Produce A Common Conformational Effect. A Monoclonal Antibody Specific for the Mutant Form”, The EMBO Journal, 9(5): 1595-1602, 1990.
Harlow et al. “Monoclonal Antibodies Specific for Simian Virus 40 Tumor Antigens”, Journal of Virology, 39(3): 861-869, 1981.
Marasco “Intracellular Antibodies (Intrabodies) as Research Reagents and Therapeutic Moleculaes for Gene Therapy”, Immunotherapy, 1: 1-19, 1995.
Milner et al. “A New Anti-P53 Monoclonal Antibody, Previously Reported to Be Directed Against the Large T Antigen of Simian Virus 40”, Oncogene, 1(4): 453-455, 1987.
Murray et al. “Codon Usage in Plant Genes”, Nucleic Acids Research, 17(2): 477-498, 1989.
Smythe et al. “Production of Linear Polymers of HIV Gp120-Binding Domains”, Protein Engineering, 7(2): 145-147, 1994. Abstract.
Stephen et al. “Mutant Confimation of P53 *1. Precise Epitope Mapping Using A Filamentous Phage Epitope Library”, Journal of Molecular Biology, 225(3): 577-583, 1992. Abstract.
Yewdell et al. “Monoclonal Antibody Analysis of P53 Expression in Normal and Transformed Cells”, Journal of Virology, 59(2): 444-452, 1986.
Verma et

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