Drug – bio-affecting and body treating compositions – Immunoglobulin – antiserum – antibody – or antibody fragment,... – Structurally-modified antibody – immunoglobulin – or fragment...
Reexamination Certificate
2003-08-18
2009-12-22
Harris, Alana M. (Department: 1643)
Drug, bio-affecting and body treating compositions
Immunoglobulin, antiserum, antibody, or antibody fragment,...
Structurally-modified antibody, immunoglobulin, or fragment...
C424S143100, C424S144100, C424S155100, C530S387100, C530S387300, C530S387700, C530S388100, C530S388220, C530S388750, C530S388800, C530S388850
Reexamination Certificate
active
07635475
ABSTRACT:
The purpose of the present invention is to provide a diabody-type bispecific antibody, which is characterized by having low immunogenicity and high infiltrating activity into tumor tissues, and by being easily mass-produced at a low cost with use of microorganisms, and by being easily altered in function by means of genetic engineering. The diabody-type bispecific antibody shows a more remarkable effect than the conventional diabody-type bispecific antibodies and chemically synthesized bispecific antibodies even in a very low concentration and in the absence of the super antigen. The present invention is related to a diabody-type bispecific antibody, having a first specificity to a human epidermal growth factor (EGF) receptor and a second specificity to a surface antigen expressed by a cell having phagocytosis or cytotoxic activity, a single-chain polypeptide constituting the antibody or each region contained therein, a nucleic acid encoding the polypeptide, a replicable cloning vector or expression vector comprising the nucleic acid, a host cell transformed with the vector, and a pharmaceutical preparation comprising thereof.
REFERENCES:
patent: 4943533 (1990-07-01), Mendelsohn et al.
patent: 5922845 (1999-07-01), Deo et al.
patent: 6407213 (2002-06-01), Carter et al.
patent: WO-94/28027 (1994-12-01), None
patent: WO-95/16037 (1995-06-01), None
patent: WO 00/23087 (2000-04-01), None
patent: WO 02/06486 (2002-01-01), None
Kipriyanov, G. et al., Protein Engineering, 10(4): 445-453, 1997.
Rudikoff, Proc. Natl. Acad. Sci. USA, 79: 1979, 1982.
Clackson, T. et al. Nature, 352: 624-628, 1991.
Renard, I., et al. American Journal of Pathology, 160(1): 113-122, Jan. 2002).
Krebber, A. et al. Journal of Immunological Methods, 201: 35-55, 1997.
Gussow, D. and Seemann, G. Methods in Enzymology, 203: 99-121, 1991.
Hiroki Hayashi et al., Abstract #2125, 75th Annual Congress of The Japanese Biochemical Society, 74(8): Aug. 25, 2002; cited in the IDS; English translation.
Gill, G.N. et al., The Journal of Biological Chemistry, 259(12): 7755-7760, 1984.
Wu, H. et al., J. Mol. Biol., 294: 151-162, 1999.
Asano, R. et al., Abstract 3P-214, 75th Annual Congress of The Japanese Biochemical Society, 74(8): Aug. 25, 2002; English translation of document cited in IDS.
Hayashi, Hiroki, et al., The 61st General Meeting of Japanese Cancer Association Presentation, Abstract #2125, Oct. 1, 2002, English translation of document cited in IDS.
Hausmann, R., et al., Int. J. Legal Med., 112: 227-232, 1999.
Sixty-first Annual Meeting of the Japanese Cancer Association, Oct. 1-3, 2002, Tokyo, Japanese Journal of Cancer Research, vol. 93, Supplement (Aug. 20, 2002).
Hollinger et al., Proc. Natl. Acad. Sci. USA, vol. 90, pp. 6444-6448, Jul. 1993.
Negri et al., “In Vitro and in vivo stability and anti-tumor efficacy of an anti-EGFR/anti-CD3 F(ab')2 bispecific monoclonal antibody,” British Journal of Cancer, vol. 72, pp. 928-933 (1995).
Zhu et al., “High Level Secretion of a Humanized Bispecific Diabody fromEscherichia coli,” Biotechnology, vol. 14., pp. 192-196 (Feb. 1996).
Adair et al., “Humanization of the murine anti-human CD3 monoclonal antibody OKT3,” Hum. Antibod. Hybridomas,vol. 5, Nos. 1 and 2, pp. 41-47 (1994).
Ferrini et al., “Targeting of T Lymphocytes Against EGF-Receptor+Tumor Cells by Bispecific Monoclonal Antibodies: Requirement of CD3 Molecule Cross-Linking for T-Cell Activation,” Int. J. Cancer, vol. 55, pp. 931-937 (1993).
M. R. Shalaby et al., “Development of Humanized Bispecific Antibodies Reactive with Cytotoxic Lymphocytes and Tumor Cells Overexpressing the HER2 Protooncogene,” J. Exp. Med., vol. 175, pp. 217-225 (Jan. 1992).
Carter et al., “Humanization of anti-p185HER2antibody for human cancer therapy,” Immunology, Proc. Natl. Acad. Sci. USA, vol. 89, pp. 4285-4289 (May 1992).
Zhu et al., “Remodeling domain interfaces to enchance heterodimer formation,” Protein Science, vol. 6, pp. 781-788 (1997).
Abstracting Journal for 75th Annual Congress of The Japanese Biochemical Society, vol. 74, No. 8, Aug. 25, 2002.
Asano Ryutaro
Kudo Toshio
Kumagai Izumi
Tsumoto Kouhei
Birch & Stewart Kolasch & Birch, LLP
Harris Alana M.
Holleran Anne L
Tohoku Techno Arch Co., Ltd.
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