Drug – bio-affecting and body treating compositions – Immunoglobulin – antiserum – antibody – or antibody fragment,... – Anti-idiotypic
Reexamination Certificate
1995-05-23
2002-08-13
Bansal, Geetha P. (Department: 1642)
Drug, bio-affecting and body treating compositions
Immunoglobulin, antiserum, antibody, or antibody fragment,...
Anti-idiotypic
C424S130100, C424S133100, C424S184100, C424S197110, C424S197110, C435S325000, C435S326000, C435S327000, C435S346000, C530S387100, C530S387200, C530S387300, C530S387500, C530S388100, C530S388250, C530S389100, C530S389300, C530S810000, C530S808000, C530S806000
Reexamination Certificate
active
06432402
ABSTRACT:
BACKGROUND OF THE INVENTION
R24, IgG3 mouse monoclonal antibody (mAb) raised against a human melanoma, (ATCC Accession No. HB 8445) recognizes the GD
3
ganglioside. The GD
3
ganglioside is abundantly expressed on most melanomas, however, expression of the GD
3
ganglioside on normal tissue is selective and occurs at low concentrations (1). Gangliosides are a subset of glycosphinogolipids which in turn are a subset of glycolipids. Glycolipids, as their name implies, are sugar-containing lipids.
R24 comprises a known mixture of three variant antibody species (
FIG. 11
) designated V1-V24, V2-R24, and R24. The V1-R24 and V2-R24 variants comprise one and two irrelevant antibody light chains, respectively; in contrast. R24 comprises relevant light chains. Generally, light and heavy antibody chains in combination effect specific antibody-antigen binding. However, antibodies comprising irrelevant antibody light chains, unlike antibodies comprising relevant antibody light chains, do not specifically bind an antigen.
In order to avoid confusion, the R24 variant from hereinafter will be referred to as “R24” and R24 comprising the three variant species will be referred to as the “R24 composition.” Each variant exhibits differences which imply that the GD
3
-binding region (also termed “paratope”) of V1-R24, V2-R24, and R24 are altered.
Anti-idiotypic monoclonal antibodies which mimic and possess the internal image of a saccharidic epitope have been developed (2). The saccharidic epitope is a tumor associated globoside, i.e. a glycolipid. However, these anti-idiotypic monoclonal antibodies do not specifically mimic a glycosphingolipid, a ganglioside, or more particularly the GD
3
ganglioside. Additionally, these anti-idiotypic monoclonal antibodies are not directed against R24 or any antibodies which specifically bind a glycosphingolipid or a ganglioside, let alone the GD
3
ganglioside.
Mice have been primed against capsular antigens of pathogenic bacteria by administration of monoclonal anti-idiotypic antibodies which mimic the polysaccharide capsule of
E. coli
(a gram negative bacteria) (3). It is generally known that lipopolysaccharides (LPS) is a major component of the outer membrane of gram negative bacteria and is released when bacteria are lysed. LPS consists of a heteropolysaccharide chain linked coavlently to a glycolipid. It is important to point out that although these monoclonal anti-idiotypic antibodies were used as a means to prime a subject against a LPS, there is no suggestion of generating monoclonal anti-idiotypic antibodies against R24 or any antibodies which would specifically bind glycosphingolipids or gangliosides, in particular the GD
3
ganglioside.
The GD
3
ganglioside is poorly immunogenic (1). Accordingly, the GD
3
ganglioside is an appealing target for cancer immunotherapy because of the commercial utility of designing molecules which would structurally mimic GD
3
and possess dramatically significant immunogenic properties.
SUMMARY OF THE INVENTION
The present invention also provides an anti-idiotypic monoclonal antibody which specifically induces an immune response against a glycosphingolipid and more specifically against a ganglioside. Additionally, this invention provides a composition of matter comprising an effective amount of a cytokine and a melanoma ganglioside-specific antibody attached to a carrier. Finally, this invention provides a method of generating the previously-identified anti-idiotypic antibody which comprises: (a) preparing an antibody; (b) purifying the antibody; (c) attaching the antibody onto a carrier so as to produce an immunogen; (d) combining the immunogen with a cytokine so as to produce a novel immunogen-cytokine combination; and (e) injecting the novel immunogen-cytokine combination into a mammal thereby producing the anti-idiotypic antibody.
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Bucholtz,Seminars in Oncol. Nursing,vol. 3, No. 1, p. 67-73 (1989).
Chapman, et al. (1993) “Use of BEC2 Anti-Idiotypic Monoclonal Antibody (Mab) To Induce Antibodies Against GD3 Ganglioside in Melanoma Patients,” Proceedings of ASCO, vol. 12, 1323:388; (Exhibit 7).
Chapman et al. “Pilot Trial of Anti-Idiotypic Monoclonal Antibody BEC2 in Patients with Metastatic Melanoma,” Proceedings of the American Association for Cancer Research, vol. 33:208 (1992); (Exhibit 8).
Forstrom J. W., et al., “Immunization To A Syngeneic Sarcoma By A Monoclonal Auto-anti-idiotypic Antibody”,Nature,vol. 303, Jun. 16, 1983, pp. 627-629; (Exhibit 9).
Irie et al. Advances in the Biology and Clinical Management of Melanoma, 35thAnnual Clinical Conference and Twenty Four Annual Pathology Program, Nov. 20-23, 1999, pp. 46-47, 1991; (Exhibit 10).
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Koprowski H., et al., “Human Anti-idiotype Antibodies In Cancer Patients: Is The Modulation Of The Immune Response Beneficial For The Patient?”,PNAS,Jan. 1984, vol. 81, pp. 216-219 ; (Exhibit 12).
Livingston, P.O. et al., (1987) “Vaccines containing purified GM2 ganglioside elicit GM2 antibodies in melanoma patients”Immunology84:2911-2915; (Exhibit 13).
Miller, et al., Proc. 11th Annual Cancer Symposium, Scripps Memorial Hospitals Cancer Center, pp. 3-5, 1987; (Exhibit 14).
Morrison, et al., “Transfectomas Provide Novel Chimeric Antibodies”, Science 1985, vol. 229, pp. 1202-1207; (Exhibit 15).
Paul, W.E., MD, ed., Fundamental Immunology 242 (3d. Ed. 1993); (Exhibit 16).
Soederstrom, et al. “TheEscherichia coliK1 Capsule Shares Antigenic Determinants with the Human Gangliosides GM3 and GD3”,New England Journal of Medicine,Mar. 1984, vol. 310: 726-727; (Exhibit 17).
Staruch, et al., “The Adjuvanticity Of Interleukin 1 In Vivo”,Journal of Immunology1983, vol. 130, pp. 2191-2194; (Exhibit 18).
Tsuchida et al., “Gangliosides of Human Melanoma,”J. Natl. Cancer Inst.Jan. 1987 vol. 78 pp. 45-54; (Exhibit 19).
Viale G., et al., “Anti-human Tumor Antibodies Induced In Mice And Rabbits By “Internal Image” Anti-idiotypic Monclonal Immunogloblins”,J. Immunology,Dec. 15, 1987, vol. 139, pp. 4250-4255; (Exhibit 20).
Vitetta et al., “Redesigning Nature's Poisons to Create Anti-Tumor Reagents,”Sciencevol. 238 p. 1098-1104, Nov. 27, 1987; (Exhibit 21).
Wei, W-Z., et al., “Improved Anti-tumor Reactivity With Monoclonal Anti-idiotypic Antibody Conjugated To Syngeneic Mouse Red Blood Cells”,J. Immunology Methods,1989, vol. 122, pp. 227-234. (Exhibit 22).
Anderson, et al., “Idiotype Network Responses to Murine Immunoglobulin G3 Anti-Carbohydrate Antibodies”, Journal of Immunotherapy, 1992, vol. 11, pp. 267-273 (Exhibit 10).
Bentley, et al., “Three-dimensional Structure Of An Idiotype-anti-idiotope Complex”, Nature 1990, vol. 348, pp. 254-257 (Exhibit 11).
Chapman, et al., “An Anti-idiotypic Monoclonal Antibody Carrying The Internal Image Of GD3 Ganglioside”, Eightieth Annual Meeting Of The American Association For Cancer Research, Mar. 1989, vol. 30, p. 344 (Exhibit 12).
Cheresh, et al., “Disialoganglioside GD3 On Human Melanoma Serves As A Relevant Target Antigen For Monoclonal Antibody-mediated Tumor Cytolysis”, PNAS 1985, vol. 82, pp. 5155-5159 (Exhibit 13).
Davis, et al., “Antibody and HIV-1 gp120 Recognition Of CD4 Undermines The Concept of Mimicry Between Antibodies And Receptors”, Nature 1992, vol. 358, pp. 76-79 (Exhibit 14);
Dippold, et
Chapman Paul B.
Houghton Alan N.
Bansal Geetha P.
Cooper & Dunham LLP
Sloan-Kettering Institute for Cancer Research
White John P.
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