Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Carbohydrate doai
Reexamination Certificate
2006-02-16
2010-10-26
Crane, Lawrence E (Department: 1623)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Carbohydrate doai
C514S061000, C536S123100, C536S123130
Reexamination Certificate
active
07820628
ABSTRACT:
The present invention discloses that an intratumoral injection of: i) glycolipids with α-gal epitope; ii) gene vectors comprising an α1,3galactosyltransferase gene; or iii) a mixture of α1,3galactosyltransferase, neuraminidase, and uridine diphosphate galactose results in tumor regression and/or destruction. Binding of the natural anti-Gal antibody to de novo expressed tumoral α-gal epitopes induces inflammation resulting in an anti-Gal antibody mediated opsonization of tumor cells and their uptake by antigen presenting cells. These antigen presenting cells migrate to draining lymph nodes and activate tumor specific T cells thereby converting the treated tumor lesions into in situ autologous tumor vaccines. This therapy can be applied to patients with multiple lesions and in neo-adjuvant therapy to patients before tumor resection. In addition to the regression and/or destruction of the treated tumor, such a vaccine will help in the immune mediated destruction of micrometastases that are not detectable during the removal of the treated tumor.
REFERENCES:
patent: 5869035 (1999-02-01), Link, Jr. et al.
patent: 5879675 (1999-03-01), Galili et al.
patent: 6361775 (2002-03-01), Galili et al.
patent: 6420335 (2002-07-01), Weichselbaum et al.
patent: 2002/0041869 (2002-04-01), Ali et al.
patent: 2004/0191229 (2004-09-01), Link, Jr. et al.
patent: 2004/0214783 (2004-10-01), Terman
Galili, U, “Autologous Tumor Vaccines Processed to Express [alpha]-gal Epitopes: A Practical Approach to Immunotherapy in Cancer,” Cancer Immunology and Immunotherapy, 53, 635-645 (2004); published online on Jun. 16, 2004.
Manches et al., “Anti-GAL-mediated Targeting of Human B Lymphoma Cells to Antigen-presenting Cells: A Potential Method for Immunotherapy Using Autologous Tumor Cells,” Haematologica, 90(5), 625-634 (2005).
Galili et al., “Intratumoral Injection of [alpha]-gal Glycolipids Induces Zenograft-Like Destruction and Conversion of Lesions into Endogenous Vaccines,” Journal of Immunology, 178, 4626-4687 (2007).
Beers et al. (eds.), a portion of the Index of The Merck Manual of Diagnosis and Therapy, 17th Edition, Merck & Co., Inc., Rahway, NJ, Jan. 1999, only title pages and text pp. 2769-2770, 2808 & 2823 supplied.
Buehler et al., “Use of the enzyme-linked immunoadsorbent assay to monitor the purification of glycosphingolipid antigens by high-performance liquid chromatography,”Anal Biochem, 164:521-525, 1987abstract only.
Chen et al., “Synthesis of alpha-gal epitopes (Galalpha1-3Galbeta1-4GlcNAc-R) on human tumor cells by recombinant alpha1,3galactosyltransferase produced inPichia pastoris,” Glycobiology, 11:577-586, 2001.
Chien et al., “Isolation and characterization of a heptaglycosylceramide from bovine erythrocyte membranes,”J Lipid Res, 20:669-673, 1979.
Collins et al., “Cardiac xenografts between primate species provide evidence for the importance of the alpha-galactosyl determinant in hyperacute rejection,”J Immunol, 154:5500-5510, 1995.
Dabrowski et al., “Immunochemistry of I/i-active oligo- and polyglycosylceramides from rabbit erythrocyte membranes,”J Biol Chem, 259:7648-7651, 1984.
Deriy et al., “Expression of alpha-gal epitopes on HeLa cells transduced with adenovirus containing alpha1,3galactosyltransferase cDNA,”Glycobiology, 12:135-144, 2002.
Deriy et al., “In vivo targeting of vaccinating tumor cells to antigen-presenting cells by a gene therapy method with adenovirus containing the α1,3galatosyltransferase gene,”Cancer Gene Therapy, 12:528-539, 2005.
Dunn et al., “Cancer immunoediting: from immunosurveillance to tumor escape,”Nat Immunol, 3:991-998, 2002.
Galili et al., “A unique natural human IgG antibody with anti-alpha-galactosyl specificity,”J Exp Med, 160:1519-1531, 1984.
Galili et al., Human natural anti-alpha-galactosyl IgG. II. The specific recognition of alpha (1—3)-linked galactose residues,J Exp Med, 162:573-582, 1985.
Galili et al., “Evolutionary relationship between the natural anti-Gal antibody and the Gal alpha 1—3Gal epitope in primates,”Proc Natl Acad Sci USA, 84:1369-1373, 1987.
Galili et al., “Interaction between human natural anti-alpha-galactosyl immunoglobulin G and bacteria of the human flora,”Infect Immun, 56:1730-1737, 1988.
Galili et al., “Man, apes, and Old World monkeys differ from other mammals in the expression of alpha-galactosyl epitopes on nucleated cells,”J Biol Chem, 263:17755-17762, 1988.
Galili et al., “Gene sequences suggest inactivation of alpha-1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys,”Proc Natl Acad Sci USA; 88:7401-7404, 1991.
Galili, “Evolution and pathophysiology of the human natural anti-alpha-galactosyl IgG (anti-Gal) antibody,”Springer Semin Immunopathol. 15:155-171, 1993.
Galili et al., “Suppression of α-galactosyl epitopes synthesis and production of the natural anti-Gal antibody: a major evolutionary event in ancestral Old World primates,”Human Evolution, 29:433-442, 1995.
Galili, “Autologous tumor vaccines processed to express alpha-gal epitopes: a practical approach to immunotherapy in cancer,”Cancer Immunology Immunotherapy, 53:935-945, 2004.
Hamadeh et al., “Anti-alpha-galactosyl immunoglobulin A (IgA), IgG, and IgM in human secretions,”Clin Diagnos Lab Immunol, 2:125-131, 1995.
Honma et al., “Isolation and partial structural characterization of macroglycolipid from rabbit erythrocyte membranes,”J Biochem(Tokyo). 90:1187-1196, 1981abstract only.
Kanda et al., “Incorporation of spin-labeled ganglioside analogues into cell and liposomal membranes,”J Biochem(Tokyo). 91:1707-1718, 1982abstract only.
Karttunen et al., “Detection of rare antigen-presenting cells by the lacZ T-cell activation assay suggests an expression cloning strategy for T-cell antigens,”Proc Natl Acad Sci USA, 89:6020-6024, 1992.
LaTemple et al., “Increased immunogenicity of tumor vaccines complexed with anti-Gal: studies in knockout mice for alpha1,3galactosyltransferase,”Cancer Res, 59:3417-3423, 1999.
Lugade et al., “Local radiation therapy of B16 melanoma tumors increases the generation of tumor antigen-specific effector cells that traffic to the tumor,”J Immunol, 174:7516-7523, 2005.
Manches et al., “Anti-Gal-mediated targeting of human B lymphoma cells to antigen-presenting cells: a potential method for immunotherapy using autologous tumor cells,”Haematologica, 90:625-634, 2005.
Marrogi et al., “Study of tumor infiltrating lymphocytes and transforming growth factor-beta as prognostic factors in breast carcinoma,”Int J Cancer, 74:492-501, 1997.
Naito et al., “CD8+ T cells infiltrated within cancer cell nests as a prognostic factor in human colorectal cancer,”Cancer Res. 58:3491-3494, 1998.
Nakano et al., “Proliferative activity of intratumoral CD8+ T-lymphocytes as a prognostic factor in human renal cell carcinoma: clinicopathologic demonstration of antitumor immunity,”Cancer Res, 61:5132-5136, 2001.
Palmetshofer et al., “Alpha-galactosyl epitope-mediated activation of porcine aortic endothelial cells: type I activation,”Transplantation, 65:844-853, 1998.
Palmetshofer et at, “Alpha-galactosyl epitope-mediated activation of porcine aortic endothelial cells: type II activation,”Transplantation, 65:971-978, 1998.
Pardoll, “Therapeutic vaccination for cancer,”Clin Immunol, 95:S44-49, 2000.
Sandrin et al., “Natural human anti-Gal alpha(1,3)Gal antibodies react with human mucin peptides,”Glycoconj J, 14:97-105, 1997.
Schumacher et al., “Prognostic significance of activated CD8(+) T cell infiltrations within esophageal carcinomas,”Cancer Res, 61:3932-3936, 2001.
Spiegel et al., “Fluorescent
Crane Lawrence E
Medlen & Carroll LLP
University of Massachusetts Medical School
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