Methods for modulating the efficacy of nucleic acid based...

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Carbohydrate doai

Reexamination Certificate

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C435S006120, C435S091100, C435S455000, C514S001000, C536S023100, C536S024500

Reexamination Certificate

active

07960364

ABSTRACT:
Covalently reactive antigen analogs are disclosed herein. The antigens of the invention may be used to stimulate production of catalytic antibodies specific for predetermined antigens associated with particular medical disorders. The antigen analogs may also be used to permanently inactivate endogenously produced catalytic antibodies produced in certain autoimmune diseases as well as in certain lymphoproliferative disorders. Also provided are methods for modulating the efficacy of nucleic acid based therapeutics.

REFERENCES:
patent: 5948658 (1999-09-01), Landry
Paul, S., D.J. Volle, C.M. Beach, D.R. Johnson, M.J. Powell, and R.J. Massey. Catalytic Hydrolysis of Vasoactive Intestinal Peptide by Human Autoantibody. Science. 1989. 244:1158-1162.
Paul, S., S. Mei, B. Mody, S.H. Eklund, C.M. Beach, R.J. Massey, and F. Hamel. Cleavage of Vasoactive Intestinal Peptide at Multiple Sites by Autoantibodies. The Journal of Biological Chemistry. 1991. 266:16128-16134.
Li, L., S. Paul, S. Tyutyulkova, M.D. Kazatchkine, and S. Kaveri. Catalytic Activity of Anti-Thyroglobulin Antibodies. The Journal of Immunology. 1995. 3328-3332.
Shuster, A.M., G.V. Gololobov, O.A. Kvashuk, A.E. Bogomolova, I.V. Smirnov, and A.G. Gabibov. DNA Hydrolyzing Autoantibodies. Science. 1992. 256:665-667.
Tawfik, D.S., R. Chap, B.S. Green, M. Sela, and Z. Eshhar. Unexpectedly high occurrance of catalytic antibodies in MRL/Ipr and SJL mice immunized with a transition-state analog: Is there a linkage to autoimmunity? Immunology. 1995. 92:2145-2149.
Davies, D.R. and S. Chacko. Antibody Structure. Acc. Chem. Res. 1993. 26:421-427.
Sun, M., Q.S. Gao, L. Li, and S. Paul. Proteolytic Activity of an Antibody Light Chain. The Journal of Immunology. 1994. 5121-5126.
Gao, Q.S., M. Sun, S. Tyutyulkova, D. Webster, A. Rees, A Tramontano, R.J. Massey, and S. Paul. Molecular Cloning of a Proteolytic Antibody Light Chain. The Journal of Biological Chemistry. 1994. 269:32389-32393.
Titmas, R.C., T.S. Angeles, R. Sugasawara, N. Aman, M.J. Darsley, G. Blackburn, and M.T. Martin. Aspects of Antibody-Catalyzed Primary Amide Hydrolysis. Applied Biochemistry and Biotechnology. 1994. 47:277-290.
Gao, Q.S., M. Sun, A.R. Rees, and S. Paul. Site-directed Mutagenesis of Proteolytic Antibody Light Chain. J. Mol. Bio. 1995. 253:658-664.
Lerner, R.A., S.J. Benkovic, and P.G. Schultz. At the Crossroads of Chemistry and Immunology: Catalytic Antibodies. Science 1991. 252:659-667.
Tyutyulkova, S., Q.S. Gao, A. Thompson, S. Rennard, and S. Paul. Efficient vasoactive intestinal polypeptide hydrolyzing autoantibody light chains selected by phage display. Biochimica et Biophysica Acta. 1996. 217-223.
Sampson, N. S. and P.A. Bartlett. Peptide Phosphonylating Agents as Irreversible Inhibitors of Serine Proteases and Models of the Tetrahedral Intermediates. Biochemistry. 1991. 30:2255-2262.
Baylis, E.K., C.D. Campbell, and J.G. Dingwall. Aminoalkylphosphonous Acids. Isosteres of the Protein Amino Acids. J. Chem. Soc Perkin Trans. 1984. 2845-2853.
Clackson, T., H.R. Hoogenboom, A. D. Griffiths, and G. Winter. Making antibody fragments using phage display libraries. Nature. 1991. 532:624-628.
McCafferty, J., K.J. Fitzgerald, J. Earnshaw, D.J. Chiswell, J. Link, R. Smith, and J. Kenten. Selection and Rapid Purification of Murine Antibody Fragments That Bind a Transition-State Analog by Phage Display. Applied Biochemistry and Biotechnology. 1994. 47:157-173.
Mei, S., B. Mody, S.H. Eklund, and S. Paul. Vasoactive Intestinal Peptide Hydrolysis by Antibody Ligh Chains. The Journal of Biological Chemistry. 1991. 266:15571-15574.
Bone, R., N.S. Sampson, P.A. Bartlett, and D.A. Agard. Crystal Structures of .alpha.-Lytic Protease Complexes with Irreversibly Bound Phosphonate Esters. Biochemistry. 1991. 30:2263-2272.
Lax, I., R. Fischer, C. Ng, J. Serge, A. Ullrich, D. Givol, and J. Schlessinger. Noncontiguous regions in the extracellular domain of EGF receptor define ligand-binding specificity. Cell Regulation. 1991. 2:337-345.
Moore, J. and A. Trkola. HIV Type 1 Coreceptors, Neutralization Serotypes, and Vaccine Development. AIDS Research and Human Retroviruses. 1997. 13:733-736.
Thali, M., C. Furman, D.D. Ho, J. Robinson, S. Tilley, A. Pinter, and J. Sodroski. Discontinuous, Conserver Neutralization Epitopes Overlapping the CD4-Binding Region of Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein. Journal of Virology. 1992. 66:5635-5641.
Pollard, S.R., W. Meier, P. Chow, J.J. Rosa, and D.C. Wiley. CD4-Binding regions of human immunodeficiency virus envelope glycoprotein gp120 defined by proteolytic digestion. Proc. Natl. Acad. Sci. 1991. 88:11320-11324.
Kalaga, R., L. Li, J.R. O'Dell, and P. Sudhir. Unexpected Presence of Polyreactive Catalytic Antibodies in IgG from Unimmunized Donors and Decreased Levels in Rheumatoid Arthritis. The Journal of Immunology. 1995. 2695-2702.
Tramontano, A., K.D. Janda, and R.A. Lemer. Chemical reactivity at an antibody binding site elicited by mechanistic design of a synthetic antigen. Proc. Natl. Acad. Sci. USA. 1986. 83:6736-6740.
Bermas, B.L., M. Petri, J.A. Berzofsky, A. Waisman, G.M. Shearer, and E. Mozes. Binding of Glycoprotein 120 and Peptides from the HIV-1 Envelope by Autoantibodies in Mice with Experimentally Induced Systemic Lupus Erythematosus and in Patients with the Disease. AIDS Research and Human Retroviruses. 1994. 10:1071-1077.
Sudhir, P., L. Li, R. Kalaga, P. Wilkins-Stevens, F.J. Stevens, and A. Solomon. Natural Catalytic Antibodies: Peptide-hydrolyzing Activities of Bence Jones Proteins and V.sub.L Fragment. The Journal of Biological Chemistry. 1995. 270:15257-15261.
Pollack, S.J., P. Hsiun, and P.G. Shultz. Stereospecific Hydrolysis of Alkyl Esters by Antibodies. J. Am. Chem. Soc. 1989. 111:5961-5962.
Ahlers, J.D., C.D. Pendelton, N. Dunlop, A. Minassian, P.L. Nara, and J.A. Berzofsky. Construction of an HIV-1 Peptide Vaccine Containing a Multideterminant Helper Peptide Linked to a V3 Loop Peptide 18 Inducing Strong Neutralizing Antibody Responses in Mice of Multiple MHC Haplotypes after Two Immunizations. The Journal of Immunology. 1993. 150:5627-5665.
Lerner, R.A., et al. “At the crossroads of chemistry and immunology: catalytic antibodies.” Science. May 3, 1991;252 (5006):659-67.
Blackburn, G.M., et al. “The medical potential of catalytic antibodies.” Pure * Appl Chem. 1996;68(11):2009-2016.
Paul, S., et al, “Specific HIV gp120-cleaving antibodies induced by covalently reactive analog of gp120.” J Biol Chem. May 30, 2003;278(22):20429-35. Epub Mar. 28, 2003.
Cunningham, C.C., et al. “A Phase I trial of H-ras antisense oligonucleotide ISIS 2503 administered as a continuous intravenous infusion in patients with advanced carcinoma.” Cancer. Sep. 1, 2001;92(5):1265-71.
Peracchi, A. “Prospects for antiviral ribozymes and deoxyribozymes.” Rev Med Virol. Jan.-Feb. 2004;14(1):47-64.
Chirila T.V., et al. “The use of synthetic polymers for delivery of therapeutic antisense oligodeoxynucleotides.” Biomaterials. Jan. 2002;23(2):321-42.
Crooke, S.T. “Progress in antisense technology.” Annu Rev Med. 2004;55:61-95.
Opalinska, J.B., et al. “Nucleic-acid therapeutics: basic principles and recent applications.” Nat Rev Drug Discov. Jul. 2002; 1(7):503-14.
Branch, A.D. “A good antisense molecule is hard to find.” Trends Biochem Sci. Feb. 1998;23(2):45-50.
Agrawal, S., et al. “Antisense therapeutics: is it as simple as complementary base recognition?” Mol Med Today. Feb. 2000;6(2):72-81.
Copple, B.L., et al. “Reaction between metabolically activated acetaminophen and phosphorothioate oligonucleotides.” Toxicol Appl Pharmacol. Jul. 1995;133(1):53-63.

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