Methods of eliciting broadly neutralizing antibodies...

Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Amino acid sequence disclosed in whole or in part; or...

Reexamination Certificate

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C424S196110

Reexamination Certificate

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10660206

ABSTRACT:
The present invention is directed to the induction and characterization of a humoral immune response targeting “entry-relevant” gp41 structures. In its broadest aspect, the present invention is directed to methods of raising a neutralizing antibody response to a broad spectrum of HIV strains and isolates. The present invention targets particular molecular conformations or structures that occur at the cell surface of HIV during viral entry into host cells. Such a humoral response can be generated in vivo as a prophylactic measure in individuals to reduce or inhibit the ability of HIV to infect uninfected cells in the individual's body. Such a response can also be employed to raise antibodies against “entry relevant” gp41 structures. These antibodies can be employed for therapeutic uses, and as tools for further illuminating the mechanism of HIV cell entry.

REFERENCES:
patent: 5464933 (1995-11-01), Bolognesi et al.
patent: 5656480 (1997-08-01), Wild et al.
patent: 2001/0047080 (2001-11-01), Root et al.
patent: 2003/0082525 (2003-05-01), Root et al.
patent: WO 00/40616 (2000-07-01), None
patent: WO 03/052122 (2003-06-01), None
The International Search Report dated Feb. 10, 2004.
Gruber, M. et al., “Study of Viral Replication in HIV-I-Infected CEM T-Cell Subclones Which Are Reduced in Their Ability to Form Syncytia,”AIDS Research and Human Retroviruses, vol. 8, No. 6, pp. 1139-1146 (Jun. 1992).
Barin, F. et al., “Virus Envelope Protein of HTLV-III Represents Major Target Antigen for Antibodies in AIDS Patients”,Science, 1094-1096 (May 1985).
Brodeur et al., “Mouse-Human Myeloma Partners for the Production of Heterohybridomas”,Monoclonal Antibody Production Techniques and Applications, Marcel Dekker, Inc., New York, 33:51-63 (1987).
Caffrey et al., “Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41”,EMBO J., 17(16):4572-4584 (Aug. 17, 1998).
Caffrey et al., “Biophysical Characterization of gp41 Aggregates Suggests a Model for the Molecular Mechanism of HIV-associated Neurological Damage and Dementia”,J. Biol. Chem., 275(26):19877-19882 (Jun. 30, 2000).
Calderone, T. et al., “High-level Misincorporation of Lysine for Arginine at AGA Codons in a Fusion Protein Expressed inEscherichia coli”, J. Mol. Biol., 262:407-412 (Oct. 1996).
Cao J. et al., “Effects of Amino Acid Changes in the Extracellular Domain of the Human Immunodeficiency Virus Type I gp41”,Journal of Virology, 67(5):2747-2755 (May 1993).
Chan, D. et al., “Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target”,Proc. Natl. Acad. Sci. USA, 95:15613-15617 (Dec. 1998).
Chan et al., “Core Structure of gp41 from the HIV Envelope Glycoprotein”,Cell, 89:263-273 (Apr. 18, 1997).
Chan et al., “HIV Entry and Its Inhibition”,Cell. 93:681-684 (May 29, 1998).
Chen, C-H., et al., “A Molecular Clasp in the Human Immunodeficiency Virus (HIV) Type 1 TM Protein Determines the anti-HIV Activity of gp41 Derivatives: Implication for Viral Fusion”,J. Virol., 69:3771-3777 (Jun. 1995).
Clackson et al., “Making antibody fragments using phage display libraries”,Nature, 352:624-628 (Aug. 15, 1991).
Connor, R. et al., “Vpr is Required for Efficient Replication of Human Immunodeficiency Virus Type-1 in Mononuclear Phagocytes”,Virology, 206:935-944 (1995).
Cull, M.G., “Biotinylation of Proteins in Vivo and in Vitro Using Small Peptide Tags”,Methods Enzymol:, 326:430-400 (2000).
de Rosny, E. et al., “Peptides Corresponding to the Heptad Repeat Motifs in the Transmembrane Protein (gp41) of Human Immunodeficiency Virus Type 1 Elicit Antibodies to Receptor-Activated Conformations of the Envelope Glycoprotein”,Journal of Virology, 75(18):8859-8863 (Sep. 2001).
Doering, D. et al., “Cysteine Scanning Mutagenesis at 40 of 76 Positions in Villin Headpiece Maps the F-Actin Binding Site and Structural Features of the Domain”,Biochemistry, 35:12677-12685 (1996).
Dong, X. et al., “N- and C-domains of HIV-1 gp41: mutation, structure and functions”,Immunology Letters, 75:215-220 (2001).
Dwyer, J. et al., “The Hydrophobic Pocket Contributes to the Structural Stability of the N-Terminal Coiled Coil of HIV gp41 but Is Not Required for Six-Helix Bundle Formation”,Biochemistry, 42:4945-4953 (2003).
Earl, P. et al., “Epitope Map of Human Immunodeficiency Virus Type 1 gp41 Derived from 47 Monoclonal Antibodies Produced by Immunization with Oligomeric Envelope Protein”,J. Virol., 71:2674-2684 (Apr. 1997).
Furuta, R. et al., “Capture of an early fusion-active conformation of HIV-1 gp41”,Nature Structural Biology, 5(4):276-279 (Apr. 1998).
Goding,Monoclonal Antibodies; Principles and Practice, Academic Press, 59-103 (1983).
Golding et al.,Aids Res. Hum. Retroviruses, 8:1607-1612 (1992).
Golding, H. et al., “LFA-1 Adhesion Molecules Are Not Involved in the Early Stages of HIV-1env-Mediated Cell Membrane Fusion”,Aids Research and Human Retroviruses, 8(9):1593-1598 (Sep. 1992).
Golding, H. et al., “Dissection of Human Immunodeficiency Virus Type 1 Entry with Neutralizing Antibodies to gp41 Fusion Intermediates”,Journal of Virology, 76(13):6780-6790 (Jul. 2002).
He et al., “Peptides Trap the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Fusion Intermediate at Two Sites”,Journal of Virology, 77(3):1666-1671 (Feb. 2003).
Holmes et al., “Bacteriophage Display of Chymotrypsin Inhibitor 2”,Protein Peptide Letters, 3(6):415-422 (1996).
Jiang, S. et al., “HIV-1 inhibition by a peptide”,Nature, 365:113 (Sep. 9, 1993).
Jiang, S. et al., “A Conformation-Specific Monoclonal Antibody Reacting with Fusion-Active gp41 from the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein”,Journal of Virology, 72(12):10213-10217 (Dec. 1998).
Jiang, S. et al., “Peptide and Non-peptide HIV Fusion inhibitors”,Current Pharmaceutical Design, 8:563-580 (2002).
Jonak, Z. et al., “A Human Lymphoid Recombinant Cell Line with Functional Human Immunodeficiency Virus Type 1 Envelope”,AIDS Research Human Retroviruses, 9(1):23-32 (Jan. 1993).
Kemble, G. et al., “Intermonomer Disulfide Bonds Impair the Fusion Activity of Influenza Virus Hemagglutinin”,J. Virol, 66:4940-4950 (Aug. 1992).
Kilby, J. et al., “Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry”,Nature Medicine, 4(11):1302-1307 (Nov. 1998).
Kohler, G. et al., “Continuous cultures of fused cells secreting antibody of predefined specificity”,Nature, 256:495-497 (Aug. 7, 1975).
Kozbor, D. et al., “A Human Hybrid Myeloma for Production of Human Monoclonal Antibodies”,Journal of Immunology, 133(6):3001-3005 (Dec. 1984).
Laue, T. et al., “Analytical Ultracentrifugation in Biochemistry and Polymer Science”, Harding, S.E., Rowe, A.J., and Horton, J. C., Eds., Royal Society for Chemistry, Cambridge, United Kingdom, pp. 90-125 (1992).
Lottenberg, R. et al., “Assay of Coagulation Proteases Using Peptide Chromogenic and Fluorogenic Substrates”,Methods in Enzymology, 80:341-361 (1981).
Louis, J. et al., “Design and Properties of NCCG-gp41, a Chimeric gp41 Molecule with Nanomolar HIV Fusion Inhibitory Activity”,Journal of Biological Chemistry, 276(31):29485-29489 (2001).
Louis, J. et al., “Covalent Trimers of the Internal N-terminal Trimeric Coiled-coil of gp41 and Antibodies Directed against them are Potent Inhibitors of HIV Envelope-mediated Cell Fusion”,Journal of Biological Chemistry, 278(22):20278-20285 (2003).
Lu, M. et al., “A trimeric structural domain of the HIV-1 transmembrane glycoprotein”,Nature Struct. Biol., 2:1075-1082 (Dec. 1995).
Lucic, M. et al., Secretion inEscherichia coliand

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