Virus coat protein/receptor chimeras and methods of use

Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Virus or component thereof

Reexamination Certificate

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C424S001210

Reexamination Certificate

active

09684026

ABSTRACT:
The invention relates to chimeric molecules comprising a virus coat sequence and a receptor sequence that can interact with each other to form a complex that is capable of binding a co-receptor. Such chimeric molecules therefore exhibit functional properties characteristic of a receptor-coat protein complex and are useful as agents that inhibit virus infection of cells due to occupancy of co-receptor present on the cell, for example. In particular aspects, the chimeric polypeptide includes an immunodeficiency virus envelope polypeptide, such as that of HIV, SIV, FIV, FeLV, FPV and herpes virus. Receptor sequences suitable for use in a chimeric polypeptide include, for example, CCR5 and CXCR4 sequences.

REFERENCES:
patent: 5420030 (1995-05-01), Reitz, Jr. et al.
patent: 5518723 (1996-05-01), DeVico et al.
patent: 5576000 (1996-11-01), Reitz, Jr. et al.
patent: 5689313 (1997-11-01), Sotheran
patent: 5770572 (1998-06-01), Gershoni
patent: 5843454 (1998-12-01), DeVico et al.
patent: 5871913 (1999-02-01), Maddon et al.
patent: 5925741 (1999-07-01), Gershoni
patent: 6020468 (2000-02-01), Gershoni
patent: 6143876 (2000-11-01), Gershoni
patent: 6165722 (2000-12-01), Gershoni et al.
patent: 6329202 (2001-12-01), Gershoni
patent: 0 325 262 (1989-07-01), None
patent: WO92/05799 (1992-04-01), None
patent: WO93/15750 (1993-08-01), None
patent: WO94/26305 (1994-11-01), None
patent: WO98/47916 (1998-10-01), None
Partidos et al. The influence of orientation and number of copies of T and B cell epitopes on the specificity and affinity of anitbodies induced by chimeric peptides. European Hournal of Immunology (1992) vol. 22, pp. 2675-2680.
Zeng et al. Assembly of synthetic peptide vaccine by chemoselective ligation of epitopes: influence of different chemical linkages and epitope orientations on biological activity. Vaccine (2001) vol. 19, pp. 3843-3852.
Moore G.J. Designing peptide mimetics. Trends in Protein Science. vol. 15 (1994) pp. 124-129.
Chackerian et al. Induction of autoantibodies to mouse CCR5 with recombinant papilomavirus particles. Proceeding of the National Academy of Sciences (Mar. 1999) vol. 96, 2373-2378.
Baker et al., Protein structure predication and structural gemonics. Science (2001) vol. 294, No. 5540, pp. 93-96.
Riffkin et al. A single amino-acid change between the antigenically different extracellular serine protease V2 and B2 from Dichelobacter nodous. Gene (1955) vol. 167, pp. 279-283.
Ngo et al, in The Protein Folding Problem and Tertiary Structure Prediction, 1994, Edited by Merz et al., (ed.), Birkhauser, Boston, MA, pp. 433 and 492-495.
Burgess et al. Possible dissociation of the heparin-binding and mitogenic activities of heparin binding growth factor-1 from its receptor-binding activities by site directed mutagenesis of a single lysine residue. Journal of Cell Biology. (1990) vol. 111, 2129-2138.
Lazar et al. Transforming growth factor alpha; mutations of aspartic acid 47 and leucine 48 results in different biological activities. Molecular and Cellular Biology (1988) vol. 8, No. 3, p. 1247-1252.
Tao et al. Studies of aglycosylated chimeric mouse-human IgG. The Journal of Immunology (1989) vol. 143 No. 8, p. 2595-2601.
Abaza et al. Effects of amino acid substitutions outside an antigenic site on protein binding to monoclonal antibodies of predetermined specificity obtained by peptide immunization. Journal of Protein Chemistry (1992) vol. 11, No. 5, pp. 433-444.
Nuss et al. Defining the requirements for an antibody epitope on influenza virus neuraminidase: How Tolarent are protein epitopes? Journal of Molecular Biology (1994) vol. 235, pp. 747-759.
di Marzo et al. Loss of a neutralizing epitope by a spontaneous point mutation in the V3 loop of HIV-1 isolated from an infected laboratory worker. Journal of Biological Chemistry (Dec. 1993) vol. 268, No. 34, pp. 25894-25901.
Attwood, T. The babel of bioinformatics. Science (2000) vol. 290, No. 5491, p. 471-473.
Attwood et al. Science, vol. 290, p. 1-6.
Baker et al. Science , vol. 294, p. 1-7.
R.A. Kaup et al., “Shutting down HIV,”, Nature, 370; 416 (1994).
R.A. Kaup et al., “Temporal association of cellular immune responses with the initial control of viremia in primary human immunodeficiency virus type 1 syndrome,” Journal of Virol, 68; 4650-4655 (1994).
E.A. Emini, et al., “Prevention of HIB-1 infection in chimpanzees by gp120 V3 domain-specific monoclonal antibody,” Nature, 355; 728-739 (1992).
R. Shibata et al., “Neutralizing antibody directed against the HIV-1 envelope glycoprotein can completely block HIV-1/SIV chimeric virus infections of macaque monkeys,” Nature Medicine, 5; 204-210 (1999).
M.C. Gauduin et al., “Passive immunization with a human monoclonal antibody protects hu-PBL-SCID mice against challenge by primary isolates of HIV-1,” Nature Medicine, 3; 1389-1393 (1997).
P.W. Parren et al., “Protection against HIV-1 infection in hu-PBL-SCID mice by passive immunization with a neutralizing human monoclonal antibody against the gp120 CD4-binding site,” AIDS, 9; F1-F6 (1995).
J.W. Eichberg et al., “Prevention of HIV infection by passive immunization with HIVIG or CD4-IgG,” AIDS Res. Hum. Retroviruses, 8; 1515 (1992).
R.H. Ward et al, “Prevention of HIV-1 IIIB infection in chimpanzees by CD4 immunoadhesin,” Nature, 352; 434-436 (1991).
J.L. Heeney et al., “Beta-chemokines and neutralizing antibody titers correlate with sterilizing immunity generated in HIV-1 vaccinated macaques,” Proc. Nat. Acad. Sci. U.S.A., 95; 10803-10808 (1998).
Mascola et al., “Protection of macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies,” Jour. Of Virol., 73; 4009-4018 (1999).
J.P. Moore et al., “HIV-1 neutralization: the consequences of viral adaptation to growth on transformed T cells,” AIDS, 9; S117-S136 (1995).
Q.J. Sattentau, “Neutralization of HIV01 by antibody,” Curr. Opin. Immun., 8; 540-545 (1996).
R. Wyatt et al., “The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens,” Science, 280; 1884-1888 (1998).
Claudio Vita. “Rational engineering of a miniprotein that reproduces the core of the CD4 site interacting with HIV-1 envelope glycoprotein,” PNAS, Nov. 9, 1999, vol. 96, No. 23, patent. 13091-13096.
Rizzuto, Carlo D., et al. “A Conserved HIV gp120 Glycoprotein Structure Involved in Chemokine Receptor Binding.” Science, vol. 280, (1998), pp. 1949-1953.
Sells, Mary Ann, et al. “Epitope-tag vectors for eukaryotic protein production.” Gene, vol. 152, (1995), pp. 187-189.
Sullivan, Nancy, et al. “CD4-Induced Conformational Changes in the Human Immunodeficiency Virus Type 1 gp120 Glycoprotein: Consequences for Virus Entry and Neutralization.” Journal of Virology, (1998), pp. 4694-4703.
DeVico et al, 1996 “Covalently Crosslinked Complexes of Human Immunodeficiency Virus Type 1 (HIV-1) gp120 and CD4 Receptor Elicit a Neutralizing Immune Response That Includes Antibodies Selective for Primary Virus Isolates”Virology218, 258-263.
DeVico, et al., 1995, “Monoclonal Antibodies Raised against Covalently Crosslinked Complexes of Human Immunodeficiency Virus Type 1 gp120 and CD4 Receptors Identify a Novel Complex-Dependent Epitope on gp120”Virology211, 583-588.

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