Source: http://www.patentgenius.com/patent/8551484.html
Timestamp: 2018-10-20 16:39:43
Document Index: 9014169

Matched Legal Cases: ['Application No. 200880010301', 'Application No. 200880010301', 'Application No. 2', 'Application No. 2009', 'Application No. 2', 'Application No. 200432', 'Application No. 2008223561', 'Application No. 200880010301', 'Application No. 200880010301', 'Application No. 08725537', 'Application No. 08725537', 'Application No. 2009', 'Application No. 200880010301']

Human antibodies against hepatitis C virus (HCV) and uses thereof - Patent # 8551484 - PatentGenius
Human antibodies against hepatitis C virus (HCV) and uses thereof
8551484 Human antibodies against hepatitis C virus (HCV) and uses thereof
Inventor: Ambrosino, et al.
Primary Examiner: Humphrey; Louise
U.S. Class: 424/149.1; 424/139.1; 424/141.1; 424/142.1; 424/147.1; 424/159.1; 424/161.1; 530/387.1; 530/387.9; 530/388.1; 530/388.15; 530/388.3; 530/391.1; 530/391.3; 530/391.7
International Class: A61K 39/00; C07K 16/08; C07K 16/00; A61K 39/395; A61K 39/42; C07K 16/10; C12P 21/08
Foreign Patent Documents: 0569537; 0599913; 0947525; 2002-521391; 2002-528140; 2004-524829; 2006-504645; WO 92/03918; WO-92/07001; WO 92/22645; WO 93/01227; WO 94/25585; WO 96/33735; WO-96/33735; WO-98/21338; WO 98/24884; WO-98/24884; WO-99/24466; WO 00/05266; WO-00/05266; WO-00/26418; WO-02/08292; WO-02/055560; WO-02/060954; WO-02/100900; WO-2004005890; WO-2006/041866
Other References: Lesniewski et al. Antibody to Hepatitis C Virus Second Envelope (HCV-E2) Glycoprotein. Journal of Medical Virology 1995, vol. 45, No. 4, pp.415-422. cited by examiner.
International Preliminary Report on Patentability for Application No. PCT/US2008/001922, dated Aug. 26, 2009. cited by applicant.
Office Action for Chinese Patent Application No. 200880010301.5, dated Nov. 2, 2011 (4 pages). cited by applicant.
English Translation of Office Action for Chinese Patent Application No. 200880010301.5, dated Nov. 2, 2011 (5 pages). cited by applicant.
Office Action issued in Canadian Patent Application No. 2,678,888, dated Dec. 19, 2012 (5 pages). cited by applicant.
Official Action issued in Japanese Patent Application No. 2009-550888, dated Dec. 21, 2012 (4 pages). cited by applicant.
Office Action for Canadian Patent Application No. 2,678,888, dated Oct. 17, 2011 (6 pages). cited by applicant.
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Bartosch, Birke et al., "In vitro assay for neutralizing antibody to hepatitis C virus: Evidence for broadly conserved neutralization epitopes," PNAS, vol. 100(24):14199-14204 (2003). cited by applicant.
Flint, Mike et al., "Characterization of Hepatitis C Virus E2 Glycoprotein Interaction with a Putative Cellular Receptor, CD81," Journal of Virology, vol. 73(8):6235-6244 (1999). cited by applicant.
Grollo, L. et al., "Exploiting information inherent in binding sites of virus-specific antibodies: design of an HCV vaccine candidate cross-reactive with multiple genotypes," Antivir. Ther., vol. 11(8):1005-1014 (2006). cited by applicant.
Habersetzer, Francois et al., "Characterization of Human Monoclonal Antibodies Specific to the Hepatitis C Virus Glycoprotein E2 with in Vitro Binding Neutralization Properties," Virology, vol. 249:32-41 (1998). cited by applicant.
Hadlock, Kenneth G. et al., "Human Monoclonal Antibodies That Inhibit Binding of Hepatitis C Virus E2 Protein to CD81 and Recognize Conserved Conformational Epitopes," Journal of Virology, vol. 74(22):10407-10416 (2000). cited by applicant.
Owsianka, Ania et al., "Monoclonal Antibody AP33 Defines a Broadly Neutralizing Epitope on the Hepatitis C Virus E2 Envelope Glycoprotein," Journal of Virology, vol. 79(17):11095-11104 (2005). cited by applicant.
Schofield, Darren J. et al., "Human Monoclonal Antibodies That React With the E2 Glycoprotein of Hepatitis C Virus and Possess Neutralizing Activity," Hepatology, vol. 42:1055-1062 (2005). cited by applicant.
Tarr, Alexander W. et al., "Characterization of the Hepatitis C Virus E2 Epitope Defined by the Broadly Neutralizing Monoclonal Antibody AP33," Hepatology, vol. 43:592-601 (2006). cited by applicant.
Triyatni, Miriam et al., "Structural Features of Envelope Proteins on Hepatitis C Virus-like Particles as Determined by Anti-envelope Monoclonal Antibodies and CD81 Binding," Virology, vol. 298:124-132 (2002). cited by applicant.
Zhou, Yi-Hua et al., "Monoclonal Antibodies to the Hypervariable Region 1 of Hepatitis C Virus Capture Virus and Inhibit Virus Adsorption to Susceptible Cells in Vitro," Virology, vol. 269:276-283 (2000). cited by applicant.
Zucchelli, Silvia et al., "Mimotopes of the Hepatitis C Virus Hypervariable Region 1, but Not the Natural Sequences, Induce Cross-Reactive Antibody Response by Genetic Immunization," Hepatology, vol. 33:692-703 (2001). cited by applicant.
International Search Report and Written Opinion for Application No. PCT/US2008/001922, dated Jul. 30, 2008. cited by applicant.
Reply to Office Action submitted in Chinese Patent Application No. 200880010301.5, filed May 17, 2012 (English Language Translation Provided) (30 pages). cited by applicant.
Second Office Action issued in Chinese Patent Application No. 200880010301.5, dated Aug. 15, 2012 (English Language Translation Provided) (12 pages). cited by applicant.
Allander et al., "Recombinant Human Monoclonal Antibodies Against Different Conformational Epitopes of the E2 Envelope Glycoprotein of Hepatitis C Virus that Inhibit Its Interaction with CD81," Journal of General Virology 81:2451-2459 (2000). citedby applicant.
Bartosch et al., "In Vitro Assay for Neutralizing Antibody to Hepatitis C Virus: Evidence for Broadly Conserved Neutralization Epitopes," Proc. Natl. Acad. Sci. USA 100:14199-14204 (2003). cited by applicant.
Blair et al., "A Novel Human Monoclonal Antibody Directed Against the E2 Glycoprotein of Hepatitis C Virus (HCV) Prevents Infection in Chimpanzees," 44.sup.th Annual Meeting of the European Association for the Study of the Liver (EASL), Copenhagen,Denmark (2009) Poster #1048. cited by applicant.
Broering et al., "Identification and Characterization of Broadly Neutralizing Human Monoclonal Antibodies Directed Against the E2 Envelope Glycoprotein of Hepatitis C Virus," Journal of Virology 83:12473-12482 (2009). cited by applicant.
Bugli et al., "Mapping B-Cell Epitopes of Hepatitis C Virus E2 Glycoprotein Using Human Monoclonal Antibodies from Phage Display Libraries," Journal of Virology 75: 9986-9990 (2001). cited by applicant.
Burioni et al., "Diverging Effects of Human Recombinant Anti-Hepatitis C Virus (HCV) Antibody Fragments Derived from a Single Patient on the Infectivity of a Vesicular Stomatitis Virus/HCV Pseudotype," J. Virol. 76:11775-11779 (2002). cited byapplicant.
Burioni et al., "Dissection of Human Humoral Immune Response Against Hepatitis C Virus E2 Glycoprotein by Repertoire Cloning and Generation of Recombinant Fab Fragments," Hepatology 28:810-814 (1998). cited by applicant.
Choo et al., "Isolation of a cDNA Clone Derived from a Blood-Borne Non-A, Non-B Viral Hepatitis Genome," Science 244:359-362 (1989). cited by applicant.
Davis et al., "A Randomized, Open-Label Study to Evaluate the Safety and Pharmacokinetics of Human Hepatitis C Immune Globulin (Civacir) in Liver Transplant Recipients," Liver Transplantation 11:941-949 (2005). cited by applicant.
Farci et al., "Prevention of Hepatitis C Virus Infection in Chimpanzees by Hyperimmune Serum Against the Hypervariable Region 1 of the Envelope 2 Protein," Proc. Natl. Acad. Sci. USA 93:15394-15399 (1996). cited by applicant.
Farci et al., "Prevention of Hepatitis C Virus Infection in Chimpanzees After Antibody-Mediated In Vitro Neutralization," Proc. Natl. Acad. Sci. USA 91:7792-7796 (1994). cited by applicant.
Fishwild et al., "High-Avidity Human IgG kappa Monoclonal Antibodies from a Novel Strain of Minilocus Transgenic Mice," Nature Biotechnology 14:845-851 (1996). cited by applicant.
Flint et al., "Characterization of Hepatitis C Virus E2 Glycoprotein Interaction with a Putative Cellular Receptor, CD81," Journal of Virology 73:6235-6244 (1999). cited by applicant.
Gal-Tanamy et al., "In Vitro Selection of a Neutralization-Resistant Hepatitis C Virus Escape Mutant," PNAS 105:19450-19455 (2008). cited by applicant.
Grollo et al., "Exploiting Information Inherent in Binding Sites of Virus-Specific Antibodies: Design of an HCV Vaccine Candidate Cross-Reactive with Multiple Genotypes," Antiviral Therapy 11:1005-1014 (2006). cited by applicant.
Guha et al., "Cell Culture Models and Animal Models of Viral Hepatitis. Part II: Hepatitis C," Lab Animal 34:39-47 (2005). cited by applicant.
Habersetzer et al., "Characterization of Human Monoclonal Antibodies Specific to the Hepatitis C Virus Glycoprotein E2 With In Vitro Binding Neutralization Properties," Virology 249:32-41 (1998). cited by applicant.
Hadlock et al., "Human Monoclonal Antibodies that Inhibit Binding of Hepatitis C Virus E2 Protein to CD81 and Recognize Conserved Conformational Epitopes," Journal of Virology 74:10407-10416 (2000). cited by applicant.
Johansson et al., "Human Combinatorial Libraries Yield Rare Antibodies that Broadly Neutralize Hepatitis C Virus," PNAS 104:16269-16274 (2007). cited by applicant.
Krawczynski et al., "Effect of Immune Globulin on the Prevention of Experimental Hepatitis C Virus Infection," The Journal of Infectious Diseases 173:822-828 (1996). cited by applicant.
Krawczynski et al., "Experimental Immune Treatment of HCV Infection--Passive Transfer of Anti-HCV in Chimpanzees," XI International Congress of Virology Meeting in Sydney, Australia, Aug. 9-13, 1999 (Abstract). cited by applicant.
Lanford et al., "The Chimpanzee Model of Hepatitis C Virus Infections," ILAR J. 42:117-126 (2001). cited by applicant.
Law et al., "Broadly Neutralizing Antibodies Protect Against Hepatitis C Virus Quasispecies Challenge," Nature 1-3 (Supplementary Figures) (2007). cited by applicant.
Owsianka et al., "Monoclonal Antibody AP33 Defines a Broadly Neutralizing Epitope on the Hepatitis C Virus E2 Envelope Glycoprotein," Journal of Virology 79:11095-11104 (2005). cited by applicant.
Owsianka et al., "Broadly Neutralizing Human Monoclonal Antibodies to the Hepatitis C Virus E2 Glycoprotein," Journal of General Virology 89:653-659 (2008). cited by applicant.
Perotti et al., "Identification of a Broadly Cross-Reacting and Neutralizing Human Monoclonal Antibody Directed Against the Hepatitis C Virus E2 Protein," Journal of Virology 82:1047-1052 (2008). cited by applicant.
Schiano et al., "Monoclonal Antibody HCV-AB.sup.XTL68 in Patients Undergoing Liver Transplantation for HCV: Results of a Phase 2 Randomized Study," Liver Transplantation 12:1381-1389 (2006). cited by applicant.
Schofield et al., "Human Monoclonal Antibodies that React with the E2 Glycoprotein of Hepatitis C Virus and Possess Neutralizing Activity," Hepatology 42:1055-1062 (2005). cited by applicant.
Simmonds, "Variability of Hepatitis C Virus," Hepatology 21:570-583 (1995). cited by applicant.
Tarr et al., "Determination of the Human Antibody Response to the Epitope Defined by the Hepatitis C Virus-Neutralizing Monoclonal Antibody AP33," J. Gen. Virol. 88:2991-3001 (2007). cited by applicant.
Tarr et al., "Characterization of the Hepatitis C Virus E2 Epitope Defined by the Broadly Neutralizing Monoclonal Antibody AP33," Hepatology 43:592-601 (2006). cited by applicant.
Triyatni et al., "Structural Features of Envelope Proteins on Hepatitis C Virus-Like Particles as Determined by Anti-Envelope Monoclonal Antibodies and CD81 Binding," Virology 298:124-132 (2002). cited by applicant.
Willems et al., "Anti-HCV Human Immunoglobulins for the Prevention of Graft Infection in HCV-Related Liver Transplantation, A Pilot Study," Abstract #96 (2002). cited by applicant.
Yu et al., "Neutralizing Antibodies to Hepatitis C Virus (HCV) in Immune Globulins Derived from Anti-HCV-Positive Plasma," PNAS 101:7705-7710 (2004). cited by applicant.
Zhou et al., "Monoclonal Antibodies to the Hypervariable Region 1 of Hepatitis C Virus Capture Virus and Inhibit Virus Adsorption to Susceptible Cells In Vitro," Virology 269:276-283 (2000). cited by applicant.
Zucchelli et al., "Mimotopes of the Hepatitis C Virus Hypervariable Region 1, but Not the Natural Sequences, Induce Cross-Reactive Antibody Response by Genetic Immunization," Hepatology 33:692-703 (2001). cited by applicant.
International Preliminary Report on Patentability (PCT/US2008/001922) issued Aug. 26, 2009. cited by applicant.
International Search Report (PCT/US2008/001922) mailed Jul. 30, 2008. cited by applicant.
Written Opinion of the International Searching Authority (PCT/US2008/001922) dated Aug. 21, 2009. cited by applicant.
First European Examination Report (Application No. 08725537.8) dated Nov. 24, 2009. cited by applicant.
Second European Examination Report (Application No. 08725537.8) dated Nov. 25, 2010. cited by applicant.
English Language Translation of Notice of Reasons for Rejection issued in Japanese Patent Application No. 2009-550888, dated Dec. 17, 2012, mailed Dec. 21, 2012 (5 pages). cited by applicant.
Decision of Final Rejection of the Application issued in Chinese Patent Application No. 200880010301.5, dated Mar. 8, 2013 (English Language Translation Provided) (12 pages). cited by applicant.
Abstract: Isolated human monoclonal antibodies which bind to hepatitis C virus (HCV), and related antibody-based compositions and molecules, are disclosed. The human antibodies can be produced in a transfectoma or in a non-human transgenic animal, e.g., a transgenic mouse, capable of producing multiple isotypes of human monoclonal antibodies by undergoing V-D-J recombination and isotype switching. Also disclosed are pharmaceutical compositions comprising the human antibodies, non-human transgenic animals, and hybridomas which produce the human antibodies, and therapeutic and diagnostic methods for using the human antibodies.
1. An isolated human monoclonal antibody, or antigen binding portion thereof, wherein the antibody, or antigen binding portion thereof comprises heavy and light chainvariable regions comprising the sequences of SEQ ID NOs:1 and 2.
2. An isolated human monoclonal antibody, or antigen binding portion thereof, comprising a heavy chain variable region comprising the sequence of SEQ ID NO:1, wherein the antibody or antigen binding portion thereof binds to a nonconformational(linear) epitope on the HCV E2 protein.
3. An isolated human monoclonal antibody, or antigen binding portion thereof, comprising a light chain variable region comprising the sequence of SEQ ID NO:2, wherein the antibody or antigen binding portion thereof binds to a nonconformational(linear) epitope on the HCV E2 protein.
4. An isolated human monoclonal antibody, or antigen binding portion thereof, wherein the antibody, or antigen binding portion thereof comprises a heavy chain variable region CDR3 sequence comprising the sequence of SEQ ID NO:9, a light chainvariable region CDR3 sequence comprising the sequence of SEQ ID NO:18, a heavy chain variable region CDR2 sequence comprising the sequence of SEQ ID NO:8, a light chain variable region CDR2 sequence comprising the sequence of SEQ ID NO:17, a heavy chainvariable region CDR1 sequence comprising the sequence of SEQ ID NO:7, and a light chain variable region CDR1 sequence comprising the sequence of SEQ ID NO:16.
5. The isolated antibody o claim 4, wherein the antibody is a full-length antibody.
6. The isolated antibody, or antigen binding portion thereof of claim 4, wherein the antibody or antigen binding portion is selected from the group consisting of an antibody comprising an Fc domain, a single-chain antibody, and a Fab fragment.
7. The isolated antibody or antigen binding portion of claim 4, wherein the antibody or antigen binding portion inhibits binding of hepatitis C virus (HCV) to mammalian cells.
8. The isolated antibody or antigen binding portion of claim 4, wherein the antibody or antigen binding portion inhibits binding of an HCV E2 protein to mammalian cells.
9. The isolated antibody or antigen binding portion of claim 4, which binds to a non-conformational (linear) epitope on the HCV E2 protein and inhibits the ability of the virus to infect cells.
10. The isolated antibody or antigen binding portion of claim 4, wherein the antibody or antigen binding portion neutralizes HCV in an HCV pseudovirus neutralization assay.
11. The isolated antibody or antigen binding portion of claim 4, wherein the antibody inhibits HCV infection of a cell.
12. The isolated antibody or antigen binding portion of claim 4, wherein the antibody binds to two or more HCV genotypes of an HCV E2 protein or fragment thereof.
13. The isolated antibody or antigen binding portion of claim 4, wherein the antibody binds an HCV E2 protein from an HCV virus having a genotype selected from the group consisting of 1a, 1b, 2b, 3a, 4a, 5, 5a, 6a, 6g, 6k, and any combinationthereof.
14. The isolated antibody or antigen binding portion of claim 4, wherein the antibody or antigen binding portion binds an epitope between amino acid residues 412-464, 412-423, or 413-420 of the E2 protein of SEQ ID NO:93.
15. The isolated antibody or antigen binding portion of claim 4, wherein the antibody or antigen binding portion thereof specifically binds to an HCV E2 protein, or fragment thereof, with a K.sub.D of at least about 1.times.10.sup.-7 M,1.times.10.sup.-8 M, 1.times.10.sup.-9 M, 1.times.10.sup.-10 M, 1.times.10.sup.-11 M, 1.times.10.sup.-12 M or better.
16. The isolated antibody or antigen binding portion of claim 4, further comprising a label or a therapeutic agent.
17. A composition comprising the isolated antibody or antigen binding portion of claim 4 in a pharmaceutically acceptable carrier.
18. A kit comprising the isolated antibody or antigen binding portion of claim 4 and instruction for use of said antibody or antigen binding portion.
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