Identifying epitopes of HIV-1 that induce protective antibodies

Nature Reviews Immunology

Volumn 4, Issue 3, 2004, Pages 199-210

  Zolla Pazner, Susan ^a  

^a NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; CD4 ANTIGEN; EPITOPE; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; POLYVALENT VACCINE; UNCLASSIFIED DRUG;

ANTIBODY PRODUCTION; ANTIBODY RESPONSE; CELLULAR IMMUNITY; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMORAL IMMUNITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; REVIEW; VACCINE PRODUCTION; VIRUS ENVELOPE;

EID: 1542615646     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri1307     Document Type: Review

References (133)

1. Robbins, J. B., Schneerson, R. & Szu, S. C. Perspective: hypothesis: serum IgG antibody is sufficient to confer protection against infectious diseases by inactivating the inoculum. J. Infect. Dis. 171, 1387-1398 (1995). A review of the data that support the hypothesis that serum antibodies confer protection against viruses and bacteria by inactivating these pathogens.
2. Hilleman, M. R. Overview of the pathogenesis, prophylaxis and therapeusis of viral hepatitis B, with focus on reduction to practical applications. Vaccine 19, 1837-1848 (2001).
3. Haigwood, N. L. et al. Passive immune globulin therapy in the SIV/ macaque model: early intervention can alter disease profile. Immunol. Lett. 51, 107-114 (1996).
4. Nishimura, Y. et al. Determination of a statistically valid neutralization titer in plasma that confers protection against simian-human immunodeficiency virus challenge following passive transfer of high-titered neutralizing antibodies. J. Virol. 76, 2123-2130 (2002).
5. Letvin, N. L. et al. Vaccine-elicited V3 loop-specific antibodies in rhesus monkeys and control of a simian-human immunodeficiency virus expressing a primary patient human immunodeficiency virus type 1 isolate envelope. J. Virol. 75, 4165-4175 (2001).
6. Emini, E. A. et al. Prevention of HIV-1 infection in chimpanzees by gp120 V3 domain-specific monoclonal antibody. Nature 355, 728-730 (1992).
7. Gauduin, M. C., Safrit, J. T., Weir, R., Fung, M. S. & Koup, R. A. Pre- and postexposure protection against human immunodeficiency virus type 1 infection mediated by a monoclonal antibody. J. Infect. Dis. 171, 1203-1209 (1995).
8. Shibata, R. et al. Neutralizing antibody directed against the HIV-1 envelope glycoprotein can completely block HIV-1/SIV chimeric virus infections of macaque monkeys. Nature Med. 5, 204-210 (1999).
9. Mascola, J. R. et al. Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus by passive infusion of neutralizing antibodies. Nature Med. 6, 207-210 (2000).
10. Scarlatti, G. et al. Mother-to-child transmission of human immunodeficiency virus type 1: correlation with neutralizing antibodies against primary isolates. J. Infect. Dis. 168, 207-210 (1993).
11. Pitt, J. et al. Human immunodeficiency virus (HIV) type 1 antibodies in perinatal HIV-1 infection: association with human HIV-1 transmission, infection, and disease progression. J. Infect. Dis. 182, 1243-1246 (2000).
12. Dimmock, N. J. Neutralization of animal viruses. Curr. Top. Microbiol. Immunol. 183, 1-149 (1993).
13. Burton, D. R. Antibodies, viruses and vaccines. Nature Rev. Immunol. 2, 706-713 (2002).
14. Hansen, J. E. et al. Inhibition of human immunodeficiency virus (HIV) infection in vitro by anticarbohydrate monoclonal antibodies: peripheral glycosylation of HIV envelope glycoprotein gp120 may be a target for virus neutralization. J. Virol. 64, 2833-2840 (1990).
15. Scanlan, C. N. et al. The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of α1→2 mannose residues on the outer face of gp120. J. Virol. 76, 7306-7321 (2002).
16. Hioe, C. E., Bastiani, L., Hildreth, J. E. K. & Zolla-Pazner, S. Role of cellular adhesion molecules in HIV type 1 infection and their impact on virus neutralization. AIDS Res. Hum. Retroviruses 14, 247-254 (1998).
17. + target cells is a major mechanism of T cell line-adapted HIV-1 neutralization. J. Exp. Med. 186, 1287-1298 (1997).
18. Chan, D. C. & Kim, P. S. HIV entry and its inhibition. Cell 93, 681-684 (1998). A review on aspects of the structural changes in HIV glycoprotein gp41 that occur as a consequence of conformational changes induced by interaction of gp120 with CD4 and chemokine receptors. The subsequent formation of the gp41 coiled-coil form leads to fusion between virus and cell membranes.
19. Gorny, M. K. & Zolla-Pazner, S. Recognition of free and complexed peptides representing the prefusogenic and fusogenic forms of HIV-1 gp41 by human monoclonal antibodies. J. Virol. 74, 6186-6192 (2000).
20. Golding, H. et al. Dissection of human immunodeficiency virus type 1 entry with neutralizing antibodies to gp41 fusion intermediates. J. Virol. 76, 6780-6790 (2002).
21. Binley, J. M. et al. Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions. J. Virol. 77, 5678-5684 (2003).
22. Spear, G. T., Takefman, D. M., Sharpe, S., Ghassemi, M. & Zolla-Pazner, S. Antibodies to the HIV-1 V3 loop in serum from infected persons contribute a major proportion of immune effector functions including complement activation, antibody binding, and neutralization. Virology 204, 609-615 (1994).
23. Tyler, D. S. et al. Identification of sites within gp41 that serve as targets for antibody-dependent cellular cytotoxicity by using human monoclonal antibodies. J. Immunol. 145, 3276-3282 (1990).
24. Koup, R. A. et al. Antibody-dependent cell-mediated cytotoxicity directed by a human monoclonal antibody reactive with gp120 of HIV-1. AIDS 5, 1309-1314 (1991).
25. Check, E. AIDS vaccines: back to 'plan A'. Nature 424, 912-914 (2003).
26. Dowbenko, D. et al. Epitope mapping of the human immunodeficiency virus type 1 gp120 with monoclonal antibodies. J. Virol. 62, 4703-4711 (1988).
27. Goudsmit, J. Immunodominant B-cell epitopes of the HIV-1 envelope recognized by infected and immunized hosts. AIDS 2 (Suppl. 1), S41-S45 (1988).
28. Broliden, P. A. et al. Identification of human neutralization-inducing regions of the human immunodeficiency virus type 1 envelope glycoproteins. Proc. Natl Acad. Sci. USA 89, 461-465 (1992).
29. Scala, G. et al. Selection of HIV-specific immunogenic epitopes by screening random peptide libraries with HIV-1-positive sera. J. Immunol. 162, 6155-6161 (1999).
30. Xu, J.-Y., Gorny, M. K., Palker, T., Karwowska, S. & Zolla-Pazner, S. Epitope mapping of two immunodominant domains of gp41, the transmembrane protein of human immunodeficiency virus type 1, using ten human monoclonal antibodies. J. Virol. 65, 4832-4838 (1991).
31. Binley, J. M. et al. Human antibody responses to HIV type 1 glycoprotein 41 cloned in phage display libraries suggest three major epitopes are recognized and give evidence for conserved antibody motifs in antigen binding. AIDS Res. Hum. Retroviruses 12, 911-924 (1996).
32. Trkola, A. et al. Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG. J. Virol. 69, 6609-6617 (1995).
33. Parker, C. E. et al. Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus type 1 for the neutralizing monoclonal antibody. 2F5. J. Virol. 75, 10906-10911 (2001).
34. Zwick, M. B. et al. Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41. J. Virol. 75, 10892-10905 (2001).
35. Sattentau, Q. J., Zolla-Pazner, S. & Poignard, P. Epitope exposure on functional, oligomer c HIV-1 gp41 molecules. Virology 206, 713-717 (1995).
36. Zolla-Pazner, S. et al. Serotyping of primary human immunodeficiency virus type 1 isolates from diverse geographic locations by flow cytometry. J. Virol. 69, 3807-3815 (1995).
37. Nyambi, P. N. et al. Conserved and exposed epitopes on intact, native, primary human immunodeficiency virus type 1 virions of group M. J. Virol. 74, 7096-7107 (2000).
38. He, Y. et al. Peptides trap the human immunodeficiency virus type 1 envelope glycoprotein fusion intermediate at two sites. J. Virol. 77, 1666-1671 (2003).
39. Zwick, M. B. et al. Identification and characterization of a peptide that specifically binds the human, broadly neutralizing anti-human immunodeficiency virus type 1 antibody b12. J. Virol. 75, 6692-6699 (2001).
40. Coeffier, E. et al. Antigenicity and immunogenicity of the HIV-1 gp41 epitope ELDKWA inserted into permissive sites of the MalE protein. Vaccine 19, 684-693 (2000).
41. Muster, T. et al. Cross-neutralizing antibodies against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS. J. Virol. 68, 4031-4034 (1994).
42. Eckhart, L. et al. Immunogenic presentation of a conserved gp41 epitope of human immunodeficiency virus type 1 on recombinant surface antigen of hepatitis B virus. J. Gen. Virol. 77, 2001-2008 (1996).
43. Cotropia, J. et al. A human monoclonal antibody to HIV-1 gp41 with neutralizing activity against diverse laboratory isolates. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 12, 221-232 (1996).
44. Ferrantelli, F. et al. Potent cross-group neutralization of primary HIV isolates with monoclonal antibodies - implications for AIDS vaccine. J. Infect. Dis. 189, 71-74 (2004).
45. Hoe, C. E. et al. Neutralization of HIV-1 primary isolates by polyclonal and monoclonal human antibodies. Int. Immunol. 9, 1281-1290 (1997).
46. Karwowska, S. et al. Production of human monoclonal antibodies specific for conformational and linear non-V3 epitopes of gp120. AIDS Res. Hum. Retroviruses 8, 1099-1106 (1992).
47. Pinter A., Honnen, W. J., Racho, M. E. & Tilley, S. A. A potent, neutralizing human monoclonal antibody against a unique epitope overlapping the CD4-binding site of HIV-1 gp120 that is broadly conserved across North American and African virus isolates. AIDS Res. Hum. Retroviruses 9, 985-996 (1993).
48. D'Souza, M. P. et al. Neutralization of primary HIV-1 isolates by anti-envelope monoclonal antibodies. AIDS 9, 867-874 (1995).
49. Barbas, C. F. et al. Recombinant human Fab fragments neutralize human type 1 immunodeficiency virus in vitro. Proc. Natl Acad. Sci. USA 89, 9339-9343 (1992).
50. Kessler, J. A. et al. Recombinant human monoclonal antibody IgG1b12 neutralizes diverse human Immunodeficiency virus type 1 primary isolates. AIDS Res. Hum. Retroviruses 13, 575-582 (1997).
51. + T cell-proliferative responses to glycoprotein 120. AIDS Res. Hum. Retroviruses 16, 893-905 (2000).
52. Hoe C. E. et al. Inhibition of human immunodeficiency virus type 1 gp120 presentation to CD4 T cells by antibodies specific for the CD4 binding domain of gp120. J. Virol. 75, 10950-10957 (2001).
53. Thali, M. et al. Characterization of conserved HIV-type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol 67, 3978-3988 (1993).
54. Feng, Y., Broder, C. C., Kennedy, P. E. & Berger, E. A. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 272, 872-877 (1996). The first description of a molecule (later identified as CXC-chemokine receptor 4) as a co-receptor that is required for the infection of cells by T-cell-line-adepted strains of HIV-1.
55. Alkhatib, G., Berger, E. A., Murphy, P. M. & Pease, J. E. Determination of HIV-1 coreceptor function on CC chemokine receptor 3. Importance of both extracellular and transmembrane/cytoplasmic regions. J. Biol. Chem. 272, 20420-20426 (1997).
56. Deng, H. et al. Identification of a major co-receptor for primary isolates of HIV-1. Nature 381, 661-666 (1996).
57. Xiang, S. H., Doka, N., Choudhary, R. K., Sodroski, J. & Robinson, J. E. Characterization of CD4-induced epitopes on the HIV type 1 gp120 envelope glycoprotein recognized by neutralizing human monoclonal antibodies. AIDS Res. Hum. Retroviruses 18, 1207-1217 (2002).
58. Moulard, M. et al. Broadly cross-reactive HIV-1-neutralizing human monoclonal Fab selected for binding to gp120-CD4-CCR5 complexes. Proc. Natl Acad. Sci. USA 99, 6913-6918 (2002).
59. Kwong, P. D. et al. Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates, Structure Fold Des. 8, 1329-1339 (2000).
60. Dey B., Del Castillo, C. S. & Berger, E. A. Neutralization of human immunodeficiency virus type 1 by sCD4-17b, a single-chain chimeric protein, based on sequential interaction of gp120 with CD4 and coreceptor. J. Virol. 77, 2859-2865 (2003).
61. Sullivan, N. et al. CD4-induced conformational changes in the human immunodeficiency virus type 1 gp120 glycoprotein: consequences for virus entry and neutralization. J. Virol. 72, 4694-4703 (1998). A description of the nature and functional significance of conformational changes in gp120 that are induced by soluble CD4.
62. Sodroski, J. in Retroviruses of Human AIDS and Related Animal Diseases (eds Vicari, M., Dodet, B. & Girard, M.) 25-27 (Elsevier, Paris, 2002).
63. Leonard, C. K. et al. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J. Biol. Chem. 265, 10373-10382 (1990).
64. Trkola, A. et al. Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. J. Virol. 70, 1100-1108 (1996).
65. Calarese, D. A. et al. Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 300, 2065-2071 (2003).
66. Fung, M. S. et al. Identification and characterization of a neutralization site within the second variable region of HIV-type 1 gp120. J. Virol. 66, 848-856 (1992).
67. Gorny, M. K. et al. Human anti-V2 monoclonal antibody that neutralizes primary but not laboratory isolates of HIV-1. J. Virol. 68, 8312-8320 (1994).
68. Javaherian, K. et al. Principal neutralizing domain of the human immunodeficiency virus type 1 envelope protein. Proc. Natl Acad. Sci. USA 86, 6768-6772 (1989).
69. Putney, S. D. et al. HTLV-III/LAV-neutralizing antibodies to an E. coli-produced fragment of the virus envelope. Science 234, 1392-1395 (1986).
70. Gorny, M. K. et al. Production of site-selected neutralizing human monoclonal antibodies against the third variable domain of the HIV-1 envelope glycoprotein. Proc. Natl Acad. Sci. USA 88, 3238-3242 (1991).
71. Robinson, H. L. New hope for an AIDS vaccine. Nature Rev. Immunol. 2, 239-250 (2002).
72. He, Y. et al. Efficient isolation of novel human monoclonal antibodies with neutralizing activity against HIV-1 from transgenic mice expressing human Ig loci. J. Immunol. 169, 595-605 (2002).
73. Pinter, A., Honnen, W. J., Kayman, S. C., Trochev, O. & Wu, Z. Potent neutralization of primary HIV-1 isolates by antibodies directed against epitopes present in the V1/V2 domain of HIV-1 gp120. Vaccine 16, 1803-1811 (1998).
74. Cao, J. et al. Replication and neutralization of human immunodeficiency virus type 1 lacking the V1 and V2 variable loops of the gp120 envelope glycoprotein. J. Virol. 71, 9808-9812 (1997).
75. Stamatatos, L. & Cheng-Mayer, C. An envelope modification that renders a primary, neutralization-resistant clade B human immunodeficiency virus type 1 isolate highly susceptible to neutralization by sera from other clades. J. Virol. 72, 7840-7845 (1998).
76. Center, R. J., Earl, P. L., Lebowitz, J., Schuck, P. & Moss, B. The human immunodeficiency virus type 1 gp120 V2 domain mediates gp41-independent intersubunit contacts. J. Virol. 74, 4448-4455 (2000).
77. Rizzuto, C. D. et al. A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding. Science 280, 1949-1953 (1998).
78. Wyatt, R. et al. Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding. J. Virol. 69, 5723-5733 (1995).
79. Wyatt, R. et al. Functonal and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions. J. Virol. 67, 4557-4565 (1993).
80. Srivastava, I. K., VanDorsten, K., Vojtech, L., Barnett, S. W. & Stamatatos, L. Changes in the immunogenic properties of soluble gp140 human immunodeficiency virus envelope constructs upon partial deletion of the second hypervariable region. J. Virol. 77, 2310-2320 (2003).
81. Kwong, P. D. et al. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393, 648-659 (1998). Presentation of the crystal structure of a truncated core form of gp120 from a T-cell-line-adapted virus.
82. Goudsmit, J. et al. Human immunodeficiency virus type 1 neutralization epitope with conserved architecture elicits early type-specific antibodies in experimentally infected chimpanzees. Proc. Natl Acad. Sci. USA 85, 4478-4482 (1988).
83. Mascola, J. R. et al. Immunization with envelope subunit vaccine products elicits neutralizng antibodies against laboratory-adapted but not primary isolates of human immunodeficiency virus type 1. J. Infect. Dis. 173, 340-348 (1996).
84. Gorny, M. K. et al. Human monoclonal antibodies to the V3 loop of HIV-1 with intra- and interclade cross-reactivity. J. Immunol. 159, 5114-5122 (1997).
85. Gorny, M. K., Xu, J.-Y., Karwowska, S., Buchbinder, A. & Zolla-Pazner, S. Repertoire of neutralizing human monoclonal antibodies specific for the V3 domaln of HIV-1 gp120. J. Immunol. 150, 635-643 (1993).
86. Gorny, M. K. et al. Human monoclonal antibodies specific for conformation-sensitive epitopes of V3 neutralize HIV-1 primary isolates from various clades. J. Virol. 76, 9035-9045 (2002).
87. Conley, A. J. et al. Neutralization of primary human immunodeficiency virus type 1 isolates by the broadly reactive anti-V3 monoclonal antibody, 447-52D. J. Virol. 68, 6994-7000 (1994).
88. Krachmarov, C. P., Kayman, S. C., Honnen, W. J., Trochev, O. & Pinter, A. V3-specifc polyclonal antibodies affinity purified from sera of infected humans effectively neutralize primary isolates of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses 17, 1737-1748 (2001).
89. Gorny, M. K. et al. The V3 loop is accessible on the surface of most HIV-1 primary isolates and serves as a neutralization epitope. J. Virol. (in the press).
90. Poignard, P. et al. Heterogeneity of envelope molecules expressed on primary human immunodeficiency virus type 1 particles as probed by the binding of neutralizing and non-neutralizing antibodies. J. Virol. 77, 353-365 (2003).
91. Andris, J. S., Johnson, S., Zolla-Pazner, S. & Capra, J. D. Molecular characterization of five human anti-HIV-1 antibody heavy chains reveals extensive somatic mutation typical of an antigen-driven immune response. Proc. Natl Acad. Sci. USA 88, 7783-7787 (1991).
92. Kwong, P. D., Wyatt, R., Sattentau, Q. J., Sodroski, J. & Hendrickson, W. A. Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus. J. Virol. 74, 1961-1972 (2000).
93. Cormier, E. G. & Dragic, T. The crown and stem of the V3 loop play distinct roles in human immunodeficiency virus type 1 envelope glycoprotein interactions with the CCR5 coreceptor. J. Virol 76, 8953-8957 (2002).
94. Suphaphiphat, P., Thitithanyanont, A., Paca-Uccaralertkun, S., Essex, M. & Lee, T. H. Effect of amino acid substitution of the V3 and bridging sheet residues in human immunodeficiency virus type 1 subtype C gp120 on CCR5 utilization. J. Virol. 77, 3832-3837 (2003).
95. Sharon, M. et al. Aternative conformations of HIV-1 V3 loops mimic β hairpins in chemokines, suggesting a mechanism for coreceptor selectivity. Structure 11, 225-236 (2003). This paper describes structural homology between the V3 loop of gp120 and β-hairpin structures in CC- and CXC-chemokines, providing an explanation for how the envelope proteins of R5 and X4 viruses selectively use the receptors for these chemokines to gain entry into cells.
96. Yonezawa, A., Hori, T., Takaori-Kondo, A., Morita, R. & Uchiyama, T. Replacement of the V3 region of gp120 with SDF-1 preserves the infectivity of T-cell line-tropic human immunodeficiency virus type 1. J. Virol. 75, 4258-4267 (2001).
97. VanCott, T. C. et al. Differential role of V3-specific antibodies in neutralization assays involving primary and laboratory-adapted isolates of HIV type 1. AIDS Res. Hum. Retroviruses 11, 1379-1391 (1995).
98. Spenlehauer, C. et al. Study of the V3 loop as a target epitope for antibodies involved in the neutralization of primary isolates versus T-cell-line-adapted strains of human immunodeficiency virus type 1. J. Virol. 72, 9855-9864 (1998).
99. Bou-Habib, D. C. et al. Cryptic nature of envelope V3 region epitopes protects primary monocytotropic human immunodeficiency virus type 1 from antibody neutralization. J. Virol. 68, 6006-6013 (1994).
100. Cavacini, L. & Posner, M. Native HIV-1 virion surface structures: relationships between antibody binding and neutralization or lessons from the viral capture assay. AIDS Res. Hum. Retroviruses (in the press).
101. Stamatatos, L., Zolla-Pazner, S., Gorny, M. K. & Cheng-Mayer, C. Binding of antibodies to virion-associated gp120 molecules of primary-like human immunodeficiency virus type 1 (HIV-1) isolates: effect on HIV-1 infection of macrophages and peripheral blood mononuclear cells. Virology 229, 360-369 (1997).
102. Bhattacharyya, D., Brooks, B. R. & Callahan, L. Positioning of positively charged residues in the V3 loop correlates with HIV type 1 syncytium-inducing phenotype. AIDS Res. Hum. Retroviruses 12, 83-90 (1996).
103. Laurence, J. S., Blanpain, C., De Leener, A., Parmentier, M. & LiWang, P. J. Importance of basic residues and quaternary structure in the function of MIP-1β: CCR5 binding and cell surface sugar interactions. Biochemistry 40, 4990-4999 (2001).
104. Palker, T. J. et al. A conserved region at the COOH terminus of human immunodeficiency virus gp120 envelope protein contains an immunodominant epitope. Proc. Natl Acad. Sci. USA 84, 2479-2483 (1987).
105. Barnett, S. W. et al. The ability of an oligomeric human immunodeficiency virus type 1 (HIV-1) envelope antigen to elicit neutralizing antibodies against primary HIV-1 isolates is improved following partial deletion of the second hypervariable region. J. Virol. 75, 5526-5540 (2001).
106. Pantophlet, R., Wilson, I. A. & Burton, D. R. Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design. J. Virol. 77, 5889-5901 (2003).
107. Kelker, H. C., Schlesinger, D. & Valentine, F. T. Immunogenic and antigenic properties of an HIV-1 gp120-derived multiple chain peptide. J. Immunol. 152, 4139-4148 (1994).
108. Liao, H. X. et al. Induction of antibodies in guinea pigs and rhesus monkeys against the human immunodeficiency virus type 1 envelope: neutralization of nonpathogenic and pathogenic primary isolate simian/human immunodeficiency virus strains. J. Virol. 74, 254-263 (2000).
109. Berger, C. L., Longley, J., Hanlon, D., Girardi, M. & Edelson, R. The clonotypic T cell receptor is a source of tumor-associated antigens in cutaneous T cell lymphoma. Ann. NY Acad. Sci. 941, 106-122 (2001).
110. Keller, P. M. et al. Identification of HIV vaccine candidate peptides by screening random phage epitope libraries. Virology 193, 709-716 (1993).
111. Saphire, E. O. et al. Crystal structure of a neutralizing human IgG against HIV-1: a template for vaccine design. Science 293, 1155-1159 (2001).
112. Saphire, E. O. et al. Contrasting IgG structures reveal extreme asymmetry and flexibility. J. Mol. Biol. 319, 9-18 (2002).
113. Tugarinov, V. et al. NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding. Structure Fold Des. 8, 385-395 (2000).
114. Frangione-Beebe, M. et al. Enhanced immunogenicity of a conformational epitope of human T-lymphotropic virus type 1 using a novel chimeric peptide. Vaccine 19, 1068-1081 (2000).
115. Steward, M. W., Stanley, C. M. & Obeid, O. E. A mimotope from a solid-phase peptide library induces a measles virus-neutralizing and protective antibody response. J. Virol. 69, 7666-7673 (1995).
116. Yu, M. W., Scott, J. K., Fournier, A. & Talbot, P. J. Characterization of murine coronavirus neutralization epitopes with phage-displayed peptides. Virology 271, 182-196 (2000).
117. Grabowska, A. M. et al. Immunisation with phage displaying peptides representing single epitopes of the glycoprotein G can give rise to partial protective immunity to HSV-2. Virology 269, 47-53 (2000).
118. Weber, J. et al. Neutralization serotypes of HIV-1 field isolates are not predicted by genetic subtype. J. Virol. 70, 7827-7832 (1996).
119. Nyambi, P. N. et al. Multivariate analysis of human immunodeficiency virus type 1 neutralization data. J. Virol. 70, 6235-6243 (1996).
120. Moore, J. P. et al. Inter- and intraclade neutralization of human immunodeficiency virus type 1: genetic clades do not correspond to neutralization serotypes but partially correspond to gp120 antigenic serotypes. J. Virol. 70, 427-444 (1996).
121. Mascola, J. R. et al. Human immunodeficiency virus type 1 neutralizing antibody serotyping using serum pools and an infectivity reduction assay AIDS Res. Hum. Retroviruses 12, 1319-1328 (1996).
122. Moore, J. P. et al. A human monoclonal antibody to a complex epitope in the V3 region of gp120 of human immunodeficiency virus type 1 has broad reactivity within and outside clade B. J. Virol. 69, 122-130 (1995).
123. De Groot, A. S. et al. Designing HIV-1 vaccines to reflect viral diversity and the global context of HIV/AIDS. AIDScience 1, 1-24 (2001).
124. Gaschen, B. et al. Diversity considerations in HIV-1 vaccine selection. Science 296, 2354-2360 (2002).
125. Zolla-Pazner, S., Gomy, M. K., Nyambi, P. N., VanCott, T. C. & Nadas, A. Immunotyping of human immunodeficiency virus type 1 (HIV): an approach to immunologic classification of HIV. J. Virol. 73, 4042-4051 (1999).
126. Gallaher, W. R., Bail, J. M., Garry, R. F., Griffin, M. C. & Montelaro, R. C. A general model for the transmembrane proteins of HIV and other retroviruses. AIDS Res. Hum. Retroviruses 5, 431-440 (1989).
127. Cohen, J. HIV. Escape artist par excellence. Science 299, 1505-1508 (2003).
128. Muster, T. et al. A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1. J. Virol. 67, 6642-6647 (1993).
129. Ho, D. D. et al. Conformational epitope on gp120 important in CD4 binding and human immunodeficiency virus type 1 neutralization identified by a human monoclonal antibody. J. Virol. 65, 489-493 (1991).
130. Gomy, M. K. et al. Neutralization of diverse HIV-1 variants by an anti-V3 human monoclonal Entibody. J. Virol. 66, 7538-7542 (1992).
131. Scott, C. F. et al. Human monoclonal antibody that recognizes the V3 region of HIV gp120 and neutralizes the human T-lymphotropic virus type III-MN strain. Proc. Natl Acad. Sci. USA 87, 8597-8601 (1990).
132. Labrijn, A. F. et al. Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1. J. Virol. 77, 10557-10565 (2003).
133. Stanfield, R. L. et al. Structural rational for the broad neutralisation of HIV-1 by human monoclonal antibody 447-52D. Structure 12, 1-20 (2004).