Human Antibodies that Neutralize HIV-1: Identification, Structures, and B Cell Ontogenies

Immunity

Volumn 37, Issue 3, 2012, Pages 412-425

  Kwong, Peter D ^a   Mascola, John R ^a  

^a NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MONOCLONAL ANTIBODY 10E8; MONOCLONAL ANTIBODY 12A12; MONOCLONAL ANTIBODY 12A21; MONOCLONAL ANTIBODY 12A30; MONOCLONAL ANTIBODY 3BNC117; MONOCLONAL ANTIBODY 3BNC60; MONOCLONAL ANTIBODY 3BNC62; MONOCLONAL ANTIBODY 4E10; MONOCLONAL ANTIBODY 8ANC131; MONOCLONAL ANTIBODY 8ANC37; MONOCLONAL ANTIBODY B12; MONOCLONAL ANTIBODY HJ16; MONOCLONAL ANTIBODY NIH45; MONOCLONAL ANTIBODY NIH46; MONOCLONAL ANTIBODY VRC01; MONOCLONAL ANTIBODY VRC02; NEUTRALIZING ANTIBODY; PG16 ANTIBODY; PG9 ANTIBODY; PGT121 ANTIBODY; PGT122 ANTIBODY; PGT123 ANTIBODY; PGT124 ANTIBODY; PGT125 ANTIBODY; PGT126 ANTIBODY; PGT127 ANTIBODY; PGT128 ANTIBODY; PGT129 ANTIBODY; PGT130 ANTIBODY; PGT131 ANTIBODY; UNCLASSIFIED DRUG;

ANTIBODY ISOLATION; ANTIBODY STRUCTURE; B LYMPHOCYTE; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS 1 INFECTION; NONHUMAN; ONTOGENY; PRIORITY JOURNAL; PROTEIN ANALYSIS; REVIEW; SOMATIC MUTATION; VIRUS NEUTRALIZATION; VIRUS STRAIN;

ANTIBODIES, MONOCLONAL; ANTIBODIES, NEUTRALIZING; B-LYMPHOCYTES; HIV ANTIBODIES; HIV ENVELOPE PROTEIN GP120; HIV INFECTIONS; HIV-1; HUMANS; MODELS, MOLECULAR; PROTEIN STRUCTURE, TERTIARY;

EID: 84866495323     PISSN: 10747613     EISSN: 10974180     Source Type: Journal    
DOI: 10.1016/j.immuni.2012.08.012     Document Type: Review

References (120)

1. Alam S.M., McAdams M., Boren D., Rak M., Scearce R.M., Gao F., Camacho Z.T., Gewirth D., Kelsoe G., Chen P., Haynes B.F. The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes. J. Immunol. 2007, 178:4424-4435.
2. Albert J., Abrahamsson B., Nagy K., Aurelius E., Gaines H., Nyström G., Fenyö E.M. Rapid development of isolate-specific neutralizing antibodies after primary HIV-1 infection and consequent emergence of virus variants which resist neutralization by autologous sera. AIDS 1990, 4:107-112.
3. Balazs A.B., Chen J., Hong C.M., Rao D.S., Yang L., Baltimore D. Antibody-based protection against HIV infection by vectored immunoprophylaxis. Nature 2012, 481:81-84.
4. Bell C.H., Pantophlet R., Schiefner A., Cavacini L.A., Stanfield R.L., Burton D.R., Wilson I.A. Structure of antibody F425-B4e8 in complex with a V3 peptide reveals a new binding mode for HIV-1 neutralization. J. Mol. Biol. 2008, 375:969-978.
5. Binley J.M., Wrin T., Korber B., Zwick M.B., Wang M., Chappey C., Stiegler G., Kunert R., Zolla-Pazner S., Katinger H., et al. Comprehensive cross-clade neutralization analysis of a panel of anti-human immunodeficiency virus type 1 monoclonal antibodies. J. Virol. 2004, 78:13232-13252.
6. Binley J.M., Lybarger E.A., Crooks E.T., Seaman M.S., Gray E., Davis K.L., Decker J.M., Wycuff D., Harris L., Hawkins N., et al. Profiling the specificity of neutralizing antibodies in a large panel of plasmas from patients chronically infected with human immunodeficiency virus type 1 subtypes B and C. J. Virol. 2008, 82:11651-11668.
7. Blish C.A., Nedellec R., Mandaliya K., Mosier D.E., Overbaugh J. HIV-1 subtype A envelope variants from early in infection have variable sensitivity to neutralization and to inhibitors of viral entry. AIDS 2007, 21:693-702.
8. Bonsignori M., Hwang K.K., Chen X., Tsao C.Y., Morris L., Gray E., Marshall D.J., Crump J.A., Kapiga S.H., Sam N.E., et al. Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors. J. Virol. 2011, 85:9998-10009.
9. Bonsignori M., Montefiori D.C., Wu X., Chen X., Hwang K.K., Tsao C.Y., Kozink D.M., Parks R.J., Tomaras G.D., Crump J.A., et al. Two distinct broadly neutralizing antibody specificities of different clonal lineages in a single HIV-1-infected donor: implications for vaccine design. J. Virol. 2012, 86:4688-4692.
10. Boyd S.D., Gaëta B.A., Jackson K.J., Fire A.Z., Marshall E.L., Merker J.D., Maniar J.M., Zhang L.N., Sahaf B., Jones C.D., et al. Individual variation in the germline Ig gene repertoire inferred from variable region gene rearrangements. J. Immunol. 2010, 184:6986-6992.
11. Breden F., Lepik C., Longo N.S., Montero M., Lipsky P.E., Scott J.K. Comparison of antibody repertoires produced by HIV-1 infection, other chronic and acute infections, and systemic autoimmune disease. PLoS ONE 2011, 6:e16857.
12. Briney B.S., Willis J.R., Crowe J.E. Human peripheral blood antibodies with long HCDR3s are established primarily at original recombination using a limited subset of germline genes. PLoS ONE 2012, 7:e36750.
13. Briney B.S., Willis J.R., Hicar M.D., Thomas J.W., Crowe J.E. Frequency and genetic characterization of V(DD)J recombinants in the human peripheral blood antibody repertoire. Immunology 2012, 137:56-64.
14. Burton D.R., Pyati J., Koduri R., Sharp S.J., Thornton G.B., Parren P.W., Sawyer L.S., Hendry R.M., Dunlop N., Nara P.L., et al. Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science 1994, 266:1024-1027.
15. Burton D.R., Stanfield R.L., Wilson I.A. Antibody vs. HIV in a clash of evolutionary titans. Proc. Natl. Acad. Sci. USA 2005, 102:14943-14948.
16. Burton D.R., Poignard P., Stanfield R.L., Wilson I.A. Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses. Science 2012, 337:183-186.
17. Buzon V., Natrajan G., Schibli D., Campelo F., Kozlov M.M., Weissenhorn W. Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions. PLoS Pathog. 2010, 6:e1000880.
18. Calarese D.A., Scanlan C.N., Zwick M.B., Deechongkit S., Mimura Y., Kunert R., Zhu P., Wormald M.R., Stanfield R.L., Roux K.H., et al. Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 2003, 300:2065-2071.
19. Cardoso R.M., Zwick M.B., Stanfield R.L., Kunert R., Binley J.M., Katinger H., Burton D.R., Wilson I.A. Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41. Immunity 2005, 22:163-173.
20. Chan D.C., Fass D., Berger J.M., Kim P.S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997, 89:263-273.
21. Chen L., Kwon Y.D., Zhou T., Wu X., O'Dell S., Cavacini L., Hessell A.J., Pancera M., Tang M., Xu L., et al. Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120. Science 2009, 326:1123-1127.
22. Corti D., Langedijk J.P., Hinz A., Seaman M.S., Vanzetta F., Fernandez-Rodriguez B.M., Silacci C., Pinna D., Jarrossay D., Balla-Jhagjhoorsingh S., et al. Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals. PLoS ONE 2010, 5:e8805.
23. Decker J.M., Bibollet-Ruche F., Wei X., Wang S., Levy D.N., Wang W., Delaporte E., Peeters M., Derdeyn C.A., Allen S., et al. Antigenic conservation and immunogenicity of the HIV coreceptor binding site. J. Exp. Med. 2005, 201:1407-1419.
24. Dey B., Svehla K., Xu L., Wycuff D., Zhou T., Voss G., Phogat A., Chakrabarti B.K., Li Y., Shaw G., et al. Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site. PLoS Pathog. 2009, 5:e1000445.
25. Diskin R., Scheid J.F., Marcovecchio P.M., West A.P., Klein F., Gao H., Gnanapragasam P.N., Abadir A., Seaman M.S., Nussenzweig M.C., Bjorkman P.J. Increasing the potency and breadth of an HIV antibody by using structure-based rational design. Science 2011, 334:1289-1293.
26. Doores K.J., Fulton Z., Huber M., Wilson I.A., Burton D.R. Antibody 2G12 recognizes di-mannose equivalently in domain- and nondomain-exchanged forms but only binds the HIV-1 glycan shield if domain exchanged. J. Virol. 2010, 84:10690-10699.
27. Doria-Rose N.A., Klein R.M., Daniels M.G., O'Dell S., Nason M., Lapedes A., Bhattacharya T., Migueles S.A., Wyatt R.T., Korber B.T., et al. Breadth of human immunodeficiency virus-specific neutralizing activity in sera: clustering analysis and association with clinical variables. J. Virol. 2010, 84:1631-1636.
28. Doria-Rose N.A., Georgiev I., O'Dell S., Chuang G.Y., Staupe R.P., McLellan J.S., Gorman J., Pancera M., Bonsignori M., Haynes B.F., et al. A short segment of the HIV-1 gp120 V1/V2 region is a major determinant of resistance to V1/V2 neutralizing antibodies. J. Virol. 2012, 86:8319-8323.
29. Doria-Rose N.A., Louder M.K., Yang Z., O'Dell S., Nason M., Schmidt S.D., McKee K., Seaman M.S., Bailer R.T., Mascola J.R. HIV-1 neutralization coverage is improved by combining monoclonal antibodies that target independent epitopes. J. Virol. 2012, 86:3393-3397.
30. Falkowska E., Ramos A., Feng Y., Zhou T., Moquin S., Walker L.M., Wu X., Seaman M.S., Wrin T., Kwong P.D., et al. PGV04, an HIV-1 gp120 CD4 binding site antibody, is broad and potent in neutralization but does not induce conformational changes characteristic of CD4. J. Virol. 2012, 86:4394-4403.
31. Glanville J., Zhai W., Berka J., Telman D., Huerta G., Mehta G.R., Ni I., Mei L., Sundar P.D., Day G.M., et al. Precise determination of the diversity of a combinatorial antibody library gives insight into the human immunoglobulin repertoire. Proc. Natl. Acad. Sci. USA 2009, 106:20216-20221.
32. Gorny M.K., Stamatatos L., Volsky B., Revesz K., Williams C., Wang X.H., Cohen S., Staudinger R., Zolla-Pazner S. Identification of a new quaternary neutralizing epitope on human immunodeficiency virus type 1 virus particles. J. Virol. 2005, 79:5232-5237.
33. Gray E.S., Moore P.L., Choge I.A., Decker J.M., Bibollet-Ruche F., Li H., Leseka N., Treurnicht F., Mlisana K., Shaw G.M., et al. Neutralizing antibody responses in acute human immunodeficiency virus type 1 subtype C infection. J. Virol. 2007, 81:6187-6196. CAPRISA 002 Study Team.
34. Gray E.S., Madiga M.C., Moore P.L., Mlisana K., Abdool Karim S.S., Binley J.M., Shaw G.M., Mascola J.R., Morris L. Broad neutralization of human immunodeficiency virus type 1 mediated by plasma antibodies against the gp41 membrane proximal external region. J. Virol. 2009, 83:11265-11274.
35. Gray E.S., Madiga M.C., Hermanus T., Moore P.L., Wibmer C.K., Tumba N.L., Werner L., Mlisana K., Sibeko S., Williamson C., et al. The neutralization breadth of HIV-1 develops incrementally over four years and is associated with CD4+ T cell decline and high viral load during acute infection. J. Virol. 2011, 85:4828-4840. and the CAPRISA002 Study Team.
36. Haynes B.F., Fleming J., St Clair E.W., Katinger H., Stiegler G., Kunert R., Robinson J., Scearce R.M., Plonk K., Staats H.F., et al. Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies. Science 2005, 308:1906-1908.
37. Haynes B.F., Kelsoe G., Harrison S.C., Kepler T.B. B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study. Nat. Biotechnol. 2012, 30:423-433.
38. Huang J., Ofek G., Laub L., Louder M.K., Doria-Rose N.A., Longo N.S., Imamichi H., Bailer R.T., Chakrabarti B., Sharma S.K., et al. Broad and potent neutralization of HIV-1 by a gp41-specific human antibody. Nature 2012, Published online September 18, 2012. 10.1038/nature11544.
39. Johnson P.R., Schnepp B.C., Zhang J., Connell M.J., Greene S.M., Yuste E., Desrosiers R.C., Clark K.R. Vector-mediated gene transfer engenders long-lived neutralizing activity and protection against SIV infection in monkeys. Nat. Med. 2009, 15:901-906.
40. Kabat E.A., Wu T.T., Perry H.M., Gottesman K.S., Foeller C. Sequences of Proteins of Immunological Interest 1991, US Department of Health and Human Services, National Institutes of Health, Bethesda, MD. Fifth Edition.
41. Kashyap A.K., Steel J., Oner A.F., Dillon M.A., Swale R.E., Wall K.M., Perry K.J., Faynboym A., Ilhan M., Horowitz M., et al. Combinatorial antibody libraries from survivors of the Turkish H5N1 avian influenza outbreak reveal virus neutralization strategies. Proc. Natl. Acad. Sci. USA 2008, 105:5986-5991.
42. Kim M., Sun Z.Y., Rand K.D., Shi X., Song L., Cheng Y., Fahmy A.F., Majumdar S., Ofek G., Yang Y., et al. Antibody mechanics on a membrane-bound HIV segment essential for GP41-targeted viral neutralization. Nat. Struct. Mol. Biol. 2011, 18:1235-1243.
43. Kong L., Sattentau Q.J. Antigenicity and immunogenicity in HIV-1 antibody-based vaccine design. J. AIDS Clin. Res. 2012, S8:003.
44. Kuhlman B., Dantas G., Ireton G.C., Varani G., Stoddard B.L., Baker D. Design of a novel globular protein fold with atomic-level accuracy. Science 2003, 302:1364-1368.
45. Kwong P.D., Wyatt R., Robinson J., Sweet R.W., Sodroski J., Hendrickson W.A. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 1998, 393:648-659.
46. Kwong P.D., Doyle M.L., Casper D.J., Cicala C., Leavitt S.A., Majeed S., Steenbeke T.D., Venturi M., Chaiken I., Fung M., et al. HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature 2002, 420:678-682.
47. Lerner R.A., Barbas C.F., Kang A.S., Burton D.R. On the use of combinatorial antibody libraries to clone the "fossil record" of an individual's immune response. Proc. Natl. Acad. Sci. USA 1991, 88:9705-9706.
48. Li M., Gao F., Mascola J.R., Stamatatos L., Polonis V.R., Koutsoukos M., Voss G., Goepfert P., Gilbert P., Greene K.M., et al. Human immunodeficiency virus type 1 env clones from acute and early subtype B infections for standardized assessments of vaccine-elicited neutralizing antibodies. J. Virol. 2005, 79:10108-10125.
49. Li Y., Migueles S.A., Welcher B., Svehla K., Phogat A., Louder M.K., Wu X., Shaw G.M., Connors M., Wyatt R.T., Mascola J.R. Broad HIV-1 neutralization mediated by CD4-binding site antibodies. Nat. Med. 2007, 13:1032-1034.
50. Li Y., Svehla K., Louder M.K., Wycuff D., Phogat S., Tang M., Migueles S.A., Wu X., Phogat A., Shaw G.M., et al. Analysis of neutralization specificities in polyclonal sera derived from human immunodeficiency virus type 1-infected individuals. J. Virol. 2009, 83:1045-1059.
51. Liu J., Bartesaghi A., Borgnia M.J., Sapiro G., Subramaniam S. Molecular architecture of native HIV-1 gp120 trimers. Nature 2008, 455:109-113.
52. Mascola J.R., Montefiori D.C. The role of antibodies in HIV vaccines. Annu. Rev. Immunol. 2010, 28:413-444.
53. Mascola J.R., Louwagie J., McCutchan F.E., Fischer C.L., Hegerich P.A., Wagner K.F., Fowler A.K., McNeil J.G., Burke D.S. Two antigenically distinct subtypes of human immunodeficiency virus type 1: viral genotype predicts neutralization serotype. J. Infect. Dis. 1994, 169:48-54.
54. Mascola J.R., Snyder S.W., Weislow O.S., Belay S.M., Belshe R.B., Schwartz D.H., Clements M.L., Dolin R., Graham B.S., Gorse G.J., et al. Immunization with envelope subunit vaccine products elicits neutralizing antibodies against laboratory-adapted but not primary isolates of human immunodeficiency virus type 1. J. Infect. Dis. 1996, 173:340-348. The National Institute of Allergy and Infectious Diseases AIDS Vaccine Evaluation Group.
55. Mascola J.R., D'Souza P., Gilbert P., Hahn B.H., Haigwood N.L., Morris L., Petropoulos C.J., Polonis V.R., Sarzotti M., Montefiori D.C. Recommendations for the design and use of standard virus panels to assess neutralizing antibody responses elicited by candidate human immunodeficiency virus type 1 vaccines. J. Virol. 2005, 79:10103-10107.
56. McCoy L.E., Quigley A.F., Strokappe N.M., Bulmer-Thomas B., Seaman M.S., Mortier D., Rutten L., Chander N., Edwards C.J., Ketteler R., et al. Potent and broad neutralization of HIV-1 by a llama antibody elicited by immunization. J. Exp. Med. 2012, 209:1091-1103.
57. McLellan J.S., Pancera M., Carrico C., Gorman J., Julien J.P., Khayat R., Louder R., Pejchal R., Sastry M., Dai K., et al. Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 2011, 480:336-343.
58. Mikell I., Sather D.N., Kalams S.A., Altfeld M., Alter G., Stamatatos L. Characteristics of the earliest cross-neutralizing antibody response to HIV-1. PLoS Pathog. 2011, 7:e1001251.
59. Moir S., Malaspina A., Fauci A.S. Prospects for an HIV vaccine: leading B cells down the right path. Nat. Struct. Mol. Biol. 2011, 18:1317-1321.
60. Moody M.A., Zhang R., Walter E.B., Woods C.W., Ginsburg G.S., McClain M.T., Denny T.N., Chen X., Munshaw S., Marshall D.J., et al. H3N2 influenza infection elicits more cross-reactive and less clonally expanded anti-hemagglutinin antibodies than influenza vaccination. PLoS ONE 2011, 6:e25797.
61. Moore P.L., Gray E.S., Sheward D., Madiga M., Ranchobe N., Lai Z., Honnen W.J., Nonyane M., Tumba N., Hermanus T., et al. Potent and broad neutralization of HIV-1 subtype C by plasma antibodies targeting a quaternary epitope including residues in the V2 loop. J. Virol. 2011, 85:3128-3141. CAPRISA 002 Study.
62. Morris L., Chen X., Alam M., Tomaras G., Zhang R., Marshall D.J., Chen B., Parks R., Foulger A., Jaeger F., et al. Isolation of a human anti-HIV gp41 membrane proximal region neutralizing antibody by antigen-specific single B cell sorting. PLoS ONE 2011, 6:e23532.
63. Muster T., Guinea R., Trkola A., Purtscher M., Klima A., Steindl F., Palese P., Katinger H. Cross-neutralizing activity against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS. J. Virol. 1994, 68:4031-4034.
64. Myszka D.G., Sweet R.W., Hensley P., Brigham-Burke M., Kwong P.D., Hendrickson W.A., Wyatt R., Sodroski J., Doyle M.L. Energetics of the HIV gp120-CD4 binding reaction. Proc. Natl. Acad. Sci. USA 2000, 97:9026-9031.
65. Ofek G., Tang M., Sambor A., Katinger H., Mascola J.R., Wyatt R., Kwong P.D. Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope. J. Virol. 2004, 78:10724-10737.
66. Ofek G., McKee K., Yang Y., Yang Z.Y., Skinner J., Guenaga F.J., Wyatt R., Zwick M.B., Nabel G.J., Mascola J.R., Kwong P.D. Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region. J. Virol. 2010, 84:2955-2962.
67. Pancera M., Majeed S., Ban Y.E., Chen L., Huang C.C., Kong L., Kwon Y.D., Stuckey J., Zhou T., Robinson J.E., et al. Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility. Proc. Natl. Acad. Sci. USA 2010, 107:1166-1171.
68. Pancera M., McLellan J.S., Wu X., Zhu J., Changela A., Schmidt S.D., Yang Y., Zhou T., Phogat S., Mascola J.R., Kwong P.D. Crystal structure of PG16 and chimeric dissection with somatically related PG9: structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1. J. Virol. 2010, 84:8098-8110.
69. Pantophlet R., Burton D.R. GP120: target for neutralizing HIV-1 antibodies. Annu. Rev. Immunol. 2006, 24:739-769.
70. Pejchal R., Gach J.S., Brunel F.M., Cardoso R.M., Stanfield R.L., Dawson P.E., Burton D.R., Zwick M.B., Wilson I.A. A conformational switch in human immunodeficiency virus gp41 revealed by the structures of overlapping epitopes recognized by neutralizing antibodies. J. Virol. 2009, 83:8451-8462.
71. Pejchal R., Walker L.M., Stanfield R.L., Phogat S.K., Koff W.C., Poignard P., Burton D.R., Wilson I.A. Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1. Proc. Natl. Acad. Sci. USA 2010, 107:11483-11488.
72. Pejchal R., Doores K.J., Walker L.M., Khayat R., Huang P.S., Wang S.K., Stanfield R.L., Julien J.P., Ramos A., Crispin M., et al. A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield. Science 2011, 334:1097-1103.
73. Piantadosi A., Panteleeff D., Blish C.A., Baeten J.M., Jaoko W., McClelland R.S., Overbaugh J. Breadth of neutralizing antibody response to human immunodeficiency virus type 1 is affected by factors early in infection but does not influence disease progression. J. Virol. 2009, 83:10269-10274.
74. Pilgrim A.K., Pantaleo G., Cohen O.J., Fink L.M., Zhou J.Y., Zhou J.T., Bolognesi D.P., Fauci A.S., Montefiori D.C. Neutralizing antibody responses to human immunodeficiency virus type 1 in primary infection and long-term-nonprogressive infection. J. Infect. Dis. 1997, 176:924-932.
75. Prabakaran P., Chen W., Singarayan M.G., Stewart C.C., Streaker E., Feng Y., Dimitrov D.S. Expressed antibody repertoires in human cord blood cells: 454 sequencing and IMGT/HighV-QUEST analysis of germline gene usage, junctional diversity, and somatic mutations. Immunogenetics 2012, 64:337-350.
76. Richman D.D., Wrin T., Little S.J., Petropoulos C.J. Rapid evolution of the neutralizing antibody response to HIV type 1 infection. Proc. Natl. Acad. Sci. USA 2003, 100:4144-4149.
77. Rong R., Li B., Lynch R.M., Haaland R.E., Murphy M.K., Mulenga J., Allen S.A., Pinter A., Shaw G.M., Hunter E., et al. Escape from autologous neutralizing antibodies in acute/early subtype C HIV-1 infection requires multiple pathways. PLoS Pathog. 2009, 5:e1000594.
78. Rothberg J.M., Leamon J.H. The development and impact of 454 sequencing. Nat. Biotechnol. 2008, 26:1117-1124.
79. Sagar M., Wu X., Lee S., Overbaugh J. Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity. J. Virol. 2006, 80:9586-9598.
80. Salzwedel K., Berger E.A. Cooperative subunit interactions within the oligomeric envelope glycoprotein of HIV-1: functional complementation of specific defects in gp120 and gp41. Proc. Natl. Acad. Sci. USA 2000, 97:12794-12799.
81. Sanders R.W., Venturi M., Schiffner L., Kalyanaraman R., Katinger H., Lloyd K.O., Kwong P.D., Moore J.P. The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. J. Virol. 2002, 76:7293-7305.
82. Sather D.N., Armann J., Ching L.K., Mavrantoni A., Sellhorn G., Caldwell Z., Yu X., Wood B., Self S., Kalams S., Stamatatos L. Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection. J. Virol. 2009, 83:757-769.
83. Scanlan C.N., Pantophlet R., Wormald M.R., Ollmann Saphire E., Stanfield R., Wilson I.A., Katinger H., Dwek R.A., Rudd P.M., Burton D.R. The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1->2 mannose residues on the outer face of gp120. J. Virol. 2002, 76:7306-7321.
84. Scheid J.F., Mouquet H., Feldhahn N., Seaman M.S., Velinzon K., Pietzsch J., Ott R.G., Anthony R.M., Zebroski H., Hurley A., et al. Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals. Nature 2009, 458:636-640.
85. Scheid J.F., Mouquet H., Ueberheide B., Diskin R., Klein F., Oliveira T.Y., Pietzsch J., Fenyo D., Abadir A., Velinzon K., et al. Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 2011, 333:1633-1637.
86. Seaman M.S., Janes H., Hawkins N., Grandpre L.E., Devoy C., Giri A., Coffey R.T., Harris L., Wood B., Daniels M.G., et al. Tiered categorization of a diverse panel of HIV-1 Env pseudoviruses for assessment of neutralizing antibodies. J. Virol. 2010, 84:1439-1452.
87. Simek M.D., Rida W., Priddy F.H., Pung P., Carrow E., Laufer D.S., Lehrman J.K., Boaz M., Tarragona-Fiol T., Miiro G., et al. Human immunodeficiency virus type 1 elite neutralizers: individuals with broad and potent neutralizing activity identified by using a high-throughput neutralization assay together with an analytical selection algorithm. J. Virol. 2009, 83:7337-7348.
88. Song L., Sun Z.Y., Coleman K.E., Zwick M.B., Gach J.S., Wang J.H., Reinherz E.L., Wagner G., Kim M. Broadly neutralizing anti-HIV-1 antibodies disrupt a hinge-related function of gp41 at the membrane interface. Proc. Natl. Acad. Sci. USA 2009, 106:9057-9062.
89. Stamatatos L., Morris L., Burton D.R., Mascola J.R. Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine?. Nat. Med. 2009, 15:866-870.
90. Stanfield R.L., Gorny M.K., Zolla-Pazner S., Wilson I.A. Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity. J. Virol. 2006, 80:6093-6105.
91. Starcich B.R., Hahn B.H., Shaw G.M., McNeely P.D., Modrow S., Wolf H., Parks E.S., Parks W.P., Josephs S.F., Gallo R.C., et al. Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV, the retrovirus of AIDS. Cell 1986, 45:637-648.
92. Stiegler G., Kunert R., Purtscher M., Wolbank S., Voglauer R., Steindl F., Katinger H. A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses 2001, 17:1757-1765.
93. Sun Z.Y., Oh K.J., Kim M., Yu J., Brusic V., Song L., Qiao Z., Wang J.H., Wagner G., Reinherz E.L. HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane. Immunity 2008, 28:52-63.
94. Tian C., Luskin G.K., Dischert K.M., Higginbotham J.N., Shepherd B.E., Crowe J.E. Immunodominance of the VH1-46 antibody gene segment in the primary repertoire of human rotavirus-specific B cells is reduced in the memory compartment through somatic mutation of nondominant clones. J. Immunol. 2008, 180:3279-3288.
95. Tiller T., Meffre E., Yurasov S., Tsuiji M., Nussenzweig M.C., Wardemann H. Efficient generation of monoclonal antibodies from single human B cells by single cell RT-PCR and expression vector cloning. J. Immunol. Methods 2008, 329:112-124.
96. Tomaras G.D., Binley J.M., Gray E.S., Crooks E.T., Osawa K., Moore P.L., Tumba N., Tong T., Shen X., Yates N.L., et al. Polyclonal B cell responses to conserved neutralization epitopes in a subset of HIV-1-infected individuals. J. Virol. 2011, 85:11502-11519.
97. Trkola A., Purtscher M., Muster T., Ballaun C., Buchacher A., Sullivan N., Srinivasan K., Sodroski J., Moore J.P., Katinger H. Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. J. Virol. 1996, 70:1100-1108.
98. Verkoczy L., Kelsoe G., Moody M.A., Haynes B.F. Role of immune mechanisms in induction of HIV-1 broadly neutralizing antibodies. Curr. Opin. Immunol. 2011, 23:383-390.
99. Walker L.M., Phogat S.K., Chan-Hui P.Y., Wagner D., Phung P., Goss J.L., Wrin T., Simek M.D., Fling S., Mitcham J.L., et al. Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 2009, 326:285-289. Protocol G Principal Investigators.
100. Walker L.M., Simek M.D., Priddy F., Gach J.S., Wagner D., Zwick M.B., Phogat S.K., Poignard P., Burton D.R. A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals. PLoS Pathog. 2010, 6:e1001028.
101. Walker L.M., Huber M., Doores K.J., Falkowska E., Pejchal R., Julien J.P., Wang S.K., Ramos A., Chan-Hui P.Y., Moyle M., et al. Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 2011, 477:466-470. Protocol G Principal Investigators.
102. Wardemann H., Yurasov S., Schaefer A., Young J.W., Meffre E., Nussenzweig M.C. Predominant autoantibody production by early human B cell precursors. Science 2003, 301:1374-1377.
103. Wei X., Decker J.M., Wang S., Hui H., Kappes J.C., Wu X., Salazar-Gonzalez J.F., Salazar M.G., Kilby J.M., Saag M.S., et al. Antibody neutralization and escape by HIV-1. Nature 2003, 422:307-312.
104. Weissenhorn W., Dessen A., Harrison S.C., Skehel J.J., Wiley D.C. Atomic structure of the ectodomain from HIV-1 gp41. Nature 1997, 387:426-430.
105. West A.P., Diskin R., Nussenzweig M.C., Bjorkman P.J. Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120. Proc. Natl. Acad. Sci. USA 2012, 109:E2083-E2090.
106. Wrammert J., Smith K., Miller J., Langley W.A., Kokko K., Larsen C., Zheng N.Y., Mays I., Garman L., Helms C., et al. Rapid cloning of high-affinity human monoclonal antibodies against influenza virus. Nature 2008, 453:667-671.
107. Wrin T., Loh T.P., Vennari J.C., Schuitemaker H., Nunberg J.H. Adaptation to persistent growth in the H9 cell line renders a primary isolate of human immunodeficiency virus type 1 sensitive to neutralization by vaccine sera. J. Virol. 1995, 69:39-48.
108. Wu X., Parast A.B., Richardson B.A., Nduati R., John-Stewart G., Mbori-Ngacha D., Rainwater S.M., Overbaugh J. Neutralization escape variants of human immunodeficiency virus type 1 are transmitted from mother to infant. J. Virol. 2006, 80:835-844.
109. Wu X., Zhou T., O'Dell S., Wyatt R.T., Kwong P.D., Mascola J.R. Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment. J. Virol. 2009, 83:10892-10907.
110. Wu X., Yang Z.Y., Li Y., Hogerkorp C.M., Schief W.R., Seaman M.S., Zhou T., Schmidt S.D., Wu L., Xu L., et al. Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 2010, 329:856-861.
111. Wu X., Changela A., O'Dell S., Schmidt S.D., Pancera M., Yang Y., Zhang B., Gorny M.K., Phogat S., Robinson J.E., et al. Immunotypes of a quaternary site of HIV-1 vulnerability and their recognition by antibodies. J. Virol. 2011, 85:4578-4585.
112. Wu X., Zhou T., Zhu J., Zhang B., Georgiev I., Wang C., Chen X., Longo N.S., Louder M., McKee K., et al. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 2011, 333:1593-1602. NISC Comparative Sequencing Program.
113. Wyatt R., Sodroski J. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 1998, 280:1884-1888.
114. Wyatt R., Kwong P.D., Desjardins E., Sweet R.W., Robinson J., Hendrickson W.A., Sodroski J.G. The antigenic structure of the HIV gp120 envelope glycoprotein. Nature 1998, 393:705-711.
115. Xiao X., Chen W., Feng Y., Zhu Z., Prabakaran P., Wang Y., Zhang M.Y., Longo N.S., Dimitrov D.S. Germline-like predecessors of broadly neutralizing antibodies lack measurable binding to HIV-1 envelope glycoproteins: implications for evasion of immune responses and design of vaccine immunogens. Biochem. Biophys. Res. Commun. 2009, 390:404-409.
116. Zhou T., Xu L., Dey B., Hessell A.J., Van Ryk D., Xiang S.H., Yang X., Zhang M.Y., Zwick M.B., Arthos J., et al. Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature 2007, 445:732-737.
117. Zhou T., Georgiev I., Wu X., Yang Z.Y., Dai K., Finzi A., Kwon Y.D., Scheid J.F., Shi W., Xu L., et al. Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 2010, 329:811-817.
118. Zhu Z., Qin H.R., Chen W., Zhao Q., Shen X., Schutte R., Wang Y., Ofek G., Streaker E., Prabakaran P., et al. Cross-reactive HIV-1-neutralizing human monoclonal antibodies identified from a patient with 2F5-like antibodies. J. Virol. 2011, 85:11401-11408.
119. Zhu J., O'Dell S., Ofek G., Pancera M., Wu X., Zhang B., Zhang Z., Program N.C.S., Mullikin J.C., Simek M., et al. Somatic populations of PGT135-137 HIV-1-neutralizing antibodies identified by 454 pyrosequencing and bioinformatics. Front. Microbio. 2012, 3:315.
120. Zwick M.B., Labrijn A.F., Wang M., Spenlehauer C., Saphire E.O., Binley J.M., Moore J.P., Stiegler G., Katinger H., Burton D.R., Parren P.W. Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41. J. Virol. 2001, 75:10892-10905.