[1]
Zhu P, Chertova E, Bess J Jr, et al. Electron tomography analysis of envelope glycoprotein trimers on HIV and simian immunodeficiency virus virions. Proc Natl Acad Sci USA 2003; 100: 15812-7.
[2]
Behrens AJ, Vasiljevic S, Pritchard LK, et al. Composition and antigenic effects of individual glycan sites of a trimeric HIV-1 envelope glycoprotein. Cell reports 2016; 14: 2695-706.
[3]
Moore PL, Crooks ET, Porter L, et al. Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1. J Virol 2006; 80: 2515-28.
[4]
Tomaras GD, Yates NL, Liu P, et al. Initial B-cell responses to transmitted human immunodeficiency virus type 1: virion-binding immunoglobulin M (IgM) and IgG antibodies followed by plasma anti-gp41 antibodies with ineffective control of initial viremia. J Virol 2008; 82: 12449-63.
[5]
Davis KL, Bibollet-Ruche F, Li H, et al. Human immunodeficiency virus type 2 (HIV-2)/HIV-1 envelope chimeras detect high titers of broadly reactive HIV-1 V3-specific antibodies in human plasma. J Virol 2009; 83: 1240-59.
[6]
Davis KL, Gray ES, Moore PL, et al. High titer HIV-1 V3-specific antibodies with broad reactivity but low neutralizing potency in acute infection and following vaccination. Virology 2009; 387: 414-26.
[7]
Gray ES, Moore PL, Choge IA, et al. Neutralizing antibody responses in acute human immunodeficiency virus type 1 subtype C infection. J Virol 2007; 81: 6187-96.
[8]
Li B, Decker JM, Johnson RW, et al. Evidence for potent autologous neutralizing antibody titers and compact envelopes in early infection with subtype C human immunodeficiency virus type 1. J Virol 2006; 80: 5211-8.
[9]
Frost SD, Wrin T, Smith DM, et al. Neutralizing antibody responses drive the evolution of human immunodeficiency virus type 1 envelope during recent HIV infection. Proc Natl Acad Sci USA 2005; 102: 18514-9.
[10]
Richman DD, Wrin T, Little SJ, Petropoulos CJ. Rapid evolution of the neutralizing antibody response to HIV type 1 infection. Proc Natl Acad Sci USA 2003; 100: 4144-9.
[11]
Wei X, Decker JM, Wang S, et al. Antibody neutralization and escape by HIV-1. Nature 2003; 422: 307-12.
[12]
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: 9586-98.
[13]
Moore PL, Gray ES, Choge IA, et al. The C3-V4 region is a major target of autologous neutralizing antibodies in human immunodeficiency virus type 1 subtype C infection. J Virol 2008; 82: 1860-9.
[14]
Bar K, Keele BF, Decker JM, et al. editors. Neutralizing antibody recognition of V1 in early HIV-1 infection. 16th Conference on retroviruses and opportunistic infections; 2009; 16th Conference on retroviruses and opportunistic infections. Palais des Congres do Montreal, Montreal, Canada
[15]
Moore PL, Ranchobe N, Lambson BE, et al. Limited neutralizing antibody specificities drive neutralization escape in early HIV-1 subtype C infection. PLoS Pathog 2009; 5: e1000598.
[16]
Rong R, Gnanakaran S, Decker JM, et al. Unique mutational patterns in the envelope alpha2 amphipathic helix and acquisition of length in gp120 hyper-variable domains are associated with resistance to autologous neutralization of subtype C human immunodeficiency virus type 1. J Virol 2007; 81: 5658-68.
[17]
Moore PL, Gray ES, Wibmer CK, et al. Evolution of an HIV glycan-dependent broadly neutralizing antibody epitope through immune escape. Nat Med 2012; 18: 1688-92.
[18]
Bar KJ, Tsao CY, Iyer SS, et al. Early low-titer neutralizing antibodies impede HIV-1 replication and select for virus escape. PLoS Pathog 2012; 8: e1002721.
[19]
Moore PL, Ranchobe N, Lambson BE, et al. Limited neutralizing antibody specificities drive neutralization escape in early HIV-1 subtype C infection. PLoS Pathog 2009; 5: e1000598.
[20]
Seaman MS, Janes H, Hawkins N, et al. Tiered categorization of a diverse panel of HIV-1 Env pseudoviruses for assessment of neutralizing antibodies. J Virol 2010; 84: 1439-52.
[21]
Rademeyer C, Korber B, Seaman MS, et al. Features of recently transmitted HIV-1 clade C viruses that impact antibody recognition: Implications for active and passive immunization. PLoS Pathog 2016; 12: e1005742.
[22]
Moody MA, Gao F, Gurley TC, et al. Strain-Specific V3 and CD4 Binding Site Autologous HIV-1 Neutralizing Antibodies Select Neutralization-Resistant Viruses. Cell host & microbe 2015; 18: 354-62.
[23]
Sanders RW, van Gils MJ, Derking R, et al. HIV-1 VACCINES. HIV-1 neutralizing antibodies induced by native-like envelope trimers. Science 2015; 349: aac4223.
[24]
de Taeye SW, Ozorowski G, Torrents de la Pena A, et al. Immunogenicity of Stabilized HIV-1 Envelope Trimers with Reduced Exposure of Non-neutralizing Epitopes. Cell 2015; 163: 1702-15.
[25]
Hraber P, Seaman MS, Bailer RT, Mascola JR, Montefiori DC, Korber BT. Prevalence of broadly neutralizing antibody responses during chronic HIV-1 infection. AIDS 2014; 28: 163-9.
[26]
Gray ES, Madiga MC, Hermanus T, et al. HIV-1 neutralization breadth develops incrementally over 4 years and is associated with CD4+ T cell decline and high viral load during acute infection. J Virol 2011; 85: 4828-40.
[27]
Landais E, Huang X, Havenar-Daughton C, et al. Broadly neutralizing antibody responses in a large longitudinal sub-saharan HIV primary infection cohort. PLoS Pathog 2016; 12: e1005369.
[28]
Piantadosi A, Panteleeff D, Blish CA, et al. 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: 10269-74.
[29]
Sather DN, Armann J, Ching LK, et al. Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection. J Virol 2009; 83: 757-69.
[30]
Muenchhoff M, Adland E, Karimanzira O, et al. Nonprogressing HIV-infected children share fundamental immunological features of nonpathogenic SIV infection. Sci Transl Med 2016; 8: 358ra125.
[31]
Goo L, Chohan V, Nduati R, Overbaugh J. Early development of broadly neutralizing antibodies in HIV-1-infected infants. Nat Med 2014; 20: 655-8.
[32]
Simonich CA, Williams KL, Verkerke HP, et al. HIV-1 Neutralizing Antibodies with Limited Hypermutation from an Infant. Cell 2016; 166: 77-87.
[33]
Wibmer CK, Bhiman JN, Gray ES, et al. Viral escape from HIV-1 neutralizing antibodies drives increased plasma neutralization breadth through sequential recognition of multiple epitopes and immunotypes. PLoS Pathog 2013; 9: e1003738.
[34]
Moore PL, Sheward D, Nonyane M, et al. Multiple pathways of escape from HIV broadly cross-neutralizing V2-dependent antibodies. J Virol 2013; 87: 4882-94.
[35]
Wu X, Wang C, O’Dell S, et al. Selection pressure on HIV-1 envelope by broadly neutralizing antibodies to the conserved CD4-binding site. J Virol 2012; 86: 5844-56.
[36]
van Gils MJ, Bunnik EM, Burger JA, et al. Rapid escape from preserved cross-reactive neutralizing humoral immunity without loss of viral fitness in HIV-1-infected progressors and long-term nonprogressors. J Virol 2010; 84: 3576-85.
[37]
Anthony C, York T, Bekker V, et al. Cooperation between strain-specific and broadly neutralizing responses limited viral escape and prolonged the exposure of the broadly neutralizing epitope. J Virol 2017; 91: e00828-17.
[38]
Bar KJ, Sneller MC, Harrison LJ, et al. Effect of HIV antibody VRC01 on viral rebound after treatment interruption. N Engl J Med 2016; 375: 2037-50.
[39]
Caskey M, Klein F, Lorenzi JC, et al. Viraemia suppressed in HIV-1-infected humans by broadly neutralizing antibody 3BNC117. Nature 2015; 522: 487-91.
[40]
Caskey M, Schoofs T, Gruell H, et al. Antibody 10-1074 suppresses viremia in HIV-1-infected individuals. Nat Med 2017; 23(2): 185-91.
[41]
Lynch RM, Boritz E, Coates EE, et al. Virologic effects of broadly neutralizing antibody VRC01 administration during chronic HIV-1 infection. Sci Transl Med 2015; 7: 319ra206.
[42]
McCoy LE, Burton DR. Identification and specificity of broadly neutralizing antibodies against HIV. Immunol Rev 2017; 275: 11-20.
[43]
Sok D, van Gils MJ, Pauthner M, et al. A Recombinant HIV Envelope Trimer Selects for Quaternary Dependent Antibodies Targeting the Trimer Apex. AIDS Res Hum Retroviruses 2014; 30(Suppl. 1): A7-8.
[44]
Doria-Rose NA, Bhiman JN, Roark RS, et al. New member of the V1V2-Directed CAP256-VRC26 lineage that shows increased breadth and exceptional potency. J Virol 2016; 90: 76-91.
[45]
Cale EM, Gorman J, Radakovich NA, et al. Virus-like particles identify an HIV V1V2 apex-binding neutralizing antibody that lacks a protruding loop. Immunity 2017; 46: 777-91.e10.
[46]
Huang J, Kang BH, Ishida E, et al. Identification of a CD4-binding-site antibody to HIV that evolved near-pan neutralization breadth. Immunity 2016; 45: 1108-21.
[47]
Walker LM, Huber M, Doores KJ, et al. Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 2011; 477: 466-70.
[48]
Doria-Rose NA, Schramm CA, Gorman J, et al. Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies. Nature 2014; 509: 55-62.
[49]
Hessell AJ, Jaworski JP, Epson E, et al. Early short-term treatment with neutralizing human monoclonal antibodies halts SHIV infection in infant macaques. Nat Med 2016; 22: 362-8.
[50]
Ledgerwood JE, Coates EE, Yamshchikov G, et al. Safety, pharmacokinetics and neutralization of the broadly neutralizing HIV-1 human monoclonal antibody VRC01 in healthy adults. Clin Exp Immunol 2015; 182: 289-301.
[51]
Mascola JR, Lewis MG, Stiegler G, et al. Protection of Macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies. J Virol 1999; 73: 4009-18.
[52]
Mascola JR, Stiegler G, VanCott TC, et al. Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus by passive infusion of neutralizing antibodies. Nat Med 2000; 6: 207-10.
[53]
Wagh K, Bhattacharya T, Williamson C, et al. Optimal combinations of broadly neutralizing antibodies for prevention and treatment of HIV-1 clade C infection. PLoS Pathog 2016; 12: e1005520.
[54]
Kong R, Xu K, Zhou T, et al. Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody. Science 2016; 352: 828-33.
[55]
Wibmer CK, Moore PL, Morris L. HIV broadly neutralizing antibody targets. Curr Opin HIV AIDS 2015; 10: 135-43.
[56]
Wu X, Zhou T, Zhu J, et al. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 2011; 333(6049): 1593-602.
[57]
Scheid JF, Mouquet H, Ueberheide B, et al. Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 2011; 333: 1633-7.
[58]
Zhou T, Zhu J, Wu X, et al. Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies. Immunity 2013; 39: 245-58.
[59]
Andrabi R, Voss JE, Liang CH, et al. Identification of common features in prototype broadly neutralizing antibodies to HIV envelope V2 apex to facilitate vaccine design. Immunity 2015; 43: 959-73.
[60]
Gorman J, Soto C, Yang MM, et al. Structures of HIV-1 Env V1V2 with broadly neutralizing antibodies reveal commonalities that enable vaccine design. Nat Struct Mol Biol 2016; 23: 81-90.
[61]
Moore PL, Gorman J, Doria-Rose NA, Morris L. Ontogeny-based immunogens for the induction of V2-directed HIV broadly neutralizing antibodies. Immunol Rev 2017; 275: 217-29.
[62]
Doores KJ, Kong L, Krumm SA, et al. Two classes of broadly neutralizing antibodies within a single lineage directed to the high-mannose patch of HIV Envelope. J Virol 2014.
[63]
Garces F, Sok D, Kong L, et al. Structural evolution of glycan recognition by a family of potent HIV antibodies. Cell 2014; 159: 69-79.
[64]
Rusert P, Kouyos RD, Kadelka C, et al. Determinants of HIV-1 broadly neutralizing antibody induction. Nat Med 2016; 22: 1260-7.
[65]
Dugast AS, Arnold K, Lofano G, et al. Virus-driven Inflammation Is Associated With the Development of bNAbs in Spontaneous Controllers of HIV. Clin Infect Dis 2017; 64: 1098-104.
[66]
Locci M, Havenar-Daughton C, Landais E, et al. Human circulating PD-1+CXCR3-CXCR5+ memory Tfh cells are highly functional and correlate with broadly neutralizing HIV antibody responses. Immunity 2013; 39: 758-69.
[67]
Cohen K, Altfeld M, Alter G, Stamatatos L. Early preservation of CXCR5+ PD-1+ helper T cells and B cell activation predict the breadth of neutralizing antibody responses in chronic HIV-1 infection. J Virol 2014; 88: 13310-21.
[68]
Havenar-Daughton C, Carnathan DG, Torrents de la Pena A, et al. Direct probing of germinal center responses reveals immunological features and bottlenecks for neutralizing antibody responses to HIV env trimer. Cell reports 2016; 17: 2195-209.
[69]
Bhiman JN, Anthony C, Doria-Rose NA, et al. Viral variants that initiate and drive maturation of V1V2-directed HIV-1 broadly neutralizing antibodies. Nat Med 2015; 21: 1332-6.
[70]
Liao HX, Lynch R, Zhou T, et al. Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus. Nature 2013; 496: 469-76.
[71]
Gao F, Bonsignori M, Liao HX, et al. Cooperation of B Cell Lineages in Induction of HIV-1-Broadly Neutralizing Antibodies. Cell 2014; 158: 481-91.
[72]
MacLeod DT, Choi NM, Briney B, et al. Early antibody lineage diversification and independent limb maturation lead to broad HIV-1 neutralization targeting the env high-mannose patch. Immunity 2016; 44: 1215-26.
[73]
Bonsignori M, Liao HX, Gao F, et al. Antibody-virus co-evolution in HIV infection: paths for HIV vaccine development. Immunol rev 2017; 275: 145-60.
[74]
Moore PL, Williamson C, Morris L. Virological features associated with the development of broadly neutralizing antibodies to HIV-1. Trends in microbiology 2015.
[75]
Klein F, Diskin R, Scheid JF, et al. Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization. Cell 2013; 153: 126-38.
[76]
Jardine JG, Sok D, Julien JP, Briney B, Sarkar A, Liang CH, et al. Minimally mutated HIV-1 broadly neutralizing antibodies to guide reductionist vaccine design. PLoS Pathog 2016; 12: e1005815.
[77]
Georgiev IS, Rudicell RS, Saunders KO, et al. Antibodies VRC01 and 10E8 neutralize HIV-1 with high breadth and potency even with Ig-framework regions substantially reverted to germline. J Immunol 2014; 192: 1100-6.
[78]
Haynes BF, Shaw GM, Korber B, et al. HIV-host interactions: implications for vaccine design. Cell host & microbe 2016; 19: 292-303.
[79]
Rudicell RS, Kwon YD, Ko SY, et al. Enhanced potency of a broadly neutralizing HIV-1 antibody in vitro improves protection against lentiviral infection in vivo. J Virol 2014.
[80]
Burton DR, Mascola JR. Antibody responses to envelope glycoproteins in HIV-1 infection. Nat Immunol 2015; 16: 571-6.
[81]
Jardine J, Julien JP, Menis S, et al. Rational HIV immunogen design to target specific germline B Cell Receptors. Science 2013; 1234150.
[82]
Walker LM, Phogat SK, Chan-Hui PY, et al. Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 2009; 326: 285-9.
[83]
Bonsignori M, Hwang KK, Chen X, 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.
[84]
Sok D, van Gils MJ, Pauthner M, et al. Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex. Proc Natl Acad Sci USA 2014; 111: 17624-9.
[85]
Briney BS, Willis JR, Hicar MD, Thomas JW 2nd, Crowe JE Jr. Frequency and genetic characterization of V(DD)J recombinants in the human peripheral blood antibody repertoire. Immunology 2012; 137: 56-64.
[86]
Briney BS, Willis JR, Crowe JE Jr. Location and length distribution of somatic hypermutation-associated DNA insertions and deletions reveals regions of antibody structural plasticity. Genes Immun 2012; 13: 523-9.
[87]
McGuire AT, Glenn JA, Lippy A, Stamatatos L. Diverse recombinant HIV-1 Envs fail to activate B cells expressing the germline B cell receptors of the broadly neutralizing anti-HIV-1 antibodies PG9 and 447-52D. J Virol 2014; 88: 2645-57.
[88]
Jardine JG, Ota T, Sok D, et al. HIV-1 VACCINES. Priming a broadly neutralizing antibody response to HIV-1 using a germline-targeting immunogen. Science 2015; 349: 156-61.
[89]
Jardine JG, Kulp DW, Havenar-Daughton C, et al. HIV-1 broadly neutralizing antibody precursor B cells revealed by germline-targeting immunogen. Science 2016; 351: 1458-63.
[90]
Dosenovic P, von Boehmer L, Escolano A, et al. Immunization for HIV-1 Broadly Neutralizing Antibodies in Human Ig Knockin Mice. Cell 2015; 161: 1505-15.
[91]
Steichen JM, Kulp DW, Tokatlian T, et al. HIV vaccine design to target germline precursors of glycan-dependent broadly neutralizing antibodies. Immunity 2016; 45: 483-96.
[92]
Haynes BF, Kelsoe G, Harrison SC, Kepler TB. B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study. Nature biotechnology 2012; 30: 423-33.
[93]
Escolano A, Steichen JM, Dosenovic P, et al. Sequential Immunization Elicits Broadly Neutralizing Anti-HIV-1 Antibodies in Ig Knockin Mice Cell 2016; 166: 1445-58. e12
[94]
Sanders RW, Moore JP. Native-like Env trimers as a platform for HIV-1 vaccine design. Immunol Rev 2017; 275: 161-82.
[95]
McCoy LE, van Gils MJ, Ozorowski G, et al. Holes in the Glycan Shield of the Native HIV Envelope Are a Target of Trimer-Elicited Neutralizing Antibodies. Cell reports 2016; 16: 2327-38.
[96]
Laird Smith M, Murrell B, Eren K, et al. Rapid sequencing of complete env genes from primary HIV-1 samples. Virus Evol 2016; 2(2): vew018.
[97]
Anthony C, Tork T, Bekker V, et al. Cooperation between strain-specific and broadly neutralizing responses limited viral escape and prolonged the exposure of the broadly neutralizing epitope. J Virol 2017; 91(18): e00828-17.