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Volumn 16, Issue 6, 2015, Pages 571-576

Antibody responses to envelope glycoproteins in HIV-1 infection

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS ANTIGEN; HUMAN IMMUNODEFICIENCY VIRUS PROTEIN; NEUTRALIZING ANTIBODY; VIRUS ENVELOPE PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS VACCINE;

EID: 84929896699     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni.3158     Document Type: Review
Times cited : (341)

References (108)
  • 1
    • 0037213278 scopus 로고    scopus 로고
    • Heterogeneity of envelope molecules expressed on primary human immunodeficiency virus type 1 particles as probed by the binding of neutralizing and nonneutralizing antibodies
    • 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 nonneutralizing antibodies. J. Virol. 77, 353-365 (2003).
    • (2003) J. Virol. , vol.77 , pp. 353-365
    • Poignard, P.1
  • 2
    • 33144486096 scopus 로고    scopus 로고
    • Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1
    • Moore, P. L. et al. Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1. J. Virol. 80, 2515-2528 (2006).
    • (2006) J. Virol. , vol.80 , pp. 2515-2528
    • Moore, P.L.1
  • 3
    • 20844448731 scopus 로고    scopus 로고
    • Antigenic conservation and immunogenicity of the HIV coreceptor binding site
    • Decker, J. M. et al. Antigenic conservation and immunogenicity of the HIV coreceptor binding site. J. Exp. Med. 201, 1407-1419 (2005).
    • (2005) J. Exp. Med. , vol.201 , pp. 1407-1419
    • Decker, J.M.1
  • 4
    • 67249085575 scopus 로고    scopus 로고
    • Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site
    • Dey, B. et al. Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site. PLoS Pathog. 5, e1000445 (2009).
    • (2009) PLoS Pathog. , vol.5 , pp. e1000445
    • Dey, B.1
  • 5
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker, L. M. et al. Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326, 285-289 (2009).
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1
  • 6
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker, L. M. et al. Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 477, 466-470 (2011).
    • (2011) Nature , vol.477 , pp. 466-470
    • Walker, L.M.1
  • 7
    • 84900517557 scopus 로고    scopus 로고
    • Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers
    • Falkowska, E. et al. Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers. Immunity 40, 657-668 (2014).
    • (2014) Immunity , vol.40 , pp. 657-668
    • Falkowska, E.1
  • 8
    • 84900467984 scopus 로고    scopus 로고
    • Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers
    • Blattner, C. et al. Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers. Immunity 40, 669-680 (2014).
    • (2014) Immunity , vol.40 , pp. 669-680
    • Blattner, C.1
  • 9
    • 84899991983 scopus 로고    scopus 로고
    • Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies
    • Doria-Rose, N. A. et al. Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies. Nature 509, 55-62 (2014).
    • (2014) Nature , vol.509 , pp. 55-62
    • Doria-Rose, N.A.1
  • 10
    • 84921607768 scopus 로고    scopus 로고
    • Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface
    • Huang, J. et al. Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface. Nature 515, 138-142 (2014).
    • (2014) Nature , vol.515 , pp. 138-142
    • Huang, J.1
  • 11
    • 84866443327 scopus 로고    scopus 로고
    • Broad neutralization by a combination of antibodies recognizing the CD4 binding site and a new conformational epitope on the HIV-1 envelope protein
    • Klein, F. et al. Broad neutralization by a combination of antibodies recognizing the CD4 binding site and a new conformational epitope on the HIV-1 envelope protein. J. Exp. Med. 209, 1469-1479 (2012).
    • (2012) J. Exp. Med. , vol.209 , pp. 1469-1479
    • Klein, F.1
  • 12
    • 0032543555 scopus 로고    scopus 로고
    • The antigenic structure of the HIV gp120 envelope glycoprotein
    • Wyatt, R. et al. The antigenic structure of the HIV gp120 envelope glycoprotein. Nature 393, 705-711 (1998).
    • (1998) Nature , vol.393 , pp. 705-711
    • Wyatt, R.1
  • 13
    • 0030043169 scopus 로고    scopus 로고
    • Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein
    • Moore, J. P. & Sodroski, J. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J. Virol. 70, 1863-1872 (1996).
    • (1996) J. Virol. , vol.70 , pp. 1863-1872
    • Moore, J.P.1    Sodroski, J.2
  • 14
    • 77952311370 scopus 로고    scopus 로고
    • The role of antibodies in HIV vaccines
    • Mascola, J. R. & Montefiori, D. C. The role of antibodies in HIV vaccines. Annu. Rev. Immunol. 28, 413-444 (2010).
    • (2010) Annu. Rev. Immunol. , vol.28 , pp. 413-444
    • Mascola, J.R.1    Montefiori, D.C.2
  • 15
    • 84884678235 scopus 로고    scopus 로고
    • A next-generation cleaved, soluble HIV-1 Env Trimer, BG505 SOSIP. 664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies
    • Sanders, R. W. et al. A next-generation cleaved, soluble HIV-1 Env Trimer, BG505 SOSIP. 664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies. PLoS Pathog. 9, e1003618 (2013).
    • (2013) PLoS Pathog. , vol.9 , pp. e1003618
    • Sanders, R.W.1
  • 16
    • 84887307095 scopus 로고    scopus 로고
    • Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation
    • Ringe, R. P. et al. Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation. Proc. Natl. Acad. Sci. USA 110, 18256-18261 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 18256-18261
    • Ringe, R.P.1
  • 17
    • 84903173697 scopus 로고    scopus 로고
    • Differential binding of neutralizing and non-neutralizing antibodies to native-like soluble HIV-1 Env trimers, uncleaved Env proteins, and monomeric subunits
    • Yasmeen, A. et al. Differential binding of neutralizing and non-neutralizing antibodies to native-like soluble HIV-1 Env trimers, uncleaved Env proteins, and monomeric subunits. Retrovirology 11, 41 (2014).
    • (2014) Retrovirology , vol.11 , pp. 41
    • Yasmeen, A.1
  • 18
    • 84890858459 scopus 로고    scopus 로고
    • Crystal structure of a soluble cleaved HIV-1 envelope trimer
    • Julien, J. P. et al. Crystal structure of a soluble cleaved HIV-1 envelope trimer. Science 342, 1477-1483 (2013).
    • (2013) Science , vol.342 , pp. 1477-1483
    • Julien, J.P.1
  • 19
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • Lyumkis, D. et al. Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science 342, 1484-1490 (2013).
    • (2013) Science , vol.342 , pp. 1484-1490
    • Lyumkis, D.1
  • 20
    • 84909640954 scopus 로고    scopus 로고
    • Structure and immune recognition of trimeric pre-fusion HIV-1 Env
    • Pancera, M. et al. Structure and immune recognition of trimeric pre-fusion HIV-1 Env. Nature 514, 455-461 (2014).
    • (2014) Nature , vol.514 , pp. 455-461
    • Pancera, M.1
  • 21
    • 57349127300 scopus 로고    scopus 로고
    • 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
    • Tomaras, G. D. 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. 82, 12449-12463 (2008).
    • (2008) J. Virol. , vol.82 , pp. 12449-12463
    • Tomaras, G.D.1
  • 22
    • 44649102135 scopus 로고    scopus 로고
    • Identification and characterization of transmitted and early founder virus envelopes in primary HIV-1 infection
    • Keele, B. F. et al. Identification and characterization of transmitted and early founder virus envelopes in primary HIV-1 infection. Proc. Natl. Acad. Sci. USA 105, 7552-7557 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7552-7557
    • Keele, B.F.1
  • 23
    • 84860153884 scopus 로고    scopus 로고
    • The antibody response against HIV-1. Cold Spring Harbor Perspect
    • Overbaugh, J. & Morris, L. The antibody response against HIV-1. Cold Spring Harbor Perspect. Med. 2, a007039 (2012).
    • (2012) Med. , vol.2 , pp. a007039
    • Overbaugh, J.1    Morris, L.2
  • 24
    • 0036719574 scopus 로고    scopus 로고
    • Antibodies, viruses and vaccines
    • Burton, D. R. Antibodies, viruses and vaccines. Nat. Rev. Immunol. 2, 706-713 (2002).
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 706-713
    • Burton, D.R.1
  • 25
    • 84869110634 scopus 로고    scopus 로고
    • A novel assay for antibody-dependent cell-mediated cytotoxicity against HIV-1-or SIV-infected cells reveals incomplete overlap with antibodies measured by neutralization and binding assays
    • Alpert, M. D. et al. A novel assay for antibody-dependent cell-mediated cytotoxicity against HIV-1-or SIV-infected cells reveals incomplete overlap with antibodies measured by neutralization and binding assays. J. Virol. 86, 12039-12052 (2012).
    • (2012) J. Virol. , vol.86 , pp. 12039-12052
    • Alpert, M.D.1
  • 26
    • 84865068814 scopus 로고    scopus 로고
    • Antibody-dependent cellular cytotoxicity against primary HIV-infected CD4+ T cells is directly associated with the magnitude of surface IgG binding
    • Smalls-Mantey, A. et al. Antibody-dependent cellular cytotoxicity against primary HIV-infected CD4+ T cells is directly associated with the magnitude of surface IgG binding. J. Virol. 86, 8672-8680 (2012).
    • (2012) J. Virol. , vol.86 , pp. 8672-8680
    • Smalls-Mantey, A.1
  • 27
    • 84883774338 scopus 로고    scopus 로고
    • Comparative efficiency of HIV-1-infected T cell killing by NK cells, monocytes and neutrophils
    • Smalls-Mantey, A. , Connors, M. & Sattentau, Q. J. Comparative efficiency of HIV-1-infected T cell killing by NK cells, monocytes and neutrophils. PLoS ONE 8, e74858 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e74858
    • Smalls-Mantey, A.1    Connors, M.2    Sattentau, Q.J.3
  • 28
    • 79960555557 scopus 로고    scopus 로고
    • High-throughput quantitative analysis of HIV-1 and SIV-specific ADCC-mediating antibody responses
    • Pollara, J. et al. High-throughput quantitative analysis of HIV-1 and SIV-specific ADCC-mediating antibody responses. Cytometry 79, 603-612 (2011).
    • (2011) Cytometry , vol.79 , pp. 603-612
    • Pollara, J.1
  • 29
    • 69549103041 scopus 로고    scopus 로고
    • Fc receptor-mediated antiviral antibodies
    • Forthal, D. N. & Moog, C. Fc receptor-mediated antiviral antibodies. Curr. Opin. HIV AIDS 4, 388-393 (2009).
    • (2009) Curr. Opin. HIV AIDS , vol.4 , pp. 388-393
    • Forthal, D.N.1    Moog, C.2
  • 31
    • 84877152391 scopus 로고    scopus 로고
    • Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity
    • Ackerman, M. E. et al. Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity. J. Clin. Invest. 123, 2183-2192 (2013).
    • (2013) J. Clin. Invest. , vol.123 , pp. 2183-2192
    • Ackerman, M.E.1
  • 32
    • 34548496893 scopus 로고    scopus 로고
    • Fc receptor but not complement binding is important in antibody protection against HIV
    • Hessell, A. J. et al. Fc receptor but not complement binding is important in antibody protection against HIV. Nature 449, 101-104 (2007).
    • (2007) Nature , vol.449 , pp. 101-104
    • Hessell, A.J.1
  • 33
    • 84908077691 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV-1 antibodies require Fc effector functions for in vivo activity
    • Bournazos, S. et al. Broadly neutralizing anti-HIV-1 antibodies require Fc effector functions for in vivo activity. Cell 158, 1243-1253 (2014).
    • (2014) Cell , vol.158 , pp. 1243-1253
    • Bournazos, S.1
  • 34
    • 73349094086 scopus 로고    scopus 로고
    • Vaccination with ALVAC and AIDSVAX to prevent HIV-1 infection in Thailand
    • Rerks-Ngarm, S. et al. Vaccination with ALVAC and AIDSVAX to prevent HIV-1 infection in Thailand. N. Engl. J. Med. 361, 2209-2220 (2009).
    • (2009) N. Engl. J. Med. , vol.361 , pp. 2209-2220
    • Rerks-Ngarm, S.1
  • 35
    • 84859393693 scopus 로고    scopus 로고
    • Immune-correlates analysis of an HIV-1 vaccine efficacy trial
    • Haynes, B. F. et al. Immune-correlates analysis of an HIV-1 vaccine efficacy trial. N. Engl. J. Med. 366, 1275-1286 (2012).
    • (2012) N. Engl. J. Med. , vol.366 , pp. 1275-1286
    • Haynes, B.F.1
  • 36
    • 84872809067 scopus 로고    scopus 로고
    • Vaccine induction of antibodies against a structurally heterogeneous site of immune pressure within HIV-1 envelope protein variable regions 1 and 2
    • Liao, H. X. et al. Vaccine induction of antibodies against a structurally heterogeneous site of immune pressure within HIV-1 envelope protein variable regions 1 and 2. Immunity 38, 176-186 (2013).
    • (2013) Immunity , vol.38 , pp. 176-186
    • Liao, H.X.1
  • 37
    • 84899087118 scopus 로고    scopus 로고
    • Vaccine-induced Env V1-V2 IgG3 correlates with lower HIV-1 infection risk and declines soon after vaccination
    • Yates, N. L. et al. Vaccine-induced Env V1-V2 IgG3 correlates with lower HIV-1 infection risk and declines soon after vaccination. Sci. Transl. Med. 6, 228ra239 (2014).
    • (2014) Sci. Transl. Med. , vol.6 , pp. 228ra239
    • Yates, N.L.1
  • 38
    • 84874051662 scopus 로고    scopus 로고
    • Human cervicovaginal mucus contains an activity that hinders HIV-1 movement
    • Shukair, S. A. et al. Human cervicovaginal mucus contains an activity that hinders HIV-1 movement. Mucosal Immunol. 6, 427-434 (2013).
    • (2013) Mucosal Immunol. , vol.6 , pp. 427-434
    • Shukair, S.A.1
  • 39
    • 81755187039 scopus 로고    scopus 로고
    • Role of donor genital tract HIV-1 diversity in the transmission bottleneck
    • Boeras, D. I. et al. Role of donor genital tract HIV-1 diversity in the transmission bottleneck. Proc. Natl. Acad. Sci. USA 108, E1156-E1163 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. E1156-E1163
    • Boeras, D.I.1
  • 40
    • 84884886414 scopus 로고    scopus 로고
    • Differential binding of IgG and IgA to mucus of the female reproductive tract
    • Fahrbach, K. M. , Malykhina, O. , Stieh, D. J. & Hope, T. J. Differential binding of IgG and IgA to mucus of the female reproductive tract. PLoS ONE 8, e76176 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e76176
    • Fahrbach, K.M.1    Malykhina, O.2    Stieh, D.J.3    Hope, T.J.4
  • 41
    • 84883368011 scopus 로고    scopus 로고
    • New paradigms for functional HIV-specific nonneutralizing antibodies
    • Forthal, D. , Hope, T. J. & Alter, G. New paradigms for functional HIV-specific nonneutralizing antibodies. Curr. Opin. HIV AIDS 8, 393-401 (2013).
    • (2013) Curr. Opin. HIV AIDS , vol.8 , pp. 393-401
    • Forthal, D.1    Hope, T.J.2    Alter, G.3
  • 42
    • 0030240623 scopus 로고    scopus 로고
    • HIV-1 gp120-specific antibody-dependent cell-mediated cytotoxicity correlates with rate of disease progression
    • Baum, L. L. et al. HIV-1 gp120-specific antibody-dependent cell-mediated cytotoxicity correlates with rate of disease progression. J. Immunol. 157, 2168-2173 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 2168-2173
    • Baum, L.L.1
  • 43
    • 0033375327 scopus 로고    scopus 로고
    • Antibody-dependent cellular cytotoxicity independently predicts survival in severely immunocompromised human immunodeficiency virus-infected patients
    • Forthal, D. N. et al. Antibody-dependent cellular cytotoxicity independently predicts survival in severely immunocompromised human immunodeficiency virus-infected patients. J. Infect. Dis. 180, 1338-1341 (1999).
    • (1999) J. Infect. Dis. , vol.180 , pp. 1338-1341
    • Forthal, D.N.1
  • 44
    • 84901262680 scopus 로고    scopus 로고
    • Lack of protection following passive transfer of polyclonal highly functional low-dose non-neutralizing antibodies
    • Dugast, A. S. et al. Lack of protection following passive transfer of polyclonal highly functional low-dose non-neutralizing antibodies. PLoS ONE 9, e97229 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e97229
    • Dugast, A.S.1
  • 45
    • 0037405488 scopus 로고    scopus 로고
    • Defining the protective antibody response for HIV-1
    • Mascola, J. R. Defining the protective antibody response for HIV-1. Curr. Mol. Med. 3, 209-216 (2003).
    • (2003) Curr. Mol. Med. , vol.3 , pp. 209-216
    • Mascola, J.R.1
  • 46
    • 84869232528 scopus 로고    scopus 로고
    • Highly potent HIV-specific antibody neutralization in vitro translates into effective protection against mucosal SHIV challenge in vivo
    • Moldt, B. et al. Highly potent HIV-specific antibody neutralization in vitro translates into effective protection against mucosal SHIV challenge in vivo. Proc. Natl. Acad. Sci. USA 109, 18921-18925 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 18921-18925
    • Moldt, B.1
  • 47
    • 84907212727 scopus 로고    scopus 로고
    • Passive transfer of modest titers of potent and broadly neutralizing anti-HIV monoclonal antibodies block SHIV infection in macaques
    • Shingai, M. et al. Passive transfer of modest titers of potent and broadly neutralizing anti-HIV monoclonal antibodies block SHIV infection in macaques. J. Exp. Med. 211, 2061-2074 (2014).
    • (2014) J. Exp. Med. , vol.211 , pp. 2061-2074
    • Shingai, M.1
  • 48
    • 84904497424 scopus 로고    scopus 로고
    • Neutralizing antibodies to HIV-1 envelope protect more effectively in vivo than those to the CD4 receptor
    • Pegu, A. et al. Neutralizing antibodies to HIV-1 envelope protect more effectively in vivo than those to the CD4 receptor. Sci. Transl. Med. 6, 243ra288 (2014).
    • (2014) Sci. Transl. Med. , vol.6 , pp. 243ra288
    • Pegu, A.1
  • 49
    • 79960585840 scopus 로고    scopus 로고
    • Limited or no protection by weakly or nonneutralizing antibodies against vaginal SHIV challenge of macaques compared with a strongly neutralizing antibody
    • Burton, D. R. et al. Limited or no protection by weakly or nonneutralizing antibodies against vaginal SHIV challenge of macaques compared with a strongly neutralizing antibody. Proc. Natl. Acad. Sci. USA 108, 11181-11186 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 11181-11186
    • Burton, D.R.1
  • 50
    • 84887626950 scopus 로고    scopus 로고
    • Therapeutic efficacy of potent neutralizing HIV-1-specific monoclonal antibodies in SHIV-infected rhesus monkeys
    • Barouch, D. H. et al. Therapeutic efficacy of potent neutralizing HIV-1-specific monoclonal antibodies in SHIV-infected rhesus monkeys. Nature 503, 224-228 (2013).
    • (2013) Nature , vol.503 , pp. 224-228
    • Barouch, D.H.1
  • 51
    • 33748482187 scopus 로고    scopus 로고
    • Evaluation of passively transferred, nonneutralizing antibody-dependent cellular cytotoxicity-mediating IgG in protection of neonatal rhesus macaques against oral SIVmac251 challenge
    • Florese, R. H. et al. Evaluation of passively transferred, nonneutralizing antibody-dependent cellular cytotoxicity-mediating IgG in protection of neonatal rhesus macaques against oral SIVmac251 challenge. J. Immunol. 177, 4028-4036 (2006).
    • (2006) J. Immunol. , vol.177 , pp. 4028-4036
    • Florese, R.H.1
  • 52
    • 84887627657 scopus 로고    scopus 로고
    • Antibody-mediated immunotherapy of macaques chronically infected with SHIV suppresses viraemia
    • Shingai, M. et al. Antibody-mediated immunotherapy of macaques chronically infected with SHIV suppresses viraemia. Nature 503, 277-280 (2013).
    • (2013) Nature , vol.503 , pp. 277-280
    • Shingai, M.1
  • 53
    • 8644251891 scopus 로고    scopus 로고
    • Comprehensive cross-clade neutralization analysis of a panel of anti-human immunodeficiency virus type 1 monoclonal antibodies
    • Binley, J. M. et al. Comprehensive cross-clade neutralization analysis of a panel of anti-human immunodeficiency virus type 1 monoclonal antibodies. J. Virol. 78, 13232-13252 (2004).
    • (2004) J. Virol. , vol.78 , pp. 13232-13252
    • Binley, J.M.1
  • 55
    • 0037456827 scopus 로고    scopus 로고
    • Antibody neutralization and escape by HIV-1
    • Wei, X. et al. Antibody neutralization and escape by HIV-1. Nature 422, 307-312 (2003).
    • (2003) Nature , vol.422 , pp. 307-312
    • Wei, X.1
  • 56
    • 0037389643 scopus 로고    scopus 로고
    • Rapid evolution of the neutralizing antibody response to HIV type 1 infection
    • 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 100, 4144-4149 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4144-4149
    • Richman, D.D.1    Wrin, T.2    Little, S.J.3    Petropoulos, C.J.4
  • 57
    • 0025267919 scopus 로고
    • Rapid development of isolate-specific neutralizing antibodies after primary HIV-1 infection and consequent emergence of virus variants which resist neutralization by autologous sera
    • Albert, J. et al. 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 4, 107-112 (1990).
    • (1990) AIDS , vol.4 , pp. 107-112
    • Albert, J.1
  • 58
    • 0025854294 scopus 로고
    • Homotypic antibody responses to fresh clinical isolates of human immunodeficiency virus
    • Montefiori, D. C. et al. Homotypic antibody responses to fresh clinical isolates of human immunodeficiency virus. Virology 182, 635-643 (1991).
    • (1991) Virology , vol.182 , pp. 635-643
    • Montefiori, D.C.1
  • 59
    • 84898538468 scopus 로고    scopus 로고
    • Development of broadly neutralizing antibodies from autologous neutralizing antibody responses in HIV infection
    • Derdeyn, C. A. , Moore, P. L. & Morris, L. Development of broadly neutralizing antibodies from autologous neutralizing antibody responses in HIV infection. Curr. Opin. HIV AIDS 9, 210-216 (2014).
    • (2014) Curr. Opin. HIV AIDS , vol.9 , pp. 210-216
    • Derdeyn, C.A.1    Moore, P.L.2    Morris, L.3
  • 60
    • 70349695689 scopus 로고    scopus 로고
    • Escape from autologous neutralizing antibodies in acute/early subtype C HIV-1 infection requires multiple pathways
    • Rong, R. et al. Escape from autologous neutralizing antibodies in acute/early subtype C HIV-1 infection requires multiple pathways. PLoS Pathog. 5, e1000594 (2009).
    • (2009) PLoS Pathog. , vol.5 , pp. e1000594
    • Rong, R.1
  • 61
    • 70349686331 scopus 로고    scopus 로고
    • Limited neutralizing antibody specificities drive neutralization escape in early HIV-1 subtype C infection
    • Moore, P. L. et al. Limited neutralizing antibody specificities drive neutralization escape in early HIV-1 subtype C infection. PLoS Pathog. 5, e1000598 (2009).
    • (2009) PLoS Pathog. , vol.5 , pp. e1000598
    • Moore, P.L.1
  • 62
    • 33846552274 scopus 로고    scopus 로고
    • Role of V1V2 and other human immunodeficiency virus type 1 envelope domains in resistance to autologous neutralization during clade C infection
    • Rong, R. et al. Role of V1V2 and other human immunodeficiency virus type 1 envelope domains in resistance to autologous neutralization during clade C infection. J. Virol. 81, 1350-1359 (2007).
    • (2007) J. Virol. , vol.81 , pp. 1350-1359
    • Rong, R.1
  • 63
    • 77958115264 scopus 로고    scopus 로고
    • A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals
    • Walker, L. M. et al. A limited number of antibody specificities mediate broad and potent serum neutralization in selected HIV-1 infected individuals. PLoS Pathog. 6, e1001028 (2010).
    • (2010) PLoS Pathog. , vol.6 , pp. e1001028
    • Walker, L.M.1
  • 64
    • 58149517700 scopus 로고    scopus 로고
    • Analysis of the neutralization specificities in polyclonal sera derived from human immunodeficiency virus type-1 infected individuals
    • Li, Y. et al. Analysis of the neutralization specificities in polyclonal sera derived from human immunodeficiency virus type-1 infected individuals. J. Virol. 83, 1045-1059 (2009).
    • (2009) J. Virol. , vol.83 , pp. 1045-1059
    • Li, Y.1
  • 65
    • 56449131391 scopus 로고    scopus 로고
    • 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
    • Binley, J. M. 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. 82, 11651-11668 (2008).
    • (2008) J. Virol. , vol.82 , pp. 11651-11668
    • Binley, J.M.1
  • 66
    • 80055104586 scopus 로고    scopus 로고
    • Polyclonal B cell responses to conserved neutralization epitopes in a subset of HIV-1-infected individuals
    • Tomaras, G. D. et al. Polyclonal B cell responses to conserved neutralization epitopes in a subset of HIV-1-infected individuals. J. Virol. 85, 11502-11519 (2011).
    • (2011) J. Virol. , vol.85 , pp. 11502-11519
    • Tomaras, G.D.1
  • 67
    • 84860723906 scopus 로고    scopus 로고
    • Two distinct broadly neutralizing antibody specificities of different clonal lineages in a single HIV-1-infected donor: Implications for vaccine design
    • Bonsignori, M. 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. 86, 4688-4692 (2012).
    • (2012) J. Virol. , vol.86 , pp. 4688-4692
    • Bonsignori, M.1
  • 68
    • 69149083668 scopus 로고    scopus 로고
    • Neutralizing antibodies generated during natural HIV-1 infection: Good news for an HIV-1 vaccine?
    • 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. 15, 866-870 (2009).
    • (2009) Nat. Med. , vol.15 , pp. 866-870
    • Stamatatos, L.1    Morris, L.2    Burton, D.R.3    Mascola, J.R.4
  • 69
    • 34249950588 scopus 로고    scopus 로고
    • Dissecting the neutralizing antibody specificities of broadly neutralizing sera from HIV-1 infected donors
    • Dhillon, A. K. et al. Dissecting the neutralizing antibody specificities of broadly neutralizing sera from HIV-1 infected donors. J. Virol. 81, 6548-6562 (2007).
    • (2007) J. Virol. , vol.81 , pp. 6548-6562
    • Dhillon, A.K.1
  • 70
    • 67650453747 scopus 로고    scopus 로고
    • 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
    • Simek, M. D. 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. 83, 7337-7348 (2009).
    • (2009) J. Virol. , vol.83 , pp. 7337-7348
    • Simek, M.D.1
  • 71
    • 79955389756 scopus 로고    scopus 로고
    • 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
    • Gray, E. S. 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. 85, 4828-4840 (2011).
    • (2011) J. Virol. , vol.85 , pp. 4828-4840
    • Gray, E.S.1
  • 72
    • 84866493348 scopus 로고    scopus 로고
    • Broad and potent neutralization of HIV-1 by a gp41-specific human antibody
    • Huang, J. et al. Broad and potent neutralization of HIV-1 by a gp41-specific human antibody. Nature 491, 406-412 (2012).
    • (2012) Nature , vol.491 , pp. 406-412
    • Huang, J.1
  • 73
    • 63849131879 scopus 로고    scopus 로고
    • Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals
    • Scheid, J. F. et al. Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals. Nature 458, 636-640 (2009).
    • (2009) Nature , vol.458 , pp. 636-640
    • Scheid, J.F.1
  • 74
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope surface identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu, X. et al. Rational design of envelope surface identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 329, 856-861 (2010).
    • (2010) Science , vol.329 , pp. 856-861
    • Wu, X.1
  • 75
    • 84917705974 scopus 로고    scopus 로고
    • Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex
    • Sok, D. et al. Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex. Proc. Natl. Acad. Sci. USA 111, 17624-17629 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 17624-17629
    • Sok, D.1
  • 76
    • 84863774072 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies: New prospects to counter highly antigenically diverse viruses
    • Burton, D. R. , Poignard, P. , Stanfield, R. L. & Wilson, I. A. Broadly neutralizing antibodies: new prospects to counter highly antigenically diverse viruses. Science 337, 183-186 (2012).
    • (2012) Science , vol.337 , pp. 183-186
    • Burton, D.R.1    Poignard, P.2    Stanfield, R.L.3    Wilson, I.A.4
  • 77
    • 84894173514 scopus 로고    scopus 로고
    • Structural insights on the role of antibodies in HIV-1 vaccine and therapy
    • West, A. P. Jr. et al. Structural insights on the role of antibodies in HIV-1 vaccine and therapy. Cell 156, 633-648 (2014).
    • (2014) Cell , vol.156 , pp. 633-648
    • West, A.P.1
  • 78
    • 84866495323 scopus 로고    scopus 로고
    • Human antibodies that neutralize HIV-1: Identification, structures, and B cell ontogenies
    • Kwong, P. D. & Mascola, J. R. Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies. Immunity 37, 412-425 (2012).
    • (2012) Immunity , vol.37 , pp. 412-425
    • Kwong, P.D.1    Mascola, J.R.2
  • 79
    • 84921606536 scopus 로고    scopus 로고
    • Insights into the trimeric HIV-1 envelope glycoprotein structure
    • Ward, A. B. & Wilson, I. A. Insights into the trimeric HIV-1 envelope glycoprotein structure. Trends Biochem. Sci. 40, 101-107 (2015).
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 101-107
    • Ward, A.B.1    Wilson, I.A.2
  • 80
    • 84862641275 scopus 로고    scopus 로고
    • HIV vaccine design: The neutralizing antibody conundrum
    • Stamatatos, L. HIV vaccine design: the neutralizing antibody conundrum. Curr. Opin. Immunol. 24, 316-323 (2012).
    • (2012) Curr. Opin. Immunol. , vol.24 , pp. 316-323
    • Stamatatos, L.1
  • 81
    • 84925844719 scopus 로고    scopus 로고
    • Virological features associated with the development of broadly neutralizing antibodies to HIV-1
    • 5 January
    • Moore, P. L. , Williamson, C. & Morris, L. Virological features associated with the development of broadly neutralizing antibodies to HIV-1. Trends Microbiol. doi:10. 1016/j. Tim. 2014. 12. 007 (5 January 2015).
    • (2015) Trends Microbiol
    • Moore, P.L.1    Williamson, C.2    Morris, L.3
  • 82
    • 84879302728 scopus 로고    scopus 로고
    • HIV-1 neutralizing antibodies: Understanding nature's pathways
    • Mascola, J. R. & Haynes, B. F. HIV-1 neutralizing antibodies: understanding nature's pathways. Immunol. Rev. 254, 225-244 (2013).
    • (2013) Immunol. Rev. , vol.254 , pp. 225-244
    • Mascola, J.R.1    Haynes, B.F.2
  • 83
    • 84867630116 scopus 로고    scopus 로고
    • A blueprint for HIV vaccine discovery
    • Burton, D. R. et al. A blueprint for HIV vaccine discovery. Cell Host Microbe 12, 396-407 (2012).
    • (2012) Cell Host Microbe , vol.12 , pp. 396-407
    • Burton, D.R.1
  • 84
    • 84875759341 scopus 로고    scopus 로고
    • Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization
    • Klein, F. et al. Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization. Cell 153, 126-138 (2013).
    • (2013) Cell , vol.153 , pp. 126-138
    • Klein, F.1
  • 85
    • 84875551472 scopus 로고    scopus 로고
    • Broadly neutralizing antiviral antibodies
    • Corti, D. & Lanzavecchia, A. Broadly neutralizing antiviral antibodies. Annu. Rev. Immunol. 31, 705-742 (2013).
    • (2013) Annu. Rev. Immunol. , vol.31 , pp. 705-742
    • Corti, D.1    Lanzavecchia, A.2
  • 86
    • 84907681865 scopus 로고    scopus 로고
    • Immunoglobulin gene insertions and deletions in the affinity maturation of HIV-1 broadly reactive neutralizing antibodies
    • Kepler, T. B. et al. Immunoglobulin gene insertions and deletions in the affinity maturation of HIV-1 broadly reactive neutralizing antibodies. Cell Host Microbe 16, 304-313 (2014).
    • (2014) Cell Host Microbe , vol.16 , pp. 304-313
    • Kepler, T.B.1
  • 87
    • 84888251984 scopus 로고    scopus 로고
    • The effects of somatic hypermutation on neutralization and binding in the PGT121 family of broadly neutralizing HIV antibodies
    • Sok, D. et al. The effects of somatic hypermutation on neutralization and binding in the PGT121 family of broadly neutralizing HIV antibodies. PLoS Pathog. 9, e1003754 (2013).
    • (2013) PLoS Pathog. , vol.9 , pp. e1003754
    • Sok, D.1
  • 88
    • 84876797103 scopus 로고    scopus 로고
    • Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus
    • Liao, H. X. et al. Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus. Nature 496, 469-476 (2013).
    • (2013) Nature , vol.496 , pp. 469-476
    • Liao, H.X.1
  • 89
    • 84860706280 scopus 로고    scopus 로고
    • Human peripheral blood antibodies with long HCDR3s are established primarily at original recombination using a limited subset of germline genes
    • Briney, B. S. , Willis, J. R. & Crowe, J. E. Jr. Human peripheral blood antibodies with long HCDR3s are established primarily at original recombination using a limited subset of germline genes. PLoS ONE 7, e36750 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e36750
    • Briney, B.S.1    Willis, J.R.2    Crowe, J.E.3
  • 90
    • 84866843530 scopus 로고    scopus 로고
    • A mouse model for HIV-1 entry
    • Pietzsch, J. et al. A mouse model for HIV-1 entry. Proc. Natl. Acad. Sci. USA 109, 15859-15864 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 15859-15864
    • Pietzsch, J.1
  • 91
    • 0034864776 scopus 로고    scopus 로고
    • Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro
    • Parren, P. W. et al. Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro. J. Virol. 75, 8340-8347 (2001).
    • (2001) J. Virol. , vol.75 , pp. 8340-8347
    • Parren, P.W.1
  • 92
    • 0036170921 scopus 로고    scopus 로고
    • 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
    • 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).
    • (2002) J. Virol. , vol.76 , pp. 2123-2130
    • Nishimura, Y.1
  • 93
    • 84907971356 scopus 로고    scopus 로고
    • Enhanced potency of a broadly neutralizing HIV-1 antibody in vitro improves protection against lentiviral infection in vivo
    • Rudicell, R. S. et al. Enhanced potency of a broadly neutralizing HIV-1 antibody in vitro improves protection against lentiviral infection in vivo. J. Virol. 88, 12669-12682 (2014).
    • (2014) J. Virol. , vol.88 , pp. 12669-12682
    • Rudicell, R.S.1
  • 94
    • 68349160853 scopus 로고    scopus 로고
    • Effective, low-titer antibody protection against low-dose repeated mucosal SHIV challenge in macaques
    • Hessell, A. J. et al. Effective, low-titer antibody protection against low-dose repeated mucosal SHIV challenge in macaques. Nat. Med. 15, 951-954 (2009).
    • (2009) Nat. Med. , vol.15 , pp. 951-954
    • Hessell, A.J.1
  • 95
    • 84870562234 scopus 로고    scopus 로고
    • HIV therapy by a combination of broadly neutralizing antibodies in humanized mice
    • Klein, F. et al. HIV therapy by a combination of broadly neutralizing antibodies in humanized mice. Nature 492, 118-122 (2012).
    • (2012) Nature , vol.492 , pp. 118-122
    • Klein, F.1
  • 96
    • 84911947017 scopus 로고    scopus 로고
    • Enhanced HIV-1 immunotherapy by commonly arising antibodies that target virus escape variants
    • Klein, F. et al. Enhanced HIV-1 immunotherapy by commonly arising antibodies that target virus escape variants. J. Exp. Med. 211, 2361-2372 (2014).
    • (2014) J. Exp. Med. , vol.211 , pp. 2361-2372
    • Klein, F.1
  • 97
    • 84905369598 scopus 로고    scopus 로고
    • Cooperation of B cell lineages in induction of HIV-1-broadly neutralizing antibodies
    • Gao, F. et al. Cooperation of B cell lineages in induction of HIV-1-broadly neutralizing antibodies. Cell 158, 481-491 (2014).
    • (2014) Cell , vol.158 , pp. 481-491
    • Gao, F.1
  • 98
    • 79958086672 scopus 로고    scopus 로고
    • Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected
    • Crooks, E. T. , Tong, T. , Osawa, K. & Binley, J. M. Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected. J. Virol. 85, 5825-5839 (2011).
    • (2011) J. Virol. , vol.85 , pp. 5825-5839
    • Crooks, E.T.1    Tong, T.2    Osawa, K.3    Binley, J.M.4
  • 99
    • 84899909771 scopus 로고    scopus 로고
    • Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike
    • Scharf, L. et al. Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike. Cell Reports 7, 785-795 (2014).
    • (2014) Cell Reports , vol.7 , pp. 785-795
    • Scharf, L.1
  • 100
    • 84880161438 scopus 로고    scopus 로고
    • Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120. Nat
    • Kong, L. et al. Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120. Nat. Struct. Mol. Biol. 20, 796-803 (2013).
    • (2013) Struct. Mol. Biol. , vol.20 , pp. 796-803
    • Kong, L.1
  • 101
    • 82255179322 scopus 로고    scopus 로고
    • A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield
    • Pejchal, R. et al. A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield. Science 334, 1097-1103 (2011).
    • (2011) Science , vol.334 , pp. 1097-1103
    • Pejchal, R.1
  • 102
    • 84878519611 scopus 로고    scopus 로고
    • Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans
    • Julien, J. P. et al. Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans. PLoS Pathog. 9, e1003342 (2013).
    • (2013) PLoS Pathog. , vol.9 , pp. e1003342
    • Julien, J.P.1
  • 105
    • 0034759882 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41
    • 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).
    • (2001) J. Virol. , vol.75 , pp. 10892-10905
    • Zwick, M.B.1
  • 106
    • 0026655937 scopus 로고
    • Recombinant human Fab fragments neutralize human type 1 immunodeficiency virus in vitro
    • Barbas, C. F. III et al. Recombinant human Fab fragments neutralize human type 1 immunodeficiency virus in vitro. Proc. Natl. Acad. Sci. USA 89, 9339-9343 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9339-9343
    • Barbas, C.F.1
  • 107
    • 80052925616 scopus 로고    scopus 로고
    • Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding
    • Scheid, J. F. et al. Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 333, 1633-1637 (2011).
    • (2011) Science , vol.333 , pp. 1633-1637
    • Scheid, J.F.1
  • 108
    • 84869831194 scopus 로고    scopus 로고
    • Complex-type N-glycan recognition by potent broadly neutralizing HIV antibodies
    • Mouquet, H. et al. Complex-type N-glycan recognition by potent broadly neutralizing HIV antibodies. Proc. Natl. Acad. Sci. USA 109, E3268-E3277 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. E3268-E3277
    • Mouquet, H.1


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