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Volumn 35, Issue 11, 2014, Pages 549-561

Antibody B cell responses in HIV-1 infection

Author keywords

Adaptive immunity; Antibodies; B cells; HIV 1; Viruses

Indexed keywords

B LYMPHOCYTE ANTIBODY; NEUTRALIZING ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; SECRETORY IMMUNOGLOBULIN;

EID: 84923814773     PISSN: 14714906     EISSN: 14714981     Source Type: Journal    
DOI: 10.1016/j.it.2014.08.007     Document Type: Review
Times cited : (86)

References (180)
  • 2
    • 80052790031 scopus 로고    scopus 로고
    • Antibodies in infectious diseases: polyclonals, monoclonals and niche biotechnology
    • Berry J.D., Gaudet R.G. Antibodies in infectious diseases: polyclonals, monoclonals and niche biotechnology. N. Biotechnol. 2011, 28:489-501.
    • (2011) N. Biotechnol. , vol.28 , pp. 489-501
    • Berry, J.D.1    Gaudet, R.G.2
  • 3
    • 36849087921 scopus 로고    scopus 로고
    • The growth and potential of human antiviral monoclonal antibody therapeutics
    • Marasco W.A., Sui J. The growth and potential of human antiviral monoclonal antibody therapeutics. Nat. Biotechnol. 2007, 25:1421-1434.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1421-1434
    • Marasco, W.A.1    Sui, J.2
  • 4
    • 0035522332 scopus 로고    scopus 로고
    • Maternal antibodies, childhood infections, and autoimmune diseases
    • Zinkernagel R.M. Maternal antibodies, childhood infections, and autoimmune diseases. N. Engl. J. Med. 2001, 345:1331-1335.
    • (2001) N. Engl. J. Med. , vol.345 , pp. 1331-1335
    • Zinkernagel, R.M.1
  • 5
    • 47549116006 scopus 로고    scopus 로고
    • Vaccines: correlates of vaccine-induced immunity
    • Plotkin S.A. Vaccines: correlates of vaccine-induced immunity. Clin. Infect. Dis. 2008, 47:401-409.
    • (2008) Clin. Infect. Dis. , vol.47 , pp. 401-409
    • Plotkin, S.A.1
  • 6
    • 0020596551 scopus 로고
    • Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS)
    • Barre-Sinoussi F., et al. Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS). Science 1983, 220:868-871.
    • (1983) Science , vol.220 , pp. 868-871
    • Barre-Sinoussi, F.1
  • 7
    • 0021840491 scopus 로고
    • HTLV-III-neutralizing antibodies in patients with AIDS and AIDS-related complex
    • Robert-Guroff M., et al. HTLV-III-neutralizing antibodies in patients with AIDS and AIDS-related complex. Nature 1985, 316:72-74.
    • (1985) Nature , vol.316 , pp. 72-74
    • Robert-Guroff, M.1
  • 8
    • 0021838099 scopus 로고
    • Neutralization of human T-lymphotropic virus type III by sera of AIDS and AIDS-risk patients
    • Weiss R.A., et al. Neutralization of human T-lymphotropic virus type III by sera of AIDS and AIDS-risk patients. Nature 1985, 316:69-72.
    • (1985) Nature , vol.316 , pp. 69-72
    • Weiss, R.A.1
  • 9
    • 1542615646 scopus 로고    scopus 로고
    • Identifying epitopes of HIV-1 that induce protective antibodies
    • Zolla-Pazner S. Identifying epitopes of HIV-1 that induce protective antibodies. Nat. Rev. Immunol. 2004, 4:199-210.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 199-210
    • Zolla-Pazner, S.1
  • 10
    • 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. 2009, 361:2209-2220.
    • (2009) N. Engl. J. Med. , vol.361 , pp. 2209-2220
    • Rerks-Ngarm, S.1
  • 11
    • 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. 2012, 366:1275-1286.
    • (2012) N. Engl. J. Med. , vol.366 , pp. 1275-1286
    • Haynes, B.F.1
  • 12
    • 79651469358 scopus 로고    scopus 로고
    • B cell responses to HIV-1 infection and vaccination: pathways to preventing infection
    • Haynes B.F., et al. B cell responses to HIV-1 infection and vaccination: pathways to preventing infection. Trends Mol. Med. 2011, 17:108-116.
    • (2011) Trends Mol. Med. , vol.17 , pp. 108-116
    • Haynes, B.F.1
  • 13
    • 84864345953 scopus 로고    scopus 로고
    • Towards an HIV cure: a global scientific strategy
    • International AIDS Society Scientific Working Group on HIV Cure, et al. Towards an HIV cure: a global scientific strategy. Nat. Rev. Immunol. 2012, 12:607-614.
    • (2012) Nat. Rev. Immunol. , vol.12 , pp. 607-614
  • 14
    • 84883796903 scopus 로고    scopus 로고
    • Antibodies in HIV-1 vaccine development and therapy
    • Klein F., et al. Antibodies in HIV-1 vaccine development and therapy. Science 2013, 341:1199-1204.
    • (2013) Science , vol.341 , pp. 1199-1204
    • Klein, F.1
  • 15
    • 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. 2008, 82:12449-12463.
    • (2008) J. Virol. , vol.82 , pp. 12449-12463
    • Tomaras, G.D.1
  • 16
    • 33744904454 scopus 로고    scopus 로고
    • Neutralizing antibody responses against autologous and heterologous viruses in acute versus chronic human immunodeficiency virus (HIV) infection: evidence for a constraint on the ability of HIV to completely evade neutralizing antibody responses
    • Deeks S.G., et al. Neutralizing antibody responses against autologous and heterologous viruses in acute versus chronic human immunodeficiency virus (HIV) infection: evidence for a constraint on the ability of HIV to completely evade neutralizing antibody responses. J. Virol. 2006, 80:6155-6164.
    • (2006) J. Virol. , vol.80 , pp. 6155-6164
    • Deeks, S.G.1
  • 17
    • 34249940652 scopus 로고    scopus 로고
    • Neutralizing antibody responses in acute human immunodeficiency virus type 1 subtype C infection
    • Gray E.S., et al. Neutralizing antibody responses in acute human immunodeficiency virus type 1 subtype C infection. J. Virol. 2007, 81:6187-6196.
    • (2007) J. Virol. , vol.81 , pp. 6187-6196
    • Gray, E.S.1
  • 18
    • 0030901363 scopus 로고    scopus 로고
    • Autologous and heterologous neutralizing antibody responses following initial seroconversion in human immunodeficiency virus type 1-infected individuals
    • Moog C., et al. Autologous and heterologous neutralizing antibody responses following initial seroconversion in human immunodeficiency virus type 1-infected individuals. J. Virol. 1997, 71:3734-3741.
    • (1997) J. Virol. , vol.71 , pp. 3734-3741
    • Moog, C.1
  • 19
    • 0037389643 scopus 로고    scopus 로고
    • Rapid evolution of the neutralizing antibody response to HIV type 1 infection
    • Richman D.D., et al. Rapid evolution of the neutralizing antibody response to HIV type 1 infection. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:4144-4149.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 4144-4149
    • Richman, D.D.1
  • 20
    • 0037456827 scopus 로고    scopus 로고
    • Antibody neutralization and escape by HIV-1
    • Wei X., et al. Antibody neutralization and escape by HIV-1. Nature 2003, 422:307-312.
    • (2003) Nature , vol.422 , pp. 307-312
    • Wei, X.1
  • 21
    • 29444442970 scopus 로고    scopus 로고
    • Neutralizing antibody responses drive the evolution of human immunodeficiency virus type 1 envelope during recent HIV infection
    • Frost S.D., et al. Neutralizing antibody responses drive the evolution of human immunodeficiency virus type 1 envelope during recent HIV infection. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:18514-18519.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 18514-18519
    • Frost, S.D.1
  • 22
    • 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. 2011, 85:4828-4840.
    • (2011) J. Virol. , vol.85 , pp. 4828-4840
    • Gray, E.S.1
  • 23
    • 79551518897 scopus 로고    scopus 로고
    • Characteristics of the earliest cross-neutralizing antibody response to HIV-1
    • Mikell I., et al. Characteristics of the earliest cross-neutralizing antibody response to HIV-1. PLoS Pathog. 2011, 7:e1001251.
    • (2011) PLoS Pathog. , vol.7
    • Mikell, I.1
  • 24
    • 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. 2008, 82:11651-11668.
    • (2008) J. Virol. , vol.82 , pp. 11651-11668
    • Binley, J.M.1
  • 25
    • 34249950588 scopus 로고    scopus 로고
    • Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors
    • Dhillon A.K., et al. Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors. J. Virol. 2007, 81:6548-6562.
    • (2007) J. Virol. , vol.81 , pp. 6548-6562
    • Dhillon, A.K.1
  • 26
    • 73949084963 scopus 로고    scopus 로고
    • Breadth of human immunodeficiency virus-specific neutralizing activity in sera: clustering analysis and association with clinical variables
    • Doria-Rose N.A., 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.
    • (2010) J. Virol. , vol.84 , pp. 1631-1636
    • Doria-Rose, N.A.1
  • 27
    • 58149517700 scopus 로고    scopus 로고
    • Analysis of neutralization specificities in polyclonal sera derived from human immunodeficiency virus type 1-infected individuals
    • Li Y., et al. Analysis of neutralization specificities in polyclonal sera derived from human immunodeficiency virus type 1-infected individuals. J. Virol. 2009, 83:1045-1059.
    • (2009) J. Virol. , vol.83 , pp. 1045-1059
    • Li, Y.1
  • 28
    • 84892365659 scopus 로고    scopus 로고
    • Prevalence of broadly neutralizing antibody responses during chronic HIV-1 infection
    • Hraber P., et al. Prevalence of broadly neutralizing antibody responses during chronic HIV-1 infection. Aids 2014, 28:163-169.
    • (2014) Aids , vol.28 , pp. 163-169
    • Hraber, P.1
  • 29
    • 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. 2009, 83:7337-7348.
    • (2009) J. Virol. , vol.83 , pp. 7337-7348
    • Simek, M.D.1
  • 30
    • 84902131373 scopus 로고    scopus 로고
    • Early development of broadly neutralizing antibodies in HIV-1-infected infants
    • Goo L., et al. Early development of broadly neutralizing antibodies in HIV-1-infected infants. Nat. Med. 2014, 20:655-658.
    • (2014) Nat. Med. , vol.20 , pp. 655-658
    • Goo, L.1
  • 31
    • 84877618448 scopus 로고    scopus 로고
    • Delineating antibody recognition in polyclonal sera from patterns of HIV-1 isolate neutralization
    • Georgiev I.S., et al. Delineating antibody recognition in polyclonal sera from patterns of HIV-1 isolate neutralization. Science 2013, 340:751-756.
    • (2013) Science , vol.340 , pp. 751-756
    • Georgiev, I.S.1
  • 32
    • 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. 2011, 85:11502-11519.
    • (2011) J. Virol. , vol.85 , pp. 11502-11519
    • Tomaras, G.D.1
  • 33
    • 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. 2010, 6:e1001028.
    • (2010) PLoS Pathog. , vol.6
    • Walker, L.M.1
  • 34
    • 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 2009, 458:636-640.
    • (2009) Nature , vol.458 , pp. 636-640
    • Scheid, J.F.1
  • 35
    • 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. U.S.A. 2012, 109:E3268-E3277.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. E3268-E3277
    • Mouquet, H.1
  • 36
    • 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 2011, 333:1633-1637.
    • (2011) Science , vol.333 , pp. 1633-1637
    • Scheid, J.F.1
  • 37
    • 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. 2012, 86:4688-4692.
    • (2012) J. Virol. , vol.86 , pp. 4688-4692
    • Bonsignori, M.1
  • 38
    • 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. 2012, 209:1469-1479.
    • (2012) J. Exp. Med. , vol.209 , pp. 1469-1479
    • Klein, F.1
  • 39
    • 54149119141 scopus 로고    scopus 로고
    • Avoiding the void: cell-to-cell spread of human viruses
    • Sattentau Q. Avoiding the void: cell-to-cell spread of human viruses. Nat. Rev. Microbiol. 2008, 6:815-826.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 815-826
    • Sattentau, Q.1
  • 40
    • 84897492743 scopus 로고    scopus 로고
    • An autoreactive antibody from an SLE/HIV-1 individual broadly neutralizes HIV-1
    • Bonsignori M., et al. An autoreactive antibody from an SLE/HIV-1 individual broadly neutralizes HIV-1. J. Clin. Invest. 2014, 124:1835-1843.
    • (2014) J. Clin. Invest. , vol.124 , pp. 1835-1843
    • Bonsignori, M.1
  • 41
    • 34248370960 scopus 로고    scopus 로고
    • Antiviral antibodies are necessary for control of simian immunodeficiency virus replication
    • Miller C.J., et al. Antiviral antibodies are necessary for control of simian immunodeficiency virus replication. J. Virol. 2007, 81:5024-5035.
    • (2007) J. Virol. , vol.81 , pp. 5024-5035
    • Miller, C.J.1
  • 42
    • 0037303113 scopus 로고    scopus 로고
    • Effect of humoral immune responses on controlling viremia during primary infection of rhesus monkeys with simian immunodeficiency virus
    • Schmitz J.E., et al. Effect of humoral immune responses on controlling viremia during primary infection of rhesus monkeys with simian immunodeficiency virus. J. Virol. 2003, 77:2165-2173.
    • (2003) J. Virol. , vol.77 , pp. 2165-2173
    • Schmitz, J.E.1
  • 43
    • 84879107855 scopus 로고    scopus 로고
    • B-cell depletion reveals a role for antibodies in the control of chronic HIV-1 infection
    • Huang K.H., et al. B-cell depletion reveals a role for antibodies in the control of chronic HIV-1 infection. Nat. Commun. 2010, 1:102.
    • (2010) Nat. Commun. , vol.1 , pp. 102
    • Huang, K.H.1
  • 44
    • 20444396989 scopus 로고    scopus 로고
    • Combination of HIV-1-specific CD4 Th1 cell responses and IgG2 antibodies is the best predictor for persistence of long-term nonprogression
    • Martinez V., et al. Combination of HIV-1-specific CD4 Th1 cell responses and IgG2 antibodies is the best predictor for persistence of long-term nonprogression. J. Infect. Dis. 2005, 191:2053-2063.
    • (2005) J. Infect. Dis. , vol.191 , pp. 2053-2063
    • Martinez, V.1
  • 45
    • 0034766611 scopus 로고    scopus 로고
    • HIV type 1-specific IgG2 antibodies: markers of helper T cell type 1 response and prognostic marker of long-term nonprogression
    • Ngo-Giang-Huong N., et al. HIV type 1-specific IgG2 antibodies: markers of helper T cell type 1 response and prognostic marker of long-term nonprogression. AIDS Res. Hum. Retroviruses 2001, 17:1435-1446.
    • (2001) AIDS Res. Hum. Retroviruses , vol.17 , pp. 1435-1446
    • Ngo-Giang-Huong, N.1
  • 46
    • 84864055665 scopus 로고    scopus 로고
    • HIV-specific antibodies capable of ADCC are common in breastmilk and are associated with reduced risk of transmission in women with high viral loads
    • Mabuka J., et al. HIV-specific antibodies capable of ADCC are common in breastmilk and are associated with reduced risk of transmission in women with high viral loads. PLoS Pathog. 2012, 8:e1002739.
    • (2012) PLoS Pathog. , vol.8
    • Mabuka, J.1
  • 47
    • 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. 2013, 123:2183-2192.
    • (2013) J. Clin. Invest. , vol.123 , pp. 2183-2192
    • Ackerman, M.E.1
  • 48
    • 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. 1996, 157:2168-2173.
    • (1996) J. Immunol. , vol.157 , pp. 2168-2173
    • Baum, L.L.1
  • 49
    • 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 2007, 449:101-104.
    • (2007) Nature , vol.449 , pp. 101-104
    • Hessell, A.J.1
  • 50
    • 84907379431 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies and viral inducers decrease rebound from HIV-1 latent reservoirs in humanized mice
    • Halper-Stromberg A., et al. Broadly neutralizing antibodies and viral inducers decrease rebound from HIV-1 latent reservoirs in humanized mice. Cell 2014, 158:989-999.
    • (2014) Cell , vol.158 , pp. 989-999
    • Halper-Stromberg, A.1
  • 52
    • 84878440866 scopus 로고    scopus 로고
    • HIV-1 gp41 envelope IgA is frequently elicited after transmission but has an initial short response half-life
    • Yates N.L., et al. HIV-1 gp41 envelope IgA is frequently elicited after transmission but has an initial short response half-life. Mucosal Immunol. 2013, 6:692-703.
    • (2013) Mucosal Immunol. , vol.6 , pp. 692-703
    • Yates, N.L.1
  • 53
    • 68049135892 scopus 로고    scopus 로고
    • Polyclonal B cell differentiation and loss of gastrointestinal tract germinal centers in the earliest stages of HIV-1 infection
    • Levesque M.C., et al. Polyclonal B cell differentiation and loss of gastrointestinal tract germinal centers in the earliest stages of HIV-1 infection. PLoS Med. 2009, 6:e1000107.
    • (2009) PLoS Med. , vol.6
    • Levesque, M.C.1
  • 54
    • 4644289983 scopus 로고    scopus 로고
    • Primary HIV-1 infection is associated with preferential depletion of CD4+ T lymphocytes from effector sites in the gastrointestinal tract
    • Mehandru S., et al. Primary HIV-1 infection is associated with preferential depletion of CD4+ T lymphocytes from effector sites in the gastrointestinal tract. J. Exp. Med. 2004, 200:761-770.
    • (2004) J. Exp. Med. , vol.200 , pp. 761-770
    • Mehandru, S.1
  • 55
    • 84861408993 scopus 로고    scopus 로고
    • Default in plasma and intestinal IgA responses during acute infection by simian immunodeficiency virus
    • Chaoul N., et al. Default in plasma and intestinal IgA responses during acute infection by simian immunodeficiency virus. Retrovirology 2012, 9:43.
    • (2012) Retrovirology , vol.9 , pp. 43
    • Chaoul, N.1
  • 56
    • 0035873475 scopus 로고    scopus 로고
    • Secretory IgA specific for a conserved epitope on gp41 envelope glycoprotein inhibits epithelial transcytosis of HIV-1
    • Alfsen A., et al. Secretory IgA specific for a conserved epitope on gp41 envelope glycoprotein inhibits epithelial transcytosis of HIV-1. J. Immunol. 2001, 166:6257-6265.
    • (2001) J. Immunol. , vol.166 , pp. 6257-6265
    • Alfsen, A.1
  • 57
    • 18844470061 scopus 로고    scopus 로고
    • Intracellular neutralization of HIV transcytosis across tight epithelial barriers by anti-HIV envelope protein dIgA or IgM
    • Bomsel M., et al. Intracellular neutralization of HIV transcytosis across tight epithelial barriers by anti-HIV envelope protein dIgA or IgM. Immunity 1998, 9:277-287.
    • (1998) Immunity , vol.9 , pp. 277-287
    • Bomsel, M.1
  • 58
    • 0034327707 scopus 로고    scopus 로고
    • Mucosal and plasma IgA from HIV-1-exposed uninfected individuals inhibit HIV-1 transcytosis across human epithelial cells
    • Devito C., et al. Mucosal and plasma IgA from HIV-1-exposed uninfected individuals inhibit HIV-1 transcytosis across human epithelial cells. J. Immunol. 2000, 165:5170-5176.
    • (2000) J. Immunol. , vol.165 , pp. 5170-5176
    • Devito, C.1
  • 59
    • 84862080740 scopus 로고    scopus 로고
    • Isolation of HIV-1-neutralizing mucosal monoclonal antibodies from human colostrum
    • Friedman J., et al. Isolation of HIV-1-neutralizing mucosal monoclonal antibodies from human colostrum. PLoS ONE 2012, 7:e37648.
    • (2012) PLoS ONE , vol.7
    • Friedman, J.1
  • 60
    • 69249086612 scopus 로고    scopus 로고
    • HIV-1 gp41-specific monoclonal mucosal IgAs derived from highly exposed but IgG-seronegative individuals block HIV-1 epithelial transcytosis and neutralize CD4(+) cell infection: an IgA gene and functional analysis
    • Tudor D., et al. HIV-1 gp41-specific monoclonal mucosal IgAs derived from highly exposed but IgG-seronegative individuals block HIV-1 epithelial transcytosis and neutralize CD4(+) cell infection: an IgA gene and functional analysis. Mucosal Immunol. 2009, 2:412-426.
    • (2009) Mucosal Immunol. , vol.2 , pp. 412-426
    • Tudor, D.1
  • 61
    • 79951754740 scopus 로고    scopus 로고
    • Immunization with HIV-1 gp41 subunit virosomes induces mucosal antibodies protecting nonhuman primates against vaginal SHIV challenges
    • Bomsel M., et al. Immunization with HIV-1 gp41 subunit virosomes induces mucosal antibodies protecting nonhuman primates against vaginal SHIV challenges. Immunity 2011, 34:269-280.
    • (2011) Immunity , vol.34 , pp. 269-280
    • Bomsel, M.1
  • 62
    • 84903765782 scopus 로고    scopus 로고
    • Abnormal B cell memory subsets dominate HIV-specific responses in infected individuals
    • Kardava L., et al. Abnormal B cell memory subsets dominate HIV-specific responses in infected individuals. J. Clin. Invest. 2014, 124:3252-3262.
    • (2014) J. Clin. Invest. , vol.124 , pp. 3252-3262
    • Kardava, L.1
  • 63
    • 84879284427 scopus 로고    scopus 로고
    • Insights into B cells and HIV-specific B-cell responses in HIV-infected individuals
    • Moir S., Fauci A.S. Insights into B cells and HIV-specific B-cell responses in HIV-infected individuals. Immunol. Rev. 2013, 254:207-224.
    • (2013) Immunol. Rev. , vol.254 , pp. 207-224
    • Moir, S.1    Fauci, A.S.2
  • 64
    • 84888009485 scopus 로고    scopus 로고
    • The HIV-1 envelope protein gp120 impairs B cell proliferation by inducing TGF-beta1 production and FcRL4 expression
    • Jelicic K., et al. The HIV-1 envelope protein gp120 impairs B cell proliferation by inducing TGF-beta1 production and FcRL4 expression. Nat. Immunol. 2013, 14:1256-1265.
    • (2013) Nat. Immunol. , vol.14 , pp. 1256-1265
    • Jelicic, K.1
  • 65
    • 84901609207 scopus 로고    scopus 로고
    • Emerging concepts on T follicular helper cell dynamics in HIV infection
    • Pissani F., Streeck H. Emerging concepts on T follicular helper cell dynamics in HIV infection. Trends Immunol. 2014, 35:278-286.
    • (2014) Trends Immunol. , vol.35 , pp. 278-286
    • Pissani, F.1    Streeck, H.2
  • 66
    • 0037393393 scopus 로고    scopus 로고
    • HIV-1: nature's master of disguise
    • Mascola J.R., Montefiori D.C. HIV-1: nature's master of disguise. Nat. Med. 2003, 9:393-394.
    • (2003) Nat. Med. , vol.9 , pp. 393-394
    • Mascola, J.R.1    Montefiori, D.C.2
  • 67
    • 77952001983 scopus 로고    scopus 로고
    • Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization
    • Binley J.M., et al. Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization. J. Virol. 2010, 84:5637-5655.
    • (2010) J. Virol. , vol.84 , pp. 5637-5655
    • Binley, J.M.1
  • 68
    • 84869155712 scopus 로고    scopus 로고
    • Evolution of an HIV glycan-dependent broadly neutralizing antibody epitope through immune escape
    • Moore P.L., et al. Evolution of an HIV glycan-dependent broadly neutralizing antibody epitope through immune escape. Nat. Med. 2012, 18:1688-1692.
    • (2012) Nat. Med. , vol.18 , pp. 1688-1692
    • Moore, P.L.1
  • 69
    • 0041689676 scopus 로고    scopus 로고
    • Predominant autoantibody production by early human B cell precursors
    • Wardemann H., et al. Predominant autoantibody production by early human B cell precursors. Science 2003, 301:1374-1377.
    • (2003) Science , vol.301 , pp. 1374-1377
    • Wardemann, H.1
  • 70
    • 0037069682 scopus 로고    scopus 로고
    • HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites
    • Kwong P.D., et al. HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature 2002, 420:678-682.
    • (2002) Nature , vol.420 , pp. 678-682
    • Kwong, P.D.1
  • 71
    • 0141521564 scopus 로고    scopus 로고
    • Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1
    • Labrijn A.F., et al. Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1. J. Virol. 2003, 77:10557-10565.
    • (2003) J. Virol. , vol.77 , pp. 10557-10565
    • Labrijn, A.F.1
  • 72
    • 41649090223 scopus 로고    scopus 로고
    • A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies
    • Frey G., et al. A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:3739-3744.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 3739-3744
    • Frey, G.1
  • 73
    • 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. 2003, 77:353-365.
    • (2003) J. Virol. , vol.77 , pp. 353-365
    • Poignard, P.1
  • 74
    • 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. 2006, 80:2515-2528.
    • (2006) J. Virol. , vol.80 , pp. 2515-2528
    • Moore, P.L.1
  • 75
    • 33745203490 scopus 로고    scopus 로고
    • Distribution and three-dimensional structure of AIDS virus envelope spikes
    • Zhu P., et al. Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 2006, 441:847-852.
    • (2006) Nature , vol.441 , pp. 847-852
    • Zhu, P.1
  • 76
    • 66149132686 scopus 로고    scopus 로고
    • Examination of the contributions of size and avidity to the neutralization mechanisms of the anti-HIV antibodies b12 and 4E10
    • Klein J.S., et al. Examination of the contributions of size and avidity to the neutralization mechanisms of the anti-HIV antibodies b12 and 4E10. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:7385-7390.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 7385-7390
    • Klein, J.S.1
  • 77
    • 0027311936 scopus 로고
    • Repertoire of neutralizing human monoclonal antibodies specific for the V3 domain of HIV-1 gp120
    • Gorny M.K., et al. Repertoire of neutralizing human monoclonal antibodies specific for the V3 domain of HIV-1 gp120. J. Immunol. 1993, 150:635-643.
    • (1993) J. Immunol. , vol.150 , pp. 635-643
    • Gorny, M.K.1
  • 78
    • 0027256814 scopus 로고
    • Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali M., et al. Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol. 1993, 67:3978-3988.
    • (1993) J. Virol. , vol.67 , pp. 3978-3988
    • Thali, M.1
  • 79
    • 0025838698 scopus 로고
    • A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals
    • Burton D.R., et al. A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals. Proc. Natl. Acad. Sci. U.S.A. 1991, 88:10134-10137.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10134-10137
    • Burton, D.R.1
  • 80
    • 9044241681 scopus 로고    scopus 로고
    • Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1
    • Trkola A., et al. Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. J. Virol. 1996, 70:1100-1108.
    • (1996) J. Virol. , vol.70 , pp. 1100-1108
    • Trkola, A.1
  • 81
    • 0028155283 scopus 로고
    • Generation of human monoclonal antibodies against HIV-1 proteins; electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization
    • Buchacher A., et al. Generation of human monoclonal antibodies against HIV-1 proteins; electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization. AIDS Res. Hum. Retroviruses 1994, 10:359-369.
    • (1994) AIDS Res. Hum. Retroviruses , vol.10 , pp. 359-369
    • Buchacher, A.1
  • 82
    • 0027378573 scopus 로고
    • A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1
    • Muster T., et al. A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1. J. Virol. 1993, 67:6642-6647.
    • (1993) J. Virol. , vol.67 , pp. 6642-6647
    • Muster, T.1
  • 83
    • 84894173514 scopus 로고    scopus 로고
    • Structural insights on the role of antibodies in HIV-1 Vaccine and therapy
    • West A.P., et al. Structural insights on the role of antibodies in HIV-1 Vaccine and therapy. Cell 2014, 156:633-648.
    • (2014) Cell , vol.156 , pp. 633-648
    • West, A.P.1
  • 84
    • 56349161598 scopus 로고    scopus 로고
    • B-cell tolerance checkpoints in health and autoimmunity
    • Meffre E., Wardemann H. B-cell tolerance checkpoints in health and autoimmunity. Curr. Opin. Immunol. 2008, 20:632-638.
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 632-638
    • Meffre, E.1    Wardemann, H.2
  • 85
    • 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 2009, 326:285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1
  • 86
    • 80052938385 scopus 로고    scopus 로고
    • Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors
    • Bonsignori M., 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.
    • (2011) J. Virol. , vol.85 , pp. 9998-10009
    • Bonsignori, M.1
  • 87
    • 63749100579 scopus 로고    scopus 로고
    • A method for identification of HIV gp140 binding memory B cells in human blood
    • Scheid J.F., et al. A method for identification of HIV gp140 binding memory B cells in human blood. J. Immunol. Methods 2009, 343:65-67.
    • (2009) J. Immunol. Methods , vol.343 , pp. 65-67
    • Scheid, J.F.1
  • 88
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu X., et al. Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 2010, 329:856-861.
    • (2010) Science , vol.329 , pp. 856-861
    • Wu, X.1
  • 89
    • 0034087050 scopus 로고    scopus 로고
    • Characterization of stable, soluble trimers containing complete ectodomains of human immunodeficiency virus type 1 envelope glycoproteins
    • Yang X., et al. Characterization of stable, soluble trimers containing complete ectodomains of human immunodeficiency virus type 1 envelope glycoproteins. J. Virol. 2000, 74:5716-5725.
    • (2000) J. Virol. , vol.74 , pp. 5716-5725
    • Yang, X.1
  • 90
    • 84867427047 scopus 로고    scopus 로고
    • Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA
    • Julien J.P., et al. Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA. Immunol. Rev. 2012, 250:180-198.
    • (2012) Immunol. Rev. , vol.250 , pp. 180-198
    • Julien, J.P.1
  • 91
    • 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 2014, 40:669-680.
    • (2014) Immunity , vol.40 , pp. 669-680
    • Blattner, C.1
  • 92
    • 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 2014, 40:657-668.
    • (2014) Immunity , vol.40 , pp. 657-668
    • Falkowska, E.1
  • 93
    • 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 Rep. 2014, 7:785-795.
    • (2014) Cell Rep. , vol.7 , pp. 785-795
    • Scharf, L.1
  • 94
    • 80052531336 scopus 로고    scopus 로고
    • Memory B cell antibodies to HIV-1 gp140 cloned from individuals infected with clade A and B viruses
    • Mouquet H., et al. Memory B cell antibodies to HIV-1 gp140 cloned from individuals infected with clade A and B viruses. PLoS ONE 2011, 6:e24078.
    • (2011) PLoS ONE , vol.6
    • Mouquet, H.1
  • 95
    • 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 2013, 153:126-138.
    • (2013) Cell , vol.153 , pp. 126-138
    • Klein, F.1
  • 96
    • 77957355961 scopus 로고    scopus 로고
    • Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation
    • Mouquet H., et al. Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation. Nature 2010, 467:591-595.
    • (2010) Nature , vol.467 , pp. 591-595
    • Mouquet, H.1
  • 97
    • 84882589754 scopus 로고    scopus 로고
    • Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies
    • Zhou T., et al. Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies. Immunity 2013, 39:245-258.
    • (2013) Immunity , vol.39 , pp. 245-258
    • Zhou, T.1
  • 98
    • 84862314634 scopus 로고    scopus 로고
    • Polyreactive antibodies in adaptive immune responses to viruses
    • Mouquet H., Nussenzweig M.C. Polyreactive antibodies in adaptive immune responses to viruses. Cell. Mol. Life Sci. 2012, 69:1435-1445.
    • (2012) Cell. Mol. Life Sci. , vol.69 , pp. 1435-1445
    • Mouquet, H.1    Nussenzweig, M.C.2
  • 99
    • 33947635198 scopus 로고    scopus 로고
    • 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
    • Alam S.M., et al. 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.
    • (2007) J. Immunol. , vol.178 , pp. 4424-4435
    • Alam, S.M.1
  • 100
    • 78651388412 scopus 로고    scopus 로고
    • Nonneutralizing HIV-1 gp41 envelope cluster II human monoclonal antibodies show polyreactivity for binding to phospholipids and protein autoantigens
    • Dennison S.M., et al. Nonneutralizing HIV-1 gp41 envelope cluster II human monoclonal antibodies show polyreactivity for binding to phospholipids and protein autoantigens. J. Virol. 2011, 85:1340-1347.
    • (2011) J. Virol. , vol.85 , pp. 1340-1347
    • Dennison, S.M.1
  • 101
    • 80053584837 scopus 로고    scopus 로고
    • Isolation of a human anti-HIV gp41 membrane proximal region neutralizing antibody by antigen-specific single B cell sorting
    • Morris L., 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.
    • (2011) PLoS ONE , vol.6
    • Morris, L.1
  • 102
    • 80055115557 scopus 로고    scopus 로고
    • Cross-reactive HIV-1-neutralizing human monoclonal antibodies identified from a patient with 2F5-like antibodies
    • Zhu Z., et al. Cross-reactive HIV-1-neutralizing human monoclonal antibodies identified from a patient with 2F5-like antibodies. J. Virol. 2011, 85:11401-11408.
    • (2011) J. Virol. , vol.85 , pp. 11401-11408
    • Zhu, Z.1
  • 103
    • 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 2013, 496:469-476.
    • (2013) Nature , vol.496 , pp. 469-476
    • Liao, H.X.1
  • 104
    • 84898463606 scopus 로고    scopus 로고
    • Autoreactivity in HIV-1 broadly neutralizing antibodies: implications for their function and induction by vaccination
    • Verkoczy L., Diaz M. Autoreactivity in HIV-1 broadly neutralizing antibodies: implications for their function and induction by vaccination. Curr. Opin. HIV AIDS 2014, 9:224-234.
    • (2014) Curr. Opin. HIV AIDS , vol.9 , pp. 224-234
    • Verkoczy, L.1    Diaz, M.2
  • 105
    • 80055118908 scopus 로고    scopus 로고
    • Initial antibodies binding to HIV-1 gp41 in acutely infected subjects are polyreactive and highly mutated
    • Liao H.X., et al. Initial antibodies binding to HIV-1 gp41 in acutely infected subjects are polyreactive and highly mutated. J. Exp. Med. 2011, 208:2237-2249.
    • (2011) J. Exp. Med. , vol.208 , pp. 2237-2249
    • Liao, H.X.1
  • 106
    • 84879614980 scopus 로고    scopus 로고
    • Unravelling the mechanisms of durable control of HIV-1
    • Walker B.D., Yu X.G. Unravelling the mechanisms of durable control of HIV-1. Nat. Rev. Immunol. 2013, 13:487-498.
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 487-498
    • Walker, B.D.1    Yu, X.G.2
  • 107
    • 84885401068 scopus 로고    scopus 로고
    • The potential of the human immune system to develop broadly neutralizing HIV-1 antibodies: implications for vaccine development
    • Zhang Y., et al. The potential of the human immune system to develop broadly neutralizing HIV-1 antibodies: implications for vaccine development. Aids 2013, 27:2529-2539.
    • (2013) Aids , vol.27 , pp. 2529-2539
    • Zhang, Y.1
  • 108
    • 58149399396 scopus 로고    scopus 로고
    • Frequency and phenotype of human immunodeficiency virus envelope-specific B cells from patients with broadly cross-neutralizing antibodies
    • Doria-Rose N.A., et al. Frequency and phenotype of human immunodeficiency virus envelope-specific B cells from patients with broadly cross-neutralizing antibodies. J. Virol. 2009, 83:188-199.
    • (2009) J. Virol. , vol.83 , pp. 188-199
    • Doria-Rose, N.A.1
  • 109
    • 77953791222 scopus 로고    scopus 로고
    • Control of HIV-1 in elite suppressors despite ongoing replication and evolution in plasma virus
    • O'Connell K.A., et al. Control of HIV-1 in elite suppressors despite ongoing replication and evolution in plasma virus. J. Virol. 2010, 84:7018-7028.
    • (2010) J. Virol. , vol.84 , pp. 7018-7028
    • O'Connell, K.A.1
  • 110
    • 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 2014, 509:55-62.
    • (2014) Nature , vol.509 , pp. 55-62
    • Doria-Rose, N.A.1
  • 111
    • 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 2014, 158:481-491.
    • (2014) Cell , vol.158 , pp. 481-491
    • Gao, F.1
  • 113
    • 84881252552 scopus 로고    scopus 로고
    • T follicular helper cell dynamics in germinal centers
    • Shulman Z., et al. T follicular helper cell dynamics in germinal centers. Science 2013, 341:673-677.
    • (2013) Science , vol.341 , pp. 673-677
    • Shulman, Z.1
  • 114
    • 84873531162 scopus 로고    scopus 로고
    • Harnessing CD4(+) T cell responses in HIV vaccine development
    • Streeck H., et al. Harnessing CD4(+) T cell responses in HIV vaccine development. Nat. Med. 2013, 19:143-149.
    • (2013) Nat. Med. , vol.19 , pp. 143-149
    • Streeck, H.1
  • 115
    • 84885743368 scopus 로고    scopus 로고
    • Human circulating PD-(+)1CXCR3(-)CXCR5(+) memory Tfh cells are highly functional and correlate with broadly neutralizing HIV antibody responses
    • Locci M., et al. Human circulating PD-(+)1CXCR3(-)CXCR5(+) memory Tfh cells are highly functional and correlate with broadly neutralizing HIV antibody responses. Immunity 2013, 39:758-769.
    • (2013) Immunity , vol.39 , pp. 758-769
    • Locci, M.1
  • 116
    • 84901644301 scopus 로고    scopus 로고
    • Clonal selection in the germinal centre by regulated proliferation and hypermutation
    • Gitlin A.D., et al. Clonal selection in the germinal centre by regulated proliferation and hypermutation. Nature 2014, 509:637-640.
    • (2014) Nature , vol.509 , pp. 637-640
    • Gitlin, A.D.1
  • 117
    • 84876802854 scopus 로고    scopus 로고
    • HIV: roadmaps to a vaccine
    • Mouquet H., Nussenzweig M.C. HIV: roadmaps to a vaccine. Nature 2013, 496:441-442.
    • (2013) Nature , vol.496 , pp. 441-442
    • Mouquet, H.1    Nussenzweig, M.C.2
  • 118
    • 84893831480 scopus 로고    scopus 로고
    • The promise and challenge of high-throughput sequencing of the antibody repertoire
    • Georgiou G., et al. The promise and challenge of high-throughput sequencing of the antibody repertoire. Nat. Biotechnol. 2014, 32:158-168.
    • (2014) Nat. Biotechnol. , vol.32 , pp. 158-168
    • Georgiou, G.1
  • 119
    • 80052942203 scopus 로고    scopus 로고
    • Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    • Wu X., et al. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 2011, 333:1593-1602.
    • (2011) Science , vol.333 , pp. 1593-1602
    • Wu, X.1
  • 120
    • 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. 2013, 9:e1003754.
    • (2013) PLoS Pathog. , vol.9
    • Sok, D.1
  • 121
    • 84872616030 scopus 로고    scopus 로고
    • Somatic populations of PGT135-137 HIV-1-neutralizing antibodies identified by 454 pyrosequencing and bioinformatics
    • Zhu J., et al. Somatic populations of PGT135-137 HIV-1-neutralizing antibodies identified by 454 pyrosequencing and bioinformatics. Front. Microbiol. 2012, 3:315.
    • (2012) Front. Microbiol. , vol.3 , pp. 315
    • Zhu, J.1
  • 122
    • 84876272159 scopus 로고    scopus 로고
    • Mining the antibodyome for HIV-1-neutralizing antibodies with next-generation sequencing and phylogenetic pairing of heavy/light chains
    • Zhu J., et al. Mining the antibodyome for HIV-1-neutralizing antibodies with next-generation sequencing and phylogenetic pairing of heavy/light chains. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:6470-6475.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 6470-6475
    • Zhu, J.1
  • 123
    • 84860759632 scopus 로고    scopus 로고
    • B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study
    • Haynes B.F., et al. B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study. Nat. Biotechnol. 2012, 30:423-433.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 423-433
    • Haynes, B.F.1
  • 124
    • 84878626061 scopus 로고    scopus 로고
    • Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies
    • McGuire A.T., et al. Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies. J. Exp. Med. 2013, 210:655-663.
    • (2013) J. Exp. Med. , vol.210 , pp. 655-663
    • McGuire, A.T.1
  • 125
    • 84877609579 scopus 로고    scopus 로고
    • Rational HIV immunogen design to target specific germline B cell receptors
    • Jardine J., et al. Rational HIV immunogen design to target specific germline B cell receptors. Science 2013, 340:711-716.
    • (2013) Science , vol.340 , pp. 711-716
    • Jardine, J.1
  • 126
    • 84919949772 scopus 로고    scopus 로고
    • HIV-1 envelope gp41 antibodies can originate from terminal ileum B cells that share cross-reactivity with commensal bacteria
    • Trama A.M., et al. HIV-1 envelope gp41 antibodies can originate from terminal ileum B cells that share cross-reactivity with commensal bacteria. Cell Host Microbe 2014, 16:215-226.
    • (2014) Cell Host Microbe , vol.16 , pp. 215-226
    • Trama, A.M.1
  • 128
    • 33646780263 scopus 로고    scopus 로고
    • Antibody polyspecificity and neutralization of HIV-1: a hypothesis
    • Haynes B.F., et al. Antibody polyspecificity and neutralization of HIV-1: a hypothesis. Hum. Antibodies 2005, 14:59-67.
    • (2005) Hum. Antibodies , vol.14 , pp. 59-67
    • Haynes, B.F.1
  • 129
    • 79957726572 scopus 로고    scopus 로고
    • Role of immune mechanisms in induction of HIV-1 broadly neutralizing antibodies
    • Verkoczy L., et al. Role of immune mechanisms in induction of HIV-1 broadly neutralizing antibodies. Curr. Opin. Immunol. 2011, 23:383-390.
    • (2011) Curr. Opin. Immunol. , vol.23 , pp. 383-390
    • Verkoczy, L.1
  • 130
    • 84880667257 scopus 로고    scopus 로고
    • Common tolerance mechanisms, but distinct cross-reactivities associated with gp41 and lipids, limit production of HIV-1 broad neutralizing antibodies 2F5 and 4E10
    • Chen Y., et al. Common tolerance mechanisms, but distinct cross-reactivities associated with gp41 and lipids, limit production of HIV-1 broad neutralizing antibodies 2F5 and 4E10. J. Immunol. 2013, 191:1260-1275.
    • (2013) J. Immunol. , vol.191 , pp. 1260-1275
    • Chen, Y.1
  • 131
    • 80053529030 scopus 로고    scopus 로고
    • Rescue of HIV-1 broad neutralizing antibody-expressing B Cells in 2F5 VH × VL knockin mice reveals multiple tolerance controls
    • Verkoczy L., et al. Rescue of HIV-1 broad neutralizing antibody-expressing B Cells in 2F5 VH × VL knockin mice reveals multiple tolerance controls. J. Immunol. 2011, 187:3785-3797.
    • (2011) J. Immunol. , vol.187 , pp. 3785-3797
    • Verkoczy, L.1
  • 132
    • 76249083814 scopus 로고    scopus 로고
    • Autoreactivity in an HIV-1 broadly reactive neutralizing antibody variable region heavy chain induces immunologic tolerance
    • Verkoczy L., et al. Autoreactivity in an HIV-1 broadly reactive neutralizing antibody variable region heavy chain induces immunologic tolerance. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:181-186.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 181-186
    • Verkoczy, L.1
  • 133
    • 33847278450 scopus 로고    scopus 로고
    • Autoreactivity in human IgG+ memory B cells
    • Tiller T., et al. Autoreactivity in human IgG+ memory B cells. Immunity 2007, 26:205-213.
    • (2007) Immunity , vol.26 , pp. 205-213
    • Tiller, T.1
  • 134
    • 84874562109 scopus 로고    scopus 로고
    • Identification of autoantigens recognized by the 2F5 and 4E10 broadly neutralizing HIV-1 antibodies
    • Yang G., et al. Identification of autoantigens recognized by the 2F5 and 4E10 broadly neutralizing HIV-1 antibodies. J. Exp. Med. 2013, 210:241-256.
    • (2013) J. Exp. Med. , vol.210 , pp. 241-256
    • Yang, G.1
  • 135
    • 84883348588 scopus 로고    scopus 로고
    • Induction of HIV-1 broad neutralizing antibodies in 2F5 knock-in mice: selection against membrane proximal external region-associated autoreactivity limits T-dependent responses
    • Verkoczy L., et al. Induction of HIV-1 broad neutralizing antibodies in 2F5 knock-in mice: selection against membrane proximal external region-associated autoreactivity limits T-dependent responses. J. Immunol. 2013, 191:2538-2550.
    • (2013) J. Immunol. , vol.191 , pp. 2538-2550
    • Verkoczy, L.1
  • 136
    • 84856371864 scopus 로고    scopus 로고
    • Enhanced HIV-1 neutralization by antibody heteroligation
    • Mouquet H., et al. Enhanced HIV-1 neutralization by antibody heteroligation. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:875-880.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 875-880
    • Mouquet, H.1
  • 137
    • 84860727717 scopus 로고    scopus 로고
    • International network for comparison of HIV neutralization assays: the NeutNet report II
    • Heyndrickx L., et al. International network for comparison of HIV neutralization assays: the NeutNet report II. PLoS ONE 2012, 7:e36438.
    • (2012) PLoS ONE , vol.7
    • Heyndrickx, L.1
  • 138
    • 84883003232 scopus 로고    scopus 로고
    • Evidence for a continuous drift of the HIV-1 species towards higher resistance to neutralizing antibodies over the course of the epidemic
    • Bouvin-Pley M., et al. Evidence for a continuous drift of the HIV-1 species towards higher resistance to neutralizing antibodies over the course of the epidemic. PLoS Pathog. 2013, 9:e1003477.
    • (2013) PLoS Pathog. , vol.9
    • Bouvin-Pley, M.1
  • 139
    • 77956425857 scopus 로고    scopus 로고
    • Adaptation of HIV-1 envelope gp120 to humoral immunity at a population level
    • Bunnik E.M., et al. Adaptation of HIV-1 envelope gp120 to humoral immunity at a population level. Nat. Med. 2010, 16:995-997.
    • (2010) Nat. Med. , vol.16 , pp. 995-997
    • Bunnik, E.M.1
  • 140
    • 79960385535 scopus 로고    scopus 로고
    • Activity of broadly neutralizing antibodies, including PG9, PG16, and VRC01, against recently transmitted subtype B HIV-1 variants from early and late in the epidemic
    • Euler Z., et al. Activity of broadly neutralizing antibodies, including PG9, PG16, and VRC01, against recently transmitted subtype B HIV-1 variants from early and late in the epidemic. J. Virol. 2011, 85:7236-7245.
    • (2011) J. Virol. , vol.85 , pp. 7236-7245
    • Euler, Z.1
  • 141
    • 77949412821 scopus 로고    scopus 로고
    • Virological synapse-mediated spread of human immunodeficiency virus type 1 between T cells is sensitive to entry inhibition
    • Martin N., et al. Virological synapse-mediated spread of human immunodeficiency virus type 1 between T cells is sensitive to entry inhibition. J. Virol. 2010, 84:3516-3527.
    • (2010) J. Virol. , vol.84 , pp. 3516-3527
    • Martin, N.1
  • 142
    • 84890824652 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies that inhibit HIV-1 cell to cell transmission
    • Malbec M., et al. Broadly neutralizing antibodies that inhibit HIV-1 cell to cell transmission. J. Exp. Med. 2013, 210:2813-2821.
    • (2013) J. Exp. Med. , vol.210 , pp. 2813-2821
    • Malbec, M.1
  • 143
    • 84893519255 scopus 로고    scopus 로고
    • High multiplicity HIV-1 infection and neutralizing antibody evasion mediated by the macrophage-T cell virological synapse
    • Duncan C.J., et al. High multiplicity HIV-1 infection and neutralizing antibody evasion mediated by the macrophage-T cell virological synapse. J. Virol. 2013, 88:2025-2034.
    • (2013) J. Virol. , vol.88 , pp. 2025-2034
    • Duncan, C.J.1
  • 144
    • 84868578424 scopus 로고    scopus 로고
    • Neutralizing antibodies inhibit HIV-1 transfer from primary dendritic cells to autologous CD4 T lymphocytes
    • Su B., et al. Neutralizing antibodies inhibit HIV-1 transfer from primary dendritic cells to autologous CD4 T lymphocytes. Blood 2012, 120:3708-3717.
    • (2012) Blood , vol.120 , pp. 3708-3717
    • Su, B.1
  • 145
    • 84870510055 scopus 로고    scopus 로고
    • Inhibitory effect of HIV-specific neutralizing IgA on mucosal transmission of HIV in humanized mice
    • Hur E.M., et al. Inhibitory effect of HIV-specific neutralizing IgA on mucosal transmission of HIV in humanized mice. Blood 2012, 120:4571-4582.
    • (2012) Blood , vol.120 , pp. 4571-4582
    • Hur, E.M.1
  • 146
    • 38449097264 scopus 로고    scopus 로고
    • Inhibition of HIV-1 infectivity and epithelial cell transfer by human monoclonal IgG and IgA antibodies carrying the b12V region
    • Mantis N.J., et al. Inhibition of HIV-1 infectivity and epithelial cell transfer by human monoclonal IgG and IgA antibodies carrying the b12V region. J. Immunol. 2007, 179:3144-3152.
    • (2007) J. Immunol. , vol.179 , pp. 3144-3152
    • Mantis, N.J.1
  • 147
    • 77951630373 scopus 로고    scopus 로고
    • GP41-specific antibody blocks cell-free HIV type 1 transcytosis through human rectal mucosa and model colonic epithelium
    • Shen R., et al. GP41-specific antibody blocks cell-free HIV type 1 transcytosis through human rectal mucosa and model colonic epithelium. J. Immunol. 2010, 184:3648-3655.
    • (2010) J. Immunol. , vol.184 , pp. 3648-3655
    • Shen, R.1
  • 148
    • 84879122811 scopus 로고    scopus 로고
    • Anti-HIV IgA isotypes: differential virion capture and inhibition of transcytosis are linked to prevention of mucosal R5 SHIV transmission
    • Watkins J.D., et al. Anti-HIV IgA isotypes: differential virion capture and inhibition of transcytosis are linked to prevention of mucosal R5 SHIV transmission. Aids 2013, 27:F13-F20.
    • (2013) Aids , vol.27 , pp. F13-F20
    • Watkins, J.D.1
  • 149
    • 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. 2009, 15:951-954.
    • (2009) Nat. Med. , vol.15 , pp. 951-954
    • Hessell, A.J.1
  • 150
    • 67249131966 scopus 로고    scopus 로고
    • Broadly neutralizing human anti-HIV antibody 2G12 is effective in protection against mucosal SHIV challenge even at low serum neutralizing titers
    • Hessell A.J., et al. Broadly neutralizing human anti-HIV antibody 2G12 is effective in protection against mucosal SHIV challenge even at low serum neutralizing titers. PLoS Pathog. 2009, 5:e1000433.
    • (2009) PLoS Pathog. , vol.5
    • Hessell, A.J.1
  • 151
    • 73949154006 scopus 로고    scopus 로고
    • Broadly neutralizing monoclonal antibodies 2F5 and 4E10 directed against the human immunodeficiency virus type 1 gp41 membrane-proximal external region protect against mucosal challenge by simian-human immunodeficiency virus SHIVBa-L
    • Hessell A.J., et al. Broadly neutralizing monoclonal antibodies 2F5 and 4E10 directed against the human immunodeficiency virus type 1 gp41 membrane-proximal external region protect against mucosal challenge by simian-human immunodeficiency virus SHIVBa-L. J. Virol. 2010, 84:1302-1313.
    • (2010) J. Virol. , vol.84 , pp. 1302-1313
    • Hessell, A.J.1
  • 152
    • 84890899378 scopus 로고    scopus 로고
    • Protective effect of vaginal application of neutralizing and nonneutralizing inhibitory antibodies against vaginal SHIV challenge in macaques
    • Moog C., et al. Protective effect of vaginal application of neutralizing and nonneutralizing inhibitory antibodies against vaginal SHIV challenge in macaques. Mucosal Immunol. 2014, 7:46-56.
    • (2014) Mucosal Immunol. , vol.7 , pp. 46-56
    • Moog, C.1
  • 153
    • 79953653241 scopus 로고    scopus 로고
    • An anti-HIV-1 V3 loop antibody fully protects cross-clade and elicits T-cell immunity in macaques mucosally challenged with an R5 clade C SHIV
    • Watkins J.D., et al. An anti-HIV-1 V3 loop antibody fully protects cross-clade and elicits T-cell immunity in macaques mucosally challenged with an R5 clade C SHIV. PLoS ONE 2011, 6:e18207.
    • (2011) PLoS ONE , vol.6
    • Watkins, J.D.1
  • 154
    • 0033951746 scopus 로고    scopus 로고
    • Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus by passive infusion of neutralizing antibodies
    • Mascola J.R., et al. Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus by passive infusion of neutralizing antibodies. Nat. Med. 2000, 6:207-210.
    • (2000) Nat. Med. , vol.6 , pp. 207-210
    • Mascola, J.R.1
  • 155
    • 36749022726 scopus 로고    scopus 로고
    • Neutralizing monoclonal antibodies to human immunodeficiency virus type 1 do not inhibit viral transcytosis through mucosal epithelial cells
    • Chomont N., et al. Neutralizing monoclonal antibodies to human immunodeficiency virus type 1 do not inhibit viral transcytosis through mucosal epithelial cells. Virology 2008, 370:246-254.
    • (2008) Virology , vol.370 , pp. 246-254
    • Chomont, N.1
  • 156
    • 84888272954 scopus 로고    scopus 로고
    • The Neonatal Fc receptor (FcRn) enhances human immunodeficiency virus type 1 (HIV-1) transcytosis across epithelial cells
    • Gupta S., et al. The Neonatal Fc receptor (FcRn) enhances human immunodeficiency virus type 1 (HIV-1) transcytosis across epithelial cells. PLoS Pathog. 2013, 9:e1003776.
    • (2013) PLoS Pathog. , vol.9
    • Gupta, S.1
  • 157
    • 84907983318 scopus 로고    scopus 로고
    • Enhanced neonatal Fc receptor function improves protection against primate SHIV infection
    • Ko S.Y., et al. Enhanced neonatal Fc receptor function improves protection against primate SHIV infection. Nature 2014, 10.1038/nature13612.
    • (2014) Nature
    • Ko, S.Y.1
  • 158
    • 0033952103 scopus 로고    scopus 로고
    • Human neutralizing monoclonal antibodies of the IgG1 subtype protect against mucosal simian-human immunodeficiency virus infection
    • Baba T.W., et al. Human neutralizing monoclonal antibodies of the IgG1 subtype protect against mucosal simian-human immunodeficiency virus infection. Nat. Med. 2000, 6:200-206.
    • (2000) Nat. Med. , vol.6 , pp. 200-206
    • Baba, T.W.1
  • 159
    • 0032947286 scopus 로고    scopus 로고
    • Protection of macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies
    • Mascola J.R., et al. Protection of macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies. J. Virol. 1999, 73:4009-4018.
    • (1999) J. Virol. , vol.73 , pp. 4009-4018
    • Mascola, J.R.1
  • 160
    • 77957820631 scopus 로고    scopus 로고
    • Passive neutralizing antibody controls SHIV viremia and enhances B cell responses in infant macaques
    • Ng C.T., et al. Passive neutralizing antibody controls SHIV viremia and enhances B cell responses in infant macaques. Nat. Med. 2010, 16:1117-1119.
    • (2010) Nat. Med. , vol.16 , pp. 1117-1119
    • Ng, C.T.1
  • 161
    • 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. 2001, 75:8340-8347.
    • (2001) J. Virol. , vol.75 , pp. 8340-8347
    • Parren, P.W.1
  • 162
    • 0032907674 scopus 로고    scopus 로고
    • Neutralizing antibody directed against the HIV-1 envelope glycoprotein can completely block HIV-1/SIV chimeric virus infections of macaque monkeys
    • Shibata R., et al. Neutralizing antibody directed against the HIV-1 envelope glycoprotein can completely block HIV-1/SIV chimeric virus infections of macaque monkeys. Nat. Med. 1999, 5:204-210.
    • (1999) Nat. Med. , vol.5 , pp. 204-210
    • Shibata, R.1
  • 163
    • 84885338257 scopus 로고    scopus 로고
    • HIV-1 suppression and durable control by combining single broadly neutralizing antibodies and antiretroviral drugs in humanized mice
    • Horwitz J.A., et al. HIV-1 suppression and durable control by combining single broadly neutralizing antibodies and antiretroviral drugs in humanized mice. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:16538-16543.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 16538-16543
    • Horwitz, J.A.1
  • 164
    • 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 2012, 492:118-122.
    • (2012) Nature , vol.492 , pp. 118-122
    • Klein, F.1
  • 165
    • 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. U.S.A. 2012, 109:18921-18925.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 18921-18925
    • Moldt, B.1
  • 166
    • 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 2013, 503:277-280.
    • (2013) Nature , vol.503 , pp. 277-280
    • Shingai, M.1
  • 167
    • 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 2013, 503:224-228.
    • (2013) Nature , vol.503 , pp. 224-228
    • Barouch, D.H.1
  • 168
    • 35148864699 scopus 로고    scopus 로고
    • Adjunctive passive immunotherapy in human immunodeficiency virus type 1-infected individuals treated with antiviral therapy during acute and early infection
    • Mehandru S., et al. Adjunctive passive immunotherapy in human immunodeficiency virus type 1-infected individuals treated with antiviral therapy during acute and early infection. J. Virol. 2007, 81:11016-11031.
    • (2007) J. Virol. , vol.81 , pp. 11016-11031
    • Mehandru, S.1
  • 169
    • 20944446452 scopus 로고    scopus 로고
    • Delay of HIV-1 rebound after cessation of antiretroviral therapy through passive transfer of human neutralizing antibodies
    • Trkola A., et al. Delay of HIV-1 rebound after cessation of antiretroviral therapy through passive transfer of human neutralizing antibodies. Nat. Med. 2005, 11:615-622.
    • (2005) Nat. Med. , vol.11 , pp. 615-622
    • Trkola, A.1
  • 170
    • 84900389177 scopus 로고    scopus 로고
    • HIV monoclonal antibodies: a new opportunity to further reduce mother-to-child HIV transmission
    • Voronin Y., et al. HIV monoclonal antibodies: a new opportunity to further reduce mother-to-child HIV transmission. PLoS Med. 2014, 11:e1001616.
    • (2014) PLoS Med. , vol.11
    • Voronin, Y.1
  • 171
    • 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 2013, 342:1477-1483.
    • (2013) Science , vol.342 , pp. 1477-1483
    • Julien, J.P.1
  • 172
    • 51349162563 scopus 로고    scopus 로고
    • Molecular architecture of native HIV-1 gp120 trimers
    • Liu J., et al. Molecular architecture of native HIV-1 gp120 trimers. Nature 2008, 455:109-113.
    • (2008) Nature , vol.455 , pp. 109-113
    • Liu, J.1
  • 173
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - a visualization system for exploratory research and analysis
    • Pettersen E.F., et al. UCSF Chimera - a visualization system for exploratory research and analysis. J. Comput. Chem. 2004, 25:1605-1612.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 174
    • 84875034460 scopus 로고    scopus 로고
    • Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9
    • Julien J.P., et al. Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:4351-4356.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 4351-4356
    • Julien, J.P.1
  • 175
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    • McLellan J.S., et al. Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 2011, 480:336-343.
    • (2011) Nature , vol.480 , pp. 336-343
    • McLellan, J.S.1
  • 176
    • 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 2011, 334:1097-1103.
    • (2011) Science , vol.334 , pp. 1097-1103
    • Pejchal, R.1
  • 177
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou T., et al. Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 2010, 329:811-817.
    • (2010) Science , vol.329 , pp. 811-817
    • Zhou, T.1
  • 178
    • 78449264099 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System
    • The PyMOL Molecular Graphics System, (1.2r3pre edn)
    • Schrödinger, L. (2011) The PyMOL Molecular Graphics System. (1.2r3pre edn), The PyMOL Molecular Graphics System.
    • (2011)
    • Schrödinger, L.1
  • 179
    • 84904124681 scopus 로고    scopus 로고
    • A critical question for HIV vaccine development: which antibodies to induce?
    • Zolla-Pazner S. A critical question for HIV vaccine development: which antibodies to induce?. Science 2014, 345:167-168.
    • (2014) Science , vol.345 , pp. 167-168
    • Zolla-Pazner, S.1
  • 180
    • 21344434534 scopus 로고    scopus 로고
    • Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies
    • Haynes B.F., et al. Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies. Science 2005, 308:1906-1908.
    • (2005) Science , vol.308 , pp. 1906-1908
    • Haynes, B.F.1


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