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Volumn 33, Issue 8, 2017, Pages 859-868

HIV-1 Consensus Envelope-Induced Broadly Binding Antibodies

Author keywords

ADCC; antibody mediated immunity; HIV; monoclonal; vaccine design

Indexed keywords

CON 6 PROTEIN; DODECYL SULFATE SODIUM; GLYCOPROTEIN GP 120; IMMUNOGLOBULIN G1 ANTIBODY; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 13D7; MONOCLONAL ANTIBODY 16H3; MONOCLONAL ANTIBODY 18F11; MONOCLONAL ANTIBODY 3B3; REAGENT; RECOMBINANT PROTEIN; RECOMBINANT VIRUS ENVELOPE PROTEIN; UNCLASSIFIED DRUG; VIRAL PROTEIN; VIRUS ENVELOPE PROTEIN; EPITOPE; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS VACCINE;

EID: 85027078808     PISSN: 08892229     EISSN: 19318405     Source Type: Journal    
DOI: 10.1089/aid.2016.0294     Document Type: Article
Times cited : (11)

References (58)
  • 1
    • 84952980275 scopus 로고    scopus 로고
    • Structural constraints of vaccine-induced tier-2 autologous HIV neutralizing antibodies targeting the receptor-binding site
    • Bradley T, Fera D, Bhiman J, et al.: Structural constraints of vaccine-induced tier-2 autologous HIV neutralizing antibodies targeting the receptor-binding site. Cell Rep 2016;14: 43-54.
    • (2016) Cell Rep , vol.14 , pp. 43-54
    • Bradley, T.1    Fera, D.2    Bhiman, J.3
  • 2
    • 84859393693 scopus 로고    scopus 로고
    • Immunecorrelates analysis of an HIV-1 vaccine efficacy trial
    • Haynes BF, Gilbert PB, McElrath MJ, et al.: Immunecorrelates 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    Gilbert, P.B.2    McElrath, M.J.3
  • 3
    • 84860759632 scopus 로고    scopus 로고
    • B-celllineage immunogen design in vaccine development with HIV-1 as a case study
    • Haynes BF, Kelsoe G, Harrison SC, Kepler TB: B-celllineage 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    Kelsoe, G.2    Harrison, S.C.3    Kepler, T.B.4
  • 4
    • 84942134414 scopus 로고    scopus 로고
    • Murine antibody responses to cleaved soluble HIV-1 envelope trimers are highly restricted in specificity
    • Hu JK, Crampton JC, Cupo A, et al.: Murine antibody responses to cleaved soluble HIV-1 envelope trimers are highly restricted in specificity. J Virol 2015;89:10383-10398.
    • (2015) J Virol , vol.89 , pp. 10383-10398
    • Hu, J.K.1    Crampton, J.C.2    Cupo, A.3
  • 5
    • 84877609579 scopus 로고    scopus 로고
    • Rational HIV immunogen design to target specific germline B cell receptors
    • Jardine J, Julien JP, Menis S, 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    Julien, J.P.2    Menis, S.3
  • 6
    • 67650741139 scopus 로고    scopus 로고
    • Structural and immunogenicity studies of a cleaved, stabilized envelope trimer derived from subtype A HIV-1
    • Kang YK, Andjelic S, Binley JM, et al.: Structural and immunogenicity studies of a cleaved, stabilized envelope trimer derived from subtype A HIV-1. Vaccine 2009;27: 5120-5132.
    • (2009) Vaccine , vol.27 , pp. 5120-5132
    • Kang, Y.K.1    Andjelic, S.2    Binley, J.M.3
  • 7
    • 73349094086 scopus 로고    scopus 로고
    • Vaccination with ALVAC and AIDSVAX to prevent HIV-1 infection in Thailand
    • Rerks-Ngarm S, Pitisuttithum P, Nitayaphan 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    Pitisuttithum, P.2    Nitayaphan, S.3
  • 8
    • 84940192994 scopus 로고    scopus 로고
    • HIV-1 VACCINES. Diversion of HIV-1 vaccine-induced immunity by gp41-microbiota cross-reactive antibodies
    • Williams WB, Liao HX, Moody MA, et al.: HIV-1 VACCINES. Diversion of HIV-1 vaccine-induced immunity by gp41-microbiota cross-reactive antibodies. Science 2015;349: aab1253.
    • (2015) Science , vol.349 , pp. aab1253
    • Williams, W.B.1    Liao, H.X.2    Moody, M.A.3
  • 9
    • 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, Hwang KK, Chen X, et al.: Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors. J Virol 2011;85: 9998-10009.
    • (2011) J Virol , vol.85 , pp. 9998-10009
    • Bonsignori, M.1    Hwang, K.K.2    Chen, X.3
  • 10
    • 84897492743 scopus 로고    scopus 로고
    • An autoreactive antibody from an SLE/HIV-1 individual broadly neutralizes HIV-1
    • Bonsignori M, Wiehe K, Grimm SK, 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    Wiehe, K.2    Grimm, S.K.3
  • 11
    • 84959296091 scopus 로고    scopus 로고
    • Maturation pathway from germline to broad HIV-1 neutralizer of a CD4-Mimic antibody
    • Bonsignori M, Zhou T, Sheng Z, et al.: Maturation pathway from germline to broad HIV-1 neutralizer of a CD4-Mimic antibody. Cell 2016;165:449-463.
    • (2016) Cell , vol.165 , pp. 449-463
    • Bonsignori, M.1    Zhou, T.2    Sheng, Z.3
  • 12
    • 12444291017 scopus 로고    scopus 로고
    • Antibody domain exchange is an immunological solution to carbohydrate cluster recognition
    • Calarese DA, Scanlan CN, Zwick MB, et al.: Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 2003;300:2065-2071.
    • (2003) Science , vol.300 , pp. 2065-2071
    • Calarese, D.A.1    Scanlan, C.N.2    Zwick, M.B.3
  • 13
    • 84953896553 scopus 로고    scopus 로고
    • New member of the V1V2-Directed CAP256-VRC26 lineage that shows increased breadth and exceptional potency
    • Doria-Rose NA, Bhiman JN, Roark RS, et al.: New member of the V1V2-Directed CAP256-VRC26 lineage that shows increased breadth and exceptional potency. J Virol 2015;90:76-91.
    • (2015) J Virol , vol.90 , pp. 76-91
    • Doria-Rose, N.A.1    Bhiman, J.N.2    Roark, R.S.3
  • 14
    • 84963620358 scopus 로고    scopus 로고
    • Affinity maturation of a potent family of HIV antibodies is primarily focused on accommodating or avoiding glycans
    • Garces F, Lee JH, de Val N, et al.: Affinity maturation of a potent family of HIV antibodies is primarily focused on accommodating or avoiding glycans. Immunity 2015;43: 1053-1063.
    • (2015) Immunity , vol.43 , pp. 1053-1063
    • Garces, F.1    Lee, J.H.2    De Val, N.3
  • 15
    • 84876797103 scopus 로고    scopus 로고
    • Co-evolution of a broadly neutralizing HIV-1 antibody and founder virus
    • Liao HX, Lynch R, Zhou T, 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    Lynch, R.2    Zhou, T.3
  • 16
    • 82255179322 scopus 로고    scopus 로고
    • A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield
    • Pejchal R, Doores KJ, Walker LM, 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    Doores, K.J.2    Walker, L.M.3
  • 17
    • 84899909771 scopus 로고    scopus 로고
    • Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike
    • Scharf L, Scheid JF, Lee JH, 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    Scheid, J.F.2    Lee, J.H.3
  • 18
    • 84917705974 scopus 로고    scopus 로고
    • Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex
    • Sok D, van Gils MJ, Pauthner M, et al.: Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex. Proc Natl Acad Sci U S A 2014; 111:17624-17629.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 17624-17629
    • Sok, D.1    Van Gils, M.J.2    Pauthner, M.3
  • 19
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker LM, Huber M, Doores KJ, et al.: Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 2011;477:466-470.
    • (2011) Nature , vol.477 , pp. 466-470
    • Walker, L.M.1    Huber, M.2    Doores, K.J.3
  • 20
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, Phogat SK, Chan-Hui PY, et al.: Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 2009;326:285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1    Phogat, S.K.2    Chan-Hui, P.Y.3
  • 21
    • 84872616030 scopus 로고    scopus 로고
    • Somatic populations of PGT135-137 HIV-1-neutralizing antibodies identified by 454 pyrosequencing and bioinformatics
    • Zhu J, O'Dell S, Ofek G, 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    O'Dell, S.2    Ofek, G.3
  • 22
    • 80055115557 scopus 로고    scopus 로고
    • Cross-reactive HIV-1-neutralizing human monoclonal antibodies identified from a patient with 2F5-like antibodies
    • Zhu Z, Qin HR, Chen W, 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    Qin, H.R.2    Chen, W.3
  • 23
    • 33750743141 scopus 로고    scopus 로고
    • Antibody binding is a dominant determinant of the efficiency of human immunodeficiency virus type 1 neutralization
    • Yang X, Lipchina I, Cocklin S, Chaiken I, Sodroski J: Antibody binding is a dominant determinant of the efficiency of human immunodeficiency virus type 1 neutralization. J Virol 2006;80:11404-11408.
    • (2006) J Virol , vol.80 , pp. 11404-11408
    • Yang, X.1    Lipchina, I.2    Cocklin, S.3    Chaiken, I.4    Sodroski, J.5
  • 24
    • 84897521911 scopus 로고    scopus 로고
    • Capacity for infectious HIV-1 virion capture differs by envelope antibody specificity
    • Liu P, Williams LD, Shen X, et al.: Capacity for infectious HIV-1 virion capture differs by envelope antibody specificity. J Virol 2014;88:5165-5170.
    • (2014) J Virol , vol.88 , pp. 5165-5170
    • Liu, P.1    Williams, L.D.2    Shen, X.3
  • 25
    • 84867902474 scopus 로고    scopus 로고
    • Antibodydependent cellular cytotoxicity-mediating antibodies from an HIV-1 vaccine efficacy trial target multiple epitopes and preferentially use the VH1 gene family
    • Bonsignori M, Pollara J, Moody MA, et al.: Antibodydependent cellular cytotoxicity-mediating antibodies from an HIV-1 vaccine efficacy trial target multiple epitopes and preferentially use the VH1 gene family. J Virol 2012;86: 11521-11532.
    • (2012) J Virol , vol.86 , pp. 11521-11532
    • Bonsignori, M.1    Pollara, J.2    Moody, M.A.3
  • 26
    • 79960342938 scopus 로고    scopus 로고
    • An HIV-1 gp120 envelope human monoclonal antibody that recognizes a C1 conformational epitope mediates potent antibodydependent cellular cytotoxicity (ADCC) activity and defines a common ADCC epitope in human HIV-1 serum
    • Ferrari G, Pollara J, Kozink D, et al.: An HIV-1 gp120 envelope human monoclonal antibody that recognizes a C1 conformational epitope mediates potent antibodydependent cellular cytotoxicity (ADCC) activity and defines a common ADCC epitope in human HIV-1 serum. J Virol 2011;85:7029-7036.
    • (2011) J Virol , vol.85 , pp. 7029-7036
    • Ferrari, G.1    Pollara, J.2    Kozink, D.3
  • 27
    • 84888991613 scopus 로고    scopus 로고
    • Epitope specificity of human immunodeficiency virus-1 antibody dependent cellular cytotoxicity [ADCC] responses
    • Pollara J, Bonsignori M, Moody MA, Pazgier M, Haynes BF, Ferrari G: Epitope specificity of human immunodeficiency virus-1 antibody dependent cellular cytotoxicity [ADCC] responses. Curr HIV Res 2013;11:378-387.
    • (2013) Curr HIV Res , vol.11 , pp. 378-387
    • Pollara, J.1    Bonsignori, M.2    Moody, M.A.3    Pazgier, M.4    Haynes, B.F.5    Ferrari, G.6
  • 28
    • 70350134276 scopus 로고    scopus 로고
    • Cross-reactive monoclonal antibodies to multiple HIV-1 subtype and SIVcpz envelope glycoproteins
    • Gao F, Scearce RM, Alam SM, et al.: Cross-reactive monoclonal antibodies to multiple HIV-1 subtype and SIVcpz envelope glycoproteins. Virology 2009;394:91-98.
    • (2009) Virology , vol.394 , pp. 91-98
    • Gao, F.1    Scearce, R.M.2    Alam, S.M.3
  • 29
    • 80053459912 scopus 로고    scopus 로고
    • Envelope deglycosylation enhances antigenicity of HIV-1 gp41 epitopes for both broad neutralizing antibodies and their unmutated ancestor antibodies
    • Ma BJ, Alam SM, Go EP, et al.: Envelope deglycosylation enhances antigenicity of HIV-1 gp41 epitopes for both broad neutralizing antibodies and their unmutated ancestor antibodies. PLoS Pathog 2011;7:e1002200.
    • (2011) PLoS Pathog , vol.7 , pp. e1002200
    • Ma, B.J.1    Alam, S.M.2    Go, E.P.3
  • 30
    • 0021365255 scopus 로고
    • Monoclonal antibodies against human T cell leukemia-lymphoma virus (HTLV) p24 internal core protein. Use as diagnostic probes and cellular localization of HTLV
    • Palker TJ, Scearce RM, Miller SE, et al.: Monoclonal antibodies against human T cell leukemia-lymphoma virus (HTLV) p24 internal core protein. Use as diagnostic probes and cellular localization of HTLV. J Exp Med 1984;159: 1117-1131.
    • (1984) J Exp Med , vol.159 , pp. 1117-1131
    • Palker, T.J.1    Scearce, R.M.2    Miller, S.E.3
  • 31
    • 84863754149 scopus 로고    scopus 로고
    • HIV-1 gp120 vaccine induces affinity maturation in both new and persistent antibody clonal lineages
    • Moody MA, Yates NL, Amos JD, et al.: HIV-1 gp120 vaccine induces affinity maturation in both new and persistent antibody clonal lineages. J Virol 2012;86:7496-7507.
    • (2012) J Virol , vol.86 , pp. 7496-7507
    • Moody, M.A.1    Yates, N.L.2    Amos, J.D.3
  • 32
    • 84960430333 scopus 로고    scopus 로고
    • Complex antigens drive permissive clonal selection in germinal centers
    • Kuraoka M, Schmidt AG, Nojima T, et al.: Complex antigens drive permissive clonal selection in germinal centers. Immunity 2016;44:542-552.
    • (2016) Immunity , vol.44 , pp. 542-552
    • Kuraoka, M.1    Schmidt, A.G.2    Nojima, T.3
  • 33
    • 55749115777 scopus 로고    scopus 로고
    • Systematic design and testing of nested (RT-)PCR primers for specific amplification of mouse rearranged/expressed immunoglobulin variable region genes from small number of B cells
    • Rohatgi S, Ganju P, Sehgal D. Systematic design and testing of nested (RT-)PCR primers for specific amplification of mouse rearranged/expressed immunoglobulin variable region genes from small number of B cells. J Immunol Methods. Dec 31 2008;339:205-219.
    • (2008) J Immunol Methods. Dec 31 , vol.339 , pp. 205-219
    • Rohatgi, S.1    Ganju, P.2    Sehgal, D.3
  • 34
    • 70349750487 scopus 로고    scopus 로고
    • Cloning and expression of murine Ig genes from single B cells
    • Oct 31
    • Tiller T, Busse CE, Wardemann H. Cloning and expression of murine Ig genes from single B cells. J Immunol Methods. Oct 31 2009;350:183-193.
    • (2009) J Immunol Methods. , vol.350 , pp. 183-193
    • Tiller, T.1    Busse, C.E.2    Wardemann, H.3
  • 35
    • 78049255341 scopus 로고    scopus 로고
    • Replication competent molecular clones of HIV-1 expressing Renilla luciferase facilitate the analysis of antibody inhibition in PBMC
    • Edmonds TG, Ding H, Yuan X, et al.: Replication competent molecular clones of HIV-1 expressing Renilla luciferase facilitate the analysis of antibody inhibition in PBMC. Virology. Dec 05 2010;408:1-13.
    • (2010) Virology. Dec 05 , vol.408 , pp. 1-13
    • Edmonds, T.G.1    Ding, H.2    Yuan, X.3
  • 36
    • 45849125030 scopus 로고    scopus 로고
    • Evaluating neutralizing antibodies against HIV, SIV, and SHIV in luciferase reporter gene assays
    • Chapter 12: Unit 12.11
    • Montefiori DC: Evaluating neutralizing antibodies against HIV, SIV, and SHIV in luciferase reporter gene assays. Curr Protoc Immunol 2005;Chapter 12:Unit 12.11.
    • (2005) Curr Protoc Immunol
    • Montefiori, D.C.1
  • 38
    • 75749133275 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility
    • Pancera M, Majeed S, Ban YE, et al.: Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility. Proc Natl Acad Sci U S A 2010;107:1166-1171.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 1166-1171
    • Pancera, M.1    Majeed, S.2    Ban, Y.E.3
  • 39
    • 84890858459 scopus 로고    scopus 로고
    • Crystal structure of a soluble cleaved HIV-1 envelope trimer
    • Julien JP, Cupo A, Sok D, 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    Cupo, A.2    Sok, D.3
  • 41
    • 0037456827 scopus 로고    scopus 로고
    • Antibody neutralization and escape by HIV-1
    • Wei X, Decker JM, Wang S, et al.: Antibody neutralization and escape by HIV-1. Nature 2003;422:307-312.
    • (2003) Nature , vol.422 , pp. 307-312
    • Wei, X.1    Decker, J.M.2    Wang, S.3
  • 42
    • 77957198704 scopus 로고    scopus 로고
    • Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16
    • Doores KJ, Burton DR: Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16. J Virol 2010;84:10510-10521.
    • (2010) J Virol , vol.84 , pp. 10510-10521
    • Doores, K.J.1    Burton, D.R.2
  • 43
    • 84899991983 scopus 로고    scopus 로고
    • Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies
    • Doria-Rose NA, Schramm CA, Gorman J, 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    Schramm, C.A.2    Gorman, J.3
  • 44
    • 84907527916 scopus 로고    scopus 로고
    • Structural evolution of glycan recognition by a family of potent HIV antibodies
    • Garces F, Sok D, Kong L, et al.: Structural evolution of glycan recognition by a family of potent HIV antibodies. Cell 2014;159:69-79.
    • (2014) Cell , vol.159 , pp. 69-79
    • Garces, F.1    Sok, D.2    Kong, L.3
  • 45
    • 18244422922 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1 - >2 mannose residues on the outer face of gp120
    • Scanlan CN, Pantophlet R, Wormald MR, et al.: The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1 - >2 mannose residues on the outer face of gp120. J Virol 2002; 76:7306-7321.
    • (2002) J Virol , vol.76 , pp. 7306-7321
    • Scanlan, C.N.1    Pantophlet, R.2    Wormald, M.R.3
  • 46
    • 84901236516 scopus 로고    scopus 로고
    • Promiscuous glycan site recognition by antibodies to the high-mannose patch of gp120 broadens neutralization of HIV
    • Sok D, Doores KJ, Briney B, et al.: Promiscuous glycan site recognition by antibodies to the high-mannose patch of gp120 broadens neutralization of HIV. Sci Transl Med 2014;6:236ra263.
    • (2014) Sci Transl Med , vol.6 , pp. 236ra263
    • Sok, D.1    Doores, K.J.2    Briney, B.3
  • 47
    • 84959932564 scopus 로고    scopus 로고
    • Composition and antigenic effects of individual glycan sites of a trimeric HIV-1 envelope glycoprotein
    • Behrens AJ, Vasiljevic S, Pritchard LK, et al.: Composition and antigenic effects of individual glycan sites of a trimeric HIV-1 envelope glycoprotein. Cell Rep 2016;14:2695-2706.
    • (2016) Cell Rep , vol.14 , pp. 2695-2706
    • Behrens, A.J.1    Vasiljevic, S.2    Pritchard, L.K.3
  • 48
    • 80055118908 scopus 로고    scopus 로고
    • Initial antibodies binding to HIV-1 gp41 in acutely infected subjects are polyreactive and highly mutated
    • Liao HX, Chen X, Munshaw S, 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    Chen, X.2    Munshaw, S.3
  • 50
    • 63849131879 scopus 로고    scopus 로고
    • Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals
    • Scheid JF, Mouquet H, Feldhahn N, 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    Mouquet, H.2    Feldhahn, N.3
  • 51
    • 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 AM, Moody MA, Alam SM, 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    Moody, M.A.2    Alam, S.M.3
  • 52
    • 34547804722 scopus 로고    scopus 로고
    • Inhibition of mammalian glycan biosynthesis produces non-self antigens for a broadly neutralising, HIV-1 specific antibody
    • Scanlan CN, Ritchie GE, Baruah K, et al.: Inhibition of mammalian glycan biosynthesis produces non-self antigens for a broadly neutralising, HIV-1 specific antibody. J Mol Biol 2007;372:16-22.
    • (2007) J Mol Biol , vol.372 , pp. 16-22
    • Scanlan, C.N.1    Ritchie, G.E.2    Baruah, K.3
  • 53
    • 84944190259 scopus 로고    scopus 로고
    • Complete epitopes for vaccine design derived from a crystal structure of the broadly neutralizing antibodies PGT128 and 8ANC195 in complex with an HIV-1 Env trimer
    • Kong L, Torrents de la Pena A, Deller MC, et al.: Complete epitopes for vaccine design derived from a crystal structure of the broadly neutralizing antibodies PGT128 and 8ANC195 in complex with an HIV-1 Env trimer. Acta Crystallogr D Biol Crystallogr 2015;71(Pt 10):2099-2108.
    • (2015) Acta Crystallogr D Biol Crystallogr , vol.71 , pp. 2099-2108
    • Kong, L.1    Torrents De La Pena, A.2    Deller, M.C.3
  • 54
    • 84937469192 scopus 로고    scopus 로고
    • HIV-1 VACCINES. HIV-1 neutralizing antibodies induced by native-like envelope trimers
    • Sanders RW, van Gils MJ, Derking R, et al.: HIV-1 VACCINES. HIV-1 neutralizing antibodies induced by native-like envelope trimers. Science 2015;349:aac4223.
    • (2015) Science , vol.349 , pp. aac4223
    • Sanders, R.W.1    Van Gils, M.J.2    Derking, R.3
  • 55
    • 84878430727 scopus 로고    scopus 로고
    • Vaccine-induced plasma IgA specific for the C1 region of the HIV-1 envelope blocks binding and effector function of IgG
    • Tomaras GD, Ferrari G, Shen X, et al.: Vaccine-induced plasma IgA specific for the C1 region of the HIV-1 envelope blocks binding and effector function of IgG. Proc Natl Acad Sci U S A 2013;110:9019-9024.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 9019-9024
    • Tomaras, G.D.1    Ferrari, G.2    Shen, X.3
  • 56
    • 84907991957 scopus 로고    scopus 로고
    • Structural definition of an antibody-dependent cellular cytotoxicity response implicated in reduced risk for HIV-1 infection
    • Acharya P, Tolbert WD, Gohain N, et al.: Structural definition of an antibody-dependent cellular cytotoxicity response implicated in reduced risk for HIV-1 infection. J Virol 2014;88:12895-12906.
    • (2014) J Virol , vol.88 , pp. 12895-12906
    • Acharya, P.1    Tolbert, W.D.2    Gohain, N.3
  • 57
    • 84871960572 scopus 로고    scopus 로고
    • Diverse specificity and effector function among human antibodies to HIV-1 envelope glycoprotein epitopes exposed by CD4 binding
    • Guan Y, Pazgier M, Sajadi MM, et al.: Diverse specificity and effector function among human antibodies to HIV-1 envelope glycoprotein epitopes exposed by CD4 binding. Proc Natl Acad Sci U S A 2013;110:E69-E78.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. E69-E78
    • Guan, Y.1    Pazgier, M.2    Sajadi, M.M.3
  • 58
    • 0028073184 scopus 로고
    • Exploration of antigenic variation in gp120 from clades A through F of human immunodeficiency virus type 1 by using monoclonal antibodies
    • Moore JP, McCutchan FE, Poon SW, et al.: Exploration of antigenic variation in gp120 from clades A through F of human immunodeficiency virus type 1 by using monoclonal antibodies. J Virol 1994;68:8350-8364.
    • (1994) J Virol , vol.68 , pp. 8350-8364
    • Moore, J.P.1    McCutchan, F.E.2    Poon, S.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.