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Volumn 87, Issue 8, 2013, Pages 4185-4201

Antigenicity and immunogenicity of transmitted/founder, consensus, and chronic envelope glycoproteins of human immunodeficiency virus type 1

(24)  Liao, Hua Xin a   Tsao, Chun Yen a   Munir Alam, S a   Muldoon, Mark b   Vandergrift, Nathan a   Ma, Ben Jiang a   Lu, Xiaozhi a   Sutherland, Laura L a   Scearce, Richard M a   Bowman, Cindy a   Parks, Robert a   Chen, Haiyan a   Blinn, Julie H a   Lapedes, Alan c   Watson, Sydeaka c,d   Xia, Shi Mao a   Foulger, Andrew a   Hahn, Beatrice H e,f   Shaw, George M e,f   Swanstrom, Ron g   more..


Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; GLYCOPROTEIN GP 140; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 17B; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG;

EID: 84875771414     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02297-12     Document Type: Article
Times cited : (80)

References (80)
  • 2
    • 69249211230 scopus 로고    scopus 로고
    • T-cell vaccine strategies for human immunodeficiency virus, the virus with a thousand faces
    • Korber BT, Letvin NL, Haynes BF. 2009. T-cell vaccine strategies for human immunodeficiency virus, the virus with a thousand faces. J. Virol. 83:8300-8314.
    • (2009) J. Virol. , vol.83 , pp. 8300-8314
    • Korber, B.T.1    Letvin, N.L.2    Haynes, B.F.3
  • 12
    • 77949409948 scopus 로고    scopus 로고
    • Targeting early infection to prevent HIV-1 mucosal transmission
    • Haase AT. 2010. Targeting early infection to prevent HIV-1 mucosal transmission. Nature 464:217-223.
    • (2010) Nature , vol.464 , pp. 217-223
    • Haase, A.T.1
  • 13
    • 79651469358 scopus 로고    scopus 로고
    • B cell responses to HIV-1 infection and vaccination: pathways to preventing infection
    • Haynes BF, Moody MA, Liao HX, Verkoczy L, Tomaras GD. 2011. B cell responses to HIV-1 infection and vaccination: pathways to preventing infection. Trends Mol. Med. 17:108-116.
    • (2011) Trends Mol. Med. , vol.17 , pp. 108-116
    • Haynes, B.F.1    Moody, M.A.2    Liao, H.X.3    Verkoczy, L.4    Tomaras, G.D.5
  • 14
    • 77951882041 scopus 로고    scopus 로고
    • Toward an antibody-based HIV-1 vaccine
    • Hoxie JA. 2010. Toward an antibody-based HIV-1 vaccine. Annu. Rev. Med. 61:135-152.
    • (2010) Annu. Rev. Med. , vol.61 , pp. 135-152
    • Hoxie, J.A.1
  • 15
    • 77953543379 scopus 로고    scopus 로고
    • Rational antibody-based HIV-1 vaccine design: current approaches and future directions
    • Walker LM, Burton DR. 2010. Rational antibody-based HIV-1 vaccine design: current approaches and future directions. Curr. Opin. Immunol. 22:358-366.
    • (2010) Curr. Opin. Immunol. , vol.22 , pp. 358-366
    • Walker, L.M.1    Burton, D.R.2
  • 16
    • 79955855015 scopus 로고    scopus 로고
    • Structural analysis of human and macaque MAbs 2909 and 2.5B: implications for the configuration of the quaternary neutralizing epitope of HIV-1 gp120
    • Spurrier B, Sampson JM, Totrov M, Li H, O'Neal T, Williams C, Robinson J, Gorny MK, Zolla-Pazner S, Kong XP. 2011. Structural analysis of human and macaque MAbs 2909 and 2.5B: implications for the configuration of the quaternary neutralizing epitope of HIV-1 gp120. Structure 19:691-699.
    • (2011) Structure , vol.19 , pp. 691-699
    • Spurrier, B.1    Sampson, J.M.2    Totrov, M.3    Li, H.4    O'Neal, T.5    Williams, C.6    Robinson, J.7    Gorny, M.K.8    Zolla-Pazner, S.9    Kong, X.P.10
  • 18
    • 84860759632 scopus 로고    scopus 로고
    • B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study
    • Haynes BF, Kelsoe G, Harrison SC, Kepler TB. 2012. B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study. Nat. Biotechnol. 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
  • 19
    • 79957726572 scopus 로고    scopus 로고
    • Role of immune mechanisms in induction of HIV-1 broadly neutralizing antibodies
    • Verkoczy L, Kelsoe G, Moody MA, Haynes BF. 2011. Role of immune mechanisms in induction of HIV-1 broadly neutralizing antibodies. Curr. Opin. Immunol. 23:383-390.
    • (2011) Curr. Opin. Immunol. , vol.23 , pp. 383-390
    • Verkoczy, L.1    Kelsoe, G.2    Moody, M.A.3    Haynes, B.F.4
  • 23
    • 84863263044 scopus 로고    scopus 로고
    • Evaluation of cervical mucosa in transmission bottleneck during acute HIV-1 infection using a cervical tissue-based organ culture
    • doi:10.1371/journal.pone.0032539
    • Shen C, Ding M, Ratner D, Montelaro RC, Chen Y, Gupta P. 2012. Evaluation of cervical mucosa in transmission bottleneck during acute HIV-1 infection using a cervical tissue-based organ culture. PLoS One 7:e32539. doi:10.1371/journal.pone.0032539.
    • (2012) PLoS One , vol.7
    • Shen, C.1    Ding, M.2    Ratner, D.3    Montelaro, R.C.4    Chen, Y.5    Gupta, P.6
  • 24
    • 18144397438 scopus 로고    scopus 로고
    • Selection for human immunodeficiency virus type 1 envelope glycosylation variants with shorter V1-V2 loop sequences occurs during transmission of certain genetic subtypes and may impact viralRNA levels
    • Chohan B, Lang D, Sagar M, Korber B, Lavreys L, Richardson B, Overbaugh J. 2005. Selection for human immunodeficiency virus type 1 envelope glycosylation variants with shorter V1-V2 loop sequences occurs during transmission of certain genetic subtypes and may impact viralRNA levels. J. Virol. 79:6528-6531.
    • (2005) J. Virol. , vol.79 , pp. 6528-6531
    • Chohan, B.1    Lang, D.2    Sagar, M.3    Korber, B.4    Lavreys, L.5    Richardson, B.6    Overbaugh, J.7
  • 34
    • 13144302861 scopus 로고    scopus 로고
    • Comparison of HIV type 1 ADA gp120 monomers versus gp140 trimers as immunogens for the induction of neutralizing antibodies
    • Kim M, Qiao ZS, Montefiori DC, Haynes BF, Reinherz EL, Liao HX. 2005. Comparison of HIV type 1 ADA gp120 monomers versus gp140 trimers as immunogens for the induction of neutralizing antibodies. AIDS Res. Hum. Retrovir. 21:58-67.
    • (2005) AIDS Res. Hum. Retrovir. , vol.21 , pp. 58-67
    • Kim, M.1    Qiao, Z.S.2    Montefiori, D.C.3    Haynes, B.F.4    Reinherz, E.L.5    Liao, H.X.6
  • 36
    • 0031906148 scopus 로고    scopus 로고
    • Increased immune response elicited by DNA vaccination with a synthetic gp120 sequence with optimized codon usage
    • Andre S, Seed B, Eberle J, Schraut W, Bultmann A, Haas J. 1998. Increased immune response elicited by DNA vaccination with a synthetic gp120 sequence with optimized codon usage. J. Virol. 72:1497-1503.
    • (1998) J. Virol. , vol.72 , pp. 1497-1503
    • Andre, S.1    Seed, B.2    Eberle, J.3    Schraut, W.4    Bultmann, A.5    Haas, J.6
  • 37
    • 0029119783 scopus 로고
    • Involvement of the V1/V2 variable loop structure in the exposure of hu-man immunodeficiency virus type 1 gp120 epitopes induced by receptor binding
    • Wyatt R, Moore J, Accola M, Desjardin E, Robinson J, Sodroski J. 1995. Involvement of the V1/V2 variable loop structure in the exposure of hu-man immunodeficiency virus type 1 gp120 epitopes induced by receptor binding. J. Virol. 69:5723-5733.
    • (1995) J. Virol. , vol.69 , pp. 5723-5733
    • Wyatt, R.1    Moore, J.2    Accola, M.3    Desjardin, E.4    Robinson, J.5    Sodroski, J.6
  • 38
    • 0035852822 scopus 로고    scopus 로고
    • Antibody 17b binding at the coreceptor site weakens the kinetics of the interaction of envelope glycoprotein gp120 with CD4
    • Zhang W, Godillot AP, Wyatt R, Sodroski J, Chaiken I. 2001. Antibody 17b binding at the coreceptor site weakens the kinetics of the interaction of envelope glycoprotein gp120 with CD4. Biochemistry 40:1662-1670.
    • (2001) Biochemistry , vol.40 , pp. 1662-1670
    • Zhang, W.1    Godillot, A.P.2    Wyatt, R.3    Sodroski, J.4    Chaiken, I.5
  • 41
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by twodimensional native electrophoresis
    • Schagger H, Cramer WA, von Jagow G. 1994. Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by twodimensional native electrophoresis. Anal. Biochem. 217:220-230.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schagger, H.1    Cramer, W.A.2    von Jagow, G.3
  • 43
    • 2342455189 scopus 로고    scopus 로고
    • Immunogenicity of constrained monoclonal antibody A32-human immunodeficiency virus (HIV) Env gp120 complexes compared to that of recombinant HIV type 1 gp120 envelope glycoproteins
    • Liao HX, Alam SM, Mascola JR, Robinson J, Ma B, Montefiori DC, Rhein M, Sutherland LL, Scearce R, Haynes BF. 2004. Immunogenicity of constrained monoclonal antibody A32-human immunodeficiency virus (HIV) Env gp120 complexes compared to that of recombinant HIV type 1 gp120 envelope glycoproteins. J. Virol. 78:5270-5278.
    • (2004) J. Virol. , vol.78 , pp. 5270-5278
    • Liao, H.X.1    Alam, S.M.2    Mascola, J.R.3    Robinson, J.4    Ma, B.5    Montefiori, D.C.6    Rhein, M.7    Sutherland, L.L.8    Scearce, R.9    Haynes, B.F.10
  • 47
    • 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. 2005. Evaluating neutralizing antibodies against HIV, SIV, and SHIV in luciferase reporter gene assays. Curr. Protoc. Immunol. Chapter 12:Unit 12-11.
    • (2005) Curr. Protoc. Immunol.
    • Montefiori, D.C.1
  • 49
    • 84863304598 scopus 로고    scopus 로고
    • R, RDCT: a language and environment for statistical computing
    • R Foundation for Statistical Computing, Vienna, Austria
    • R Foundation for Statistical Computing. 2010. R, RDCT: a language and environment for statistical computing. R Foundation for Statistical Computing, Vienna, Austria.
    • (2010) R Foundation for Statistical Computing
  • 50
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: a practical and powerful approach to multiple testing
    • Benjamini Y, Hochberg Y. 1995. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J. R. Stat. Soc. Ser. B Stat. Methodol. 57:289-300.
    • (1995) J. R. Stat. Soc. Ser. B Stat. Methodol. , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 51
    • 18544382833 scopus 로고    scopus 로고
    • Generalized additive models for location, scale, and shape
    • Rigby RA, Stasinopoulos DM. 2005. Generalized additive models for location, scale, and shape. Appl. Statistics 54:507-554. 52. Hothorn T, Bretz F, Westfall P. 2008. Simultaneous inference in general parametric models. Biometrical J. 50:346-363.
    • (2005) Appl. Statistics , vol.54 , pp. 507-554
    • Rigby, R.A.1    Stasinopoulos, D.M.2
  • 52
    • 49849092907 scopus 로고    scopus 로고
    • Simultaneous inference in general parametric models
    • Hothorn T, Bretz F, Westfall P. 2008. Simultaneous inference in general parametric models. Biometrical J. 50:346-363.
    • (2008) Biometrical J. , vol.50 , pp. 346-363
    • Hothorn, T.1    Bretz, F.2    Westfall, P.3
  • 53
    • 84887411391 scopus 로고    scopus 로고
    • BSagri: statistical methods for safety assessment in agricultural field trials
    • Schaarschmidt F. 2010. BSagri: statistical methods for safety assessment in agricultural field trials. R package, version 0.1-6. http://cran.r-project .org/web/packages/BSagri/BSagri.pdf.
    • (2010) R package, version 0.1-6
    • Schaarschmidt, F.1
  • 56
    • 45549101708 scopus 로고    scopus 로고
    • Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility
    • Go EP, Irungu J, Zhang Y, Dalpathado DS, Liao HX, Sutherland LL, Alam SM, Haynes BF, Desaire H. 2008. Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility. J. Proteome Res. 7:1660-1674.
    • (2008) J. Proteome Res. , vol.7 , pp. 1660-1674
    • Go, E.P.1    Irungu, J.2    Zhang, Y.3    Dalpathado, D.S.4    Liao, H.X.5    Sutherland, L.L.6    Alam, S.M.7    Haynes, B.F.8    Desaire, H.9
  • 63
    • 84872809067 scopus 로고    scopus 로고
    • Vaccine induction of antibodies against a structurally heterogeneous site of immune pressure within HIV-1 envelope protein variable regions 1 and 2
    • doi:101016/j.immuni .2012.11.011
    • Liao HX, Bonsignori M. 2013. Vaccine induction of antibodies against a structurally heterogeneous site of immune pressure within HIV-1 envelope protein variable regions 1 and 2. Immunity doi:10.1016/j.immuni .2012.11.011.
    • (2013) Immunity
    • Liao, H.X.1    Bonsignori, M.2
  • 65
    • 4544379899 scopus 로고    scopus 로고
    • Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope
    • Ofek G, Tang M, Sambor A, Katinger H, Mascola JR, Wyatt R, Kwong PD. 2004. Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope. J. Virol. 78:10724-10737.
    • (2004) J. Virol. , vol.78 , pp. 10724-10737
    • Ofek, G.1    Tang, M.2    Sambor, A.3    Katinger, H.4    Mascola, J.R.5    Wyatt, R.6    Kwong, P.D.7
  • 66
    • 33744937069 scopus 로고    scopus 로고
    • The HIV-neutralizing monoclonal antibody 4E10 recognizes N-terminal sequences on the native antigen
    • Hager-Braun C, Katinger H, Tomer KB. 2006. The HIV-neutralizing monoclonal antibody 4E10 recognizes N-terminal sequences on the native antigen. J. Immunol. 176:7471-7481.
    • (2006) J. Immunol. , vol.176 , pp. 7471-7481
    • Hager-Braun, C.1    Katinger, H.2    Tomer, K.B.3
  • 70
    • 77956839028 scopus 로고    scopus 로고
    • Alterations in the immunogenic properties of soluble trimeric human immunodeficiency virus type 1 envelope proteins induced by deletion or heterologous substitutions of the V1 loop
    • Ching L, Stamatatos L. 2010. Alterations in the immunogenic properties of soluble trimeric human immunodeficiency virus type 1 envelope proteins induced by deletion or heterologous substitutions of the V1 loop. J. Virol. 84:9932-9946.
    • (2010) J. Virol. , vol.84 , pp. 9932-9946
    • Ching, L.1    Stamatatos, L.2
  • 72
    • 0034826583 scopus 로고    scopus 로고
    • Differential recognition of epitopes present on monomeric and oligomeric forms of gp160 glycoprotein of human immunodeficiency virus type 1 by human monoclonal antibodies
    • Zeder-Lutz G, Hoebeke J, Van Regenmortel MH. 2001. Differential recognition of epitopes present on monomeric and oligomeric forms of gp160 glycoprotein of human immunodeficiency virus type 1 by human monoclonal antibodies. Eur. J. Biochem. 268:2856-2866.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2856-2866
    • Zeder-Lutz, G.1    Hoebeke, J.2    Van Regenmortel, M.H.3
  • 76
    • 0030823325 scopus 로고    scopus 로고
    • Potent and synergistic neutralization of human immunodeficiency virus (HIV) type 1 primary isolates by hyperimmune anti-HIV immunoglobulin combined with monoclonal antibodies 2F5 and 2G12
    • Mascola JR, Louder MK, VanCott TC, Sapan CV, Lambert JS, Muenz LR, Bunow B, Birx DL, Robb ML. 1997. Potent and synergistic neutralization of human immunodeficiency virus (HIV) type 1 primary isolates by hyperimmune anti-HIV immunoglobulin combined with monoclonal antibodies 2F5 and 2G12. J. Virol. 71:7198-7206.
    • (1997) J. Virol. , vol.71 , pp. 7198-7206
    • Mascola, J.R.1    Louder, M.K.2    VanCott, T.C.3    Sapan, C.V.4    Lambert, J.S.5    Muenz, L.R.6    Bunow, B.7    Birx, D.L.8    Robb, M.L.9
  • 77
    • 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 PW, Marx PA, Hessell AJ, Luckay A, Harouse J, Cheng-Mayer C, Moore JP, Burton DR. 2001. Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro. J. Virol. 75:8340-8347.
    • (2001) J. Virol. , vol.75 , pp. 8340-8347
    • Parren, P.W.1    Marx, P.A.2    Hessell, A.J.3    Luckay, A.4    Harouse, J.5    Cheng-Mayer, C.6    Moore, J.P.7    Burton, D.R.8
  • 78
    • 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, Igarashi T, Haigwood N, Buckler-White A, Ogert R, Ross W, Willey R, Cho MW, Martin MA. 1999. Neutralizing antibody directed against the HIV-1 envelope glycoprotein can completely block HIV-1/SIV chimeric virus infections of macaque monkeys. Nat. Med. 5:204-210.
    • (1999) Nat. Med. , vol.5 , pp. 204-210
    • Shibata, R.1    Igarashi, T.2    Haigwood, N.3    Buckler-White, A.4    Ogert, R.5    Ross, W.6    Willey, R.7    Cho, M.W.8    Martin, M.A.9
  • 80
    • 69549114407 scopus 로고    scopus 로고
    • Neutralizing antibodies against HIV-1: can we elicit them with vaccines and how much do we need?
    • Montefiori DC, Mascola JR. 2009. Neutralizing antibodies against HIV-1: can we elicit them with vaccines and how much do we need? Curr. Opin. HIV AIDS 4:347-351.
    • (2009) Curr. Opin. HIV AIDS , vol.4 , pp. 347-351
    • Montefiori, D.C.1    Mascola, J.R.2


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