메뉴 건너뛰기




Volumn 86, Issue 22, 2012, Pages 12105-12114

Sequences in glycoprotein gp41, the CD4 binding Site, and the V2 domain regulate sensitivity and resistance of HIV-1 to broadly neutralizing antibodies

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN GP 41;

EID: 84869140656     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01352-12     Document Type: Article
Times cited : (24)

References (72)
  • 1
    • 0031764239 scopus 로고    scopus 로고
    • Development of bivalent rgp120 vaccines to prevent HIV type 1 infection
    • Berman PW. 1998. Development of bivalent rgp120 vaccines to prevent HIV type 1 infection. AIDS Res. Hum. Retroviruses 14(Suppl 3):S277-S289.
    • (1998) AIDS Res. Hum. Retroviruses , vol.14 , Issue.SUPPL. 3
    • Berman, P.W.1
  • 2
    • 0033985999 scopus 로고    scopus 로고
    • A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure
    • Binley JM, et al. 2000. A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure. J. Virol. 74:627-643.
    • (2000) J. Virol , vol.74 , pp. 627-643
    • Binley, J.M.1
  • 3
    • 38849205377 scopus 로고    scopus 로고
    • Enhancing exposure of HIV-1 neutralization epitopes through mutations in gp41
    • doi:10.1371/journal.pmed.0050009
    • Blish CA, Nguyen MA, Overbaugh J. 2008. Enhancing exposure of HIV-1 neutralization epitopes through mutations in gp41. PLoS Med. 5:e9. doi:10.1371/journal.pmed.0050009.
    • (2008) PLoS Med. , vol.5
    • Blish, C.A.1    Nguyen, M.A.2    Overbaugh, J.3
  • 5
    • 1542317452 scopus 로고    scopus 로고
    • HIV vaccine design and the neutralizing antibody problem
    • Burton DR, et al. 2004. HIV vaccine design and the neutralizing antibody problem. Nat. Immunol. 5:233-236.
    • (2004) Nat. Immunol. , vol.5 , pp. 233-236
    • Burton, D.R.1
  • 6
    • 0027985431 scopus 로고
    • Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody
    • Burton DR, et al. 1994. Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science 266: 1024-1027.
    • (1994) Science , vol.266 , pp. 1024-1027
    • Burton, D.R.1
  • 7
    • 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 SG, et al. 2006. 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. 80: 6155-6164.
    • (2006) J. Virol. , vol.80 , pp. 6155-6164
    • Deeks, S.G.1
  • 9
    • 34249950588 scopus 로고    scopus 로고
    • Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors
    • Dhillon AK, et al. 2007. Dissecting the neutralizing antibody specificities of broadly neutralizing sera from human immunodeficiency virus type 1-infected donors. J. Virol. 81:6548-6562.
    • (2007) J. Virol. , vol.81 , pp. 6548-6562
    • Dhillon, A.K.1
  • 10
    • 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 NA, et al. 2009. Frequency and phenotype of human immunodeficiency virus envelope-specific B cells from patients with broadly cross-neutralizing antibodies. J. Virol. 83:188-199.
    • (2009) J. Virol , vol.83 , pp. 188-199
    • Doria-Rose, N.A.1
  • 11
    • 77956043460 scopus 로고    scopus 로고
    • HIV-1 gp120 determinants proximal to the CD4 binding site shift protective glycans that are targeted by monoclonal antibody 2G12
    • Duenas-Decamp MJ, Clapham PR. 2010. HIV-1 gp120 determinants proximal to the CD4 binding site shift protective glycans that are targeted by monoclonal antibody 2G12. J. Virol. 84:9608-9612.
    • (2010) J. Virol , vol.84 , pp. 9608-9612
    • Duenas-Decamp, M.J.1    Clapham, P.R.2
  • 12
    • 44949125679 scopus 로고    scopus 로고
    • Natural resistance of human immunodeficiency virus type 1 to the CD4bs antibody b12 conferred by a glycan and an arginine residue close to the CD4 binding loop
    • Duenas-Decamp MJ, Peters P, Burton D, Clapham PR. 2008. Natural resistance of human immunodeficiency virus type 1 to the CD4bs antibody b12 conferred by a glycan and an arginine residue close to the CD4 binding loop. J. Virol. 82:5807-5814.
    • (2008) J. Virol , vol.82 , pp. 5807-5814
    • Duenas-Decamp, M.J.1    Peters, P.2    Burton, D.3    Clapham, P.R.4
  • 13
    • 0036187805 scopus 로고    scopus 로고
    • Truncation of the cytoplasmic domain induces exposure of conserved regions in the ectodomain of human immunodeficiency virus type 1 envelope protein
    • Edwards TG, et al. 2002. Truncation of the cytoplasmic domain induces exposure of conserved regions in the ectodomain of human immunodeficiency virus type 1 envelope protein. J. Virol. 76:2683-2691.
    • (2002) J. Virol , vol.76 , pp. 2683-2691
    • Edwards, T.G.1
  • 14
    • 13944254982 scopus 로고    scopus 로고
    • Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection
    • Flynn NM, et al. 2005. Placebo-controlled phase 3 trial of a recombinant glycoprotein 120 vaccine to prevent HIV-1 infection. J. Infect. Dis. 191:654-665.
    • (2005) J. Infect. Dis , vol.191 , pp. 654-665
    • Flynn, N.M.1
  • 15
    • 18144429071 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 (HIV-1) envelope variation and neutralizing antibody responses during transmission of HIV-1 subtype B.
    • Frost SD, et al. 2005. Characterization of human immunodeficiency virus type 1 (HIV-1) envelope variation and neutralizing antibody responses during transmission of HIV-1 subtype B. J. Virol. 79:6523-6527.
    • (2005) J. Virol. , vol.79 , pp. 6523-6527
    • Frost, S.D.1
  • 16
    • 0026595148 scopus 로고
    • Identification and characterization of a neutralization site within the second variable region of human immunodeficiency virus type 1 gp120.
    • Fung MS, et al. 1992. Identification and characterization of a neutralization site within the second variable region of human immunodeficiency virus type 1 gp120. J. Virol. 66:848-856.
    • (1992) J. Virol. , vol.66 , pp. 848-856
    • Fung, M.S.1
  • 17
    • 24644479045 scopus 로고    scopus 로고
    • HIV-1 virologic and immunologic progression and initiation of antiretroviral therapy among HIV-1-infected subjects in a trial of the efficacy of recombinant glycoprotein 120 vaccine
    • Gilbert PB, et al. 2005. HIV-1 virologic and immunologic progression and initiation of antiretroviral therapy among HIV-1-infected subjects in a trial of the efficacy of recombinant glycoprotein 120 vaccine. J. Infect. Dis. 192:974-983.
    • (2005) J. Infect. Dis. , vol.192 , pp. 974-983
    • Gilbert, P.B.1
  • 18
    • 16244419386 scopus 로고    scopus 로고
    • Identification of a new quaternary neutralizing epitope on human immunodeficiency virus type 1 virus particles
    • Gorny MK, et al. 2005. Identification of a new quaternary neutralizing epitope on human immunodeficiency virus type 1 virus particles. J. Virol. 79:5232-5237.
    • (2005) J. Virol. , vol.79 , pp. 5232-5237
    • Gorny, M.K.1
  • 19
    • 39749136530 scopus 로고    scopus 로고
    • 4E10-resistant variants in a human immunodeficiency virus type 1 subtype C-infected individual with an anti-membraneproximal external region-neutralizing antibody response
    • Gray ES, et al. 2008. 4E10-resistant variants in a human immunodeficiency virus type 1 subtype C-infected individual with an anti-membraneproximal external region-neutralizing antibody response. J. Virol. 82:2367-2375.
    • (2008) J. Virol. , vol.82 , pp. 2367-2375
    • Gray, E.S.1
  • 20
    • 84865066445 scopus 로고    scopus 로고
    • Solution structure, conformational dynamics, and CD4-induced activation in fulllength, glycosylated, monomeric HIV gp120
    • Guttman M, Kahn M, Garcia NK, Hu SL, Lee KK. 2012. Solution structure, conformational dynamics, and CD4-induced activation in fulllength, glycosylated, monomeric HIV gp120. J. Virol. 86:8750-8764.
    • (2012) J. Virol. , vol.86 , pp. 8750-8764
    • Guttman, M.1    Kahn, M.2    Garcia, N.K.3    Hu, S.L.4    Lee, K.K.5
  • 21
    • 0026054574 scopus 로고
    • The cytoplasmic tail of HIV-1 gp160 contains regions that associate with cellular membranes
    • Haffar OK, Dowbenko DJ, Berman PW. 1991. The cytoplasmic tail of HIV-1 gp160 contains regions that associate with cellular membranes. Virology 180:439-441.
    • (1991) Virology , vol.180 , pp. 439-441
    • Haffar, O.K.1    Dowbenko, D.J.2    Berman, P.W.3
  • 22
    • 0023732248 scopus 로고
    • Topogenic analysis of the human immunodeficiency virus type 1 envelope glycoprotein, gp160, in microsomal membranes
    • Haffar OK, Dowbenko DJ, Berman PW. 1988. Topogenic analysis of the human immunodeficiency virus type 1 envelope glycoprotein, gp160, in microsomal membranes. J. Cell Biol. 107:1677-1687.
    • (1988) J. Cell Biol. , vol.107 , pp. 1677-1687
    • Haffar, O.K.1    Dowbenko, D.J.2    Berman, P.W.3
  • 23
    • 33846556067 scopus 로고    scopus 로고
    • Type-specific epitopes targeted by monoclonal antibodies with exceptionally potent neutralizing activities for selected strains of human immunodeficiency virus type 1 map to a common region of the V2 domain of gp120 and differ only at single positions from the clade B consensus sequence
    • Honnen WJ, et al. 2007. Type-specific epitopes targeted by monoclonal antibodies with exceptionally potent neutralizing activities for selected strains of human immunodeficiency virus type 1 map to a common region of the V2 domain of gp120 and differ only at single positions from the clade B consensus sequence. J. Virol. 81:1424-1432.
    • (2007) J. Virol. , vol.81 , pp. 1424-1432
    • Honnen, W.J.1
  • 24
    • 43949118440 scopus 로고    scopus 로고
    • Coreceptor tropism can be influenced by amino acid substitutions in the gp41 transmembrane subunit of human immunodeficiency virus type 1 envelope protein
    • Huang W, et al. 2008. Coreceptor tropism can be influenced by amino acid substitutions in the gp41 transmembrane subunit of human immunodeficiency virus type 1 envelope protein. J. Virol. 82:5584-5593.
    • (2008) J. Virol. , vol.82 , pp. 5584-5593
    • Huang, W.1
  • 25
    • 69249202492 scopus 로고    scopus 로고
    • Transitions to and from the CD4-bound conformation are modulated by a single-residue change in the human immunodeficiency virus type 1 gp120 inner domain
    • Kassa A, et al. 2009. Transitions to and from the CD4-bound conformation are modulated by a single-residue change in the human immunodeficiency virus type 1 gp120 inner domain. J. Virol. 83:8364-8378.
    • (2009) J. Virol. , vol.83 , pp. 8364-8378
    • Kassa, A.1
  • 26
    • 0035100868 scopus 로고    scopus 로고
    • Loss of a single N-linked glycan allows CD4-independent human immunodeficiency virus type 1 infection by altering the position of the gp120 V1/V2 variable loops
    • Kolchinsky P, Kiprilov E, Bartley P, Rubinstein R, Sodroski J. 2001. Loss of a single N-linked glycan allows CD4-independent human immunodeficiency virus type 1 infection by altering the position of the gp120 V1/V2 variable loops. J. Virol. 75:3435-3443.
    • (2001) J. Virol. , vol.75 , pp. 3435-3443
    • Kolchinsky, P.1    Kiprilov, E.2    Bartley, P.3    Rubinstein, R.4    Sodroski, J.5
  • 27
    • 0035131175 scopus 로고    scopus 로고
    • Increased neutralization sensitivity of CD4-independent human immunodeficiency virus variants
    • Kolchinsky P, Kiprilov E, Sodroski J. 2001. Increased neutralization sensitivity of CD4-independent human immunodeficiency virus variants. J. Virol. 75:2041-2050.
    • (2001) J. Virol. , vol.75 , pp. 2041-2050
    • Kolchinsky, P.1    Kiprilov, E.2    Sodroski, J.3
  • 28
    • 0023217711 scopus 로고
    • Functional regions of the envelope glycoprotein of human immunodeficiency virus type 1
    • Kowalski M, et al. 1987. Functional regions of the envelope glycoprotein of human immunodeficiency virus type 1. Science 237:1351-1355.
    • (1987) Science , vol.237 , pp. 1351-1355
    • Kowalski, M.1
  • 29
    • 84859561617 scopus 로고    scopus 로고
    • Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops
    • Kwon YD, et al. 2012. Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops. Proc. Natl. Acad. Sci. U. S. A. 109:5663-5668.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 5663-5668
    • Kwon, Y.D.1
  • 30
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong PD, et al. 1998. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393:648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1
  • 31
    • 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 AF, et al. 2003. 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. 77:10557-10565.
    • (2003) J. Virol. , vol.77 , pp. 10557-10565
    • Labrijn, A.F.1
  • 32
    • 23244434512 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 env clones from acute and early subtype B infections for standardized assessments of vaccine-elicited neutralizing antibodies
    • Li M, et al. 2005. Human immunodeficiency virus type 1 env clones from acute and early subtype B infections for standardized assessments of vaccine-elicited neutralizing antibodies. J. Virol. 79:10108-10125.
    • (2005) J. Virol. , vol.79 , pp. 10108-10125
    • Li, M.1
  • 33
    • 34948854718 scopus 로고    scopus 로고
    • Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses. J. Virol. 82:638-651. 34. Li Y, et al. 2007. Broad HIV-1 neutralization mediated by CD4-binding site antibodies
    • Li Y, et al. 2008. Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses. J. Virol. 82:638-651. 34. Li Y, et al. 2007. Broad HIV-1 neutralization mediated by CD4-binding site antibodies. Nat. Med. 13:1032-1034.
    • (2008) Nat. Med. , vol.13 , pp. 1032-1034
    • Li, Y.1
  • 34
    • 34948854718 scopus 로고    scopus 로고
    • Broad HIV-1 neutralization mediated by CD4-binding site antibodies
    • Li Y, et al. 2007. Broad HIV-1 neutralization mediated by CD4-binding site antibodies. Nat. Med. 13:1032-1034.
    • (2007) Nat. Med. , vol.13 , pp. 1032-1034
    • Li, Y.1
  • 36
    • 0033942750 scopus 로고    scopus 로고
    • V2 loop glycosylation of the human immunodeficiency virus type 1 SF162 envelope facilitates interaction of this protein with CD4 and CCR5 receptors and protects the virus from neutralization by anti-V3 loop and anti-CD4 binding site antibodies
    • Ly A, Stamatatos L. 2000. V2 loop glycosylation of the human immunodeficiency virus type 1 SF162 envelope facilitates interaction of this protein with CD4 and CCR5 receptors and protects the virus from neutralization by anti-V3 loop and anti-CD4 binding site antibodies. J. Virol. 74:6769-6776.
    • (2000) J. Virol. , vol.74 , pp. 6769-6776
    • Ly, A.1    Stamatatos, L.2
  • 37
    • 0027199489 scopus 로고
    • Characterization of neutralizing monoclonal antibodies to linear and conformation-dependent epitopes within the first and second variable domains of human immunodeficiency virus type 1 gp120
    • McKeating JA, et al. 1993. Characterization of neutralizing monoclonal antibodies to linear and conformation-dependent epitopes within the first and second variable domains of human immunodeficiency virus type 1 gp120. J. Virol. 67:4932-4944.
    • (1993) J. Virol. , vol.67 , pp. 4932-4944
    • McKeating, J.A.1
  • 38
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    • McLellan JS, et al. 2011. Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 480:336-343.
    • (2011) Nature , vol.480 , pp. 336-343
    • McLellan, J.S.1
  • 40
    • 79952579682 scopus 로고    scopus 로고
    • Potent and broad neutralization of HIV-1 subtype C by plasma antibodies targeting a quaternary epitope including residues in the V2 loop
    • Moore PL, et al. 2011. Potent and broad neutralization of HIV-1 subtype C by plasma antibodies targeting a quaternary epitope including residues in the V2 loop. J. Virol. 85:3128-3141.
    • (2011) J. Virol. , vol.85 , pp. 3128-3141
    • Moore, P.L.1
  • 41
    • 84862173040 scopus 로고    scopus 로고
    • Monoclonal antibodies to the V2 domain of MN-rgp120: fine mapping of epitopes and inhibition of 47 binding
    • doi:10.1371/journal.pone.0039045
    • Nakamura GR, Fonseca DP, O'Rourke SM, Vollrath AL, Berman PW. 2012. Monoclonal antibodies to the V2 domain of MN-rgp120: fine mapping of epitopes and inhibition of 47 binding. PLoS One 7:e39045. doi:10.1371/journal.pone.0039045.
    • (2012) PLoS One , vol.7
    • Nakamura, G.R.1    Fonseca, D.P.2    O'Rourke, S.M.3    Vollrath, A.L.4    Berman, P.W.5
  • 42
    • 77957940271 scopus 로고    scopus 로고
    • Mutation at a single position in the V2 domain of the HIV-1 envelope protein confers neutralization sensitivity to a highly neutralization-resistant virus
    • O'Rourke SM, et al. 2010. Mutation at a single position in the V2 domain of the HIV-1 envelope protein confers neutralization sensitivity to a highly neutralization-resistant virus. J. Virol. 84:11200-11209.
    • (2010) J. Virol. , vol.84 , pp. 11200-11209
    • O'Rourke, S.M.1
  • 43
    • 67650891897 scopus 로고    scopus 로고
    • Novel ring structure in the gp41 trimer of human immunodeficiency virus type 1 that modulates sensitivity and resistance to broadly neutralizing antibodies
    • O'Rourke SM, et al. 2009. Novel ring structure in the gp41 trimer of human immunodeficiency virus type 1 that modulates sensitivity and resistance to broadly neutralizing antibodies. J. Virol. 83:7728-7738.
    • (2009) J. Virol. , vol.83 , pp. 7728-7738
    • O'Rourke, S.M.1
  • 44
    • 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, et al. 2010. 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. 107:1166-1171.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 1166-1171
    • Pancera, M.1
  • 45
    • 74549175896 scopus 로고    scopus 로고
    • Phylodynamics of HIV-1 from a phase-III AIDS vaccine trial in North America
    • Perez-Losada M, et al. 2010. Phylodynamics of HIV-1 from a phase-III AIDS vaccine trial in North America. Mol. Biol. Evol. 27:417-425.
    • (2010) Mol. Biol. Evol. , vol.27 , pp. 417-425
    • Perez-Losada, M.1
  • 46
    • 0034019566 scopus 로고    scopus 로고
    • A novel phenotypic drug susceptibility assay for human immunodeficiency virus type 1
    • Petropoulos CJ, et al. 2000. A novel phenotypic drug susceptibility assay for human immunodeficiency virus type 1. Antimicrob. Agents Chemother. 44:920-928.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 920-928
    • Petropoulos, C.J.1
  • 47
    • 38949186531 scopus 로고    scopus 로고
    • Roles of HIV-1 Env variable regions in viral neutralization and vaccine development
    • Pinter A. 2007. Roles of HIV-1 Env variable regions in viral neutralization and vaccine development. Curr. HIV Res. 5:542-553.
    • (2007) Curr. HIV Res. , vol.5 , pp. 542-553
    • Pinter, A.1
  • 48
    • 2342644898 scopus 로고    scopus 로고
    • The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection
    • Pinter A, et al. 2004. The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection. J. Virol. 78:5205-5215.
    • (2004) J. Virol. , vol.78 , pp. 5205-5215
    • Pinter, A.1
  • 50
    • 33846552274 scopus 로고    scopus 로고
    • Role of V1V2 and other human immunodeficiency virus type 1 envelope domains in resistance to autologous neutralization during clade C infection
    • Rong R, et al. 2007. Role of V1V2 and other human immunodeficiency virus type 1 envelope domains in resistance to autologous neutralization during clade C infection. J. Virol. 81:1350-1359.
    • (2007) J. Virol. , vol.81 , pp. 1350-1359
    • Rong, R.1
  • 51
    • 70349695689 scopus 로고    scopus 로고
    • Escape from autologous neutralizing antibodies in acute/early subtype C HIV-1 infection requires multiple pathways
    • doi:10.1371/journal.ppat.1000594
    • Rong R, et al. 2009. Escape from autologous neutralizing antibodies in acute/early subtype C HIV-1 infection requires multiple pathways. PLoS Pathog. 5:e1000594. doi:10.1371/journal.ppat.1000594.
    • (2009) PLoS Pathog. , vol.5
    • Rong, R.1
  • 52
    • 58149487645 scopus 로고    scopus 로고
    • Factors associated with the development of crossreactive neutralizing antibodies during human immunodeficiency virus type 1 infection
    • Sather DN, et al. 2009. Factors associated with the development of crossreactive neutralizing antibodies during human immunodeficiency virus type 1 infection. J. Virol. 83:757-769.
    • (2009) J. Virol. , vol.83 , pp. 757-769
    • Sather, D.N.1
  • 53
    • 21644446614 scopus 로고    scopus 로고
    • The V1, V2, and V3 regions of the human immunodeficiency virus type 1 envelope differentially affect the viral phenotype in an isolate-dependent manner
    • Saunders CJ, et al. 2005. The V1, V2, and V3 regions of the human immunodeficiency virus type 1 envelope differentially affect the viral phenotype in an isolate-dependent manner. J. Virol. 79:9069-9080.
    • (2005) J. Virol. , vol.79 , pp. 9069-9080
    • Saunders, C.J.1
  • 54
    • 34848864584 scopus 로고    scopus 로고
    • Development of an HIV-1 reference panel of subtype B envelope clones isolated from the plasma of recently infected individuals
    • Schweighardt B, et al. 2007. Development of an HIV-1 reference panel of subtype B envelope clones isolated from the plasma of recently infected individuals. J. Acquir. Immune Defic. Syndr. 46:1-11.
    • (2007) J. Acquir. Immune Defic. Syndr. , vol.46 , pp. 1-11
    • Schweighardt, B.1
  • 55
    • 73949127978 scopus 로고    scopus 로고
    • Tiered categorization of a diverse panel of HIV-1 Env pseudoviruses for assessment of neutralizing antibodies
    • Seaman MS, et al. 2010. Tiered categorization of a diverse panel of HIV-1 Env pseudoviruses for assessment of neutralizing antibodies. J. Virol. 84:1439-1452.
    • (2010) J. Virol. , vol.84 , pp. 1439-1452
    • Seaman, M.S.1
  • 56
    • 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 MD, et al. 2009. Human immunodeficiency virus type 1 elite neutralizers: individuals with broad and potent neutralizing activity identified by using a high-throughput neutralization assay together with an analytical selection algorithm. J. Virol. 83:7337-7348.
    • (2009) J. Virol. , vol.83 , pp. 7337-7348
    • Simek, M.D.1
  • 57
    • 0031666180 scopus 로고    scopus 로고
    • An envelope modification that renders a primary, neutralization-resistant clade B human immunodeficiency virus type 1 isolate highly susceptible to neutralization by sera from other clades
    • Stamatatos L, Cheng-Mayer C. 1998. An envelope modification that renders a primary, neutralization-resistant clade B human immunodeficiency virus type 1 isolate highly susceptible to neutralization by sera from other clades. J. Virol. 72:7840-7845.
    • (1998) J. Virol. , vol.72 , pp. 7840-7845
    • Stamatatos, L.1    Cheng-Mayer, C.2
  • 58
    • 69149083668 scopus 로고    scopus 로고
    • Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine?
    • Stamatatos L, Morris L, Burton DR, Mascola JR. 2009. Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine? Nat. Med. 15:866-870.
    • (2009) Nat. Med. , vol.15 , pp. 866-870
    • Stamatatos, L.1    Morris, L.2    Burton, D.R.3    Mascola, J.R.4
  • 59
    • 0035701421 scopus 로고    scopus 로고
    • A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1
    • Stiegler G, et al. 2001. A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses 17:1757-1765.
    • (2001) AIDS Res. Hum. Retroviruses , vol.17 , pp. 1757-1765
    • Stiegler, G.1
  • 60
    • 0027256814 scopus 로고
    • Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali M, et al. 1993. Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol. 67:3978-3988.
    • (1993) J. Virol. , vol.67 , pp. 3978-3988
    • Thali, M.1
  • 61
    • 84864603281 scopus 로고    scopus 로고
    • Structural mechanism of trimeric HIV-1 envelope glycoprotein activation
    • doi:10.1371/journal.ppat.1002797
    • Tran EE, et al. 2012. Structural mechanism of trimeric HIV-1 envelope glycoprotein activation. PLoS Pathog. 8:e1002797. doi:10.1371/journal.ppat.1002797.
    • (2012) PLoS Pathog. , vol.8
    • Tran, E.E.1
  • 62
    • 77950816445 scopus 로고    scopus 로고
    • Two N-linked glycosylation sites in the V2 and C2 regions of human immunodeficiency virus type 1 CRF01_AE envelope glycoprotein gp120 regulate viral neutralization susceptibility to the human monoclonal antibody specific for the CD4 binding domain
    • Utachee P, et al. 2010. Two N-linked glycosylation sites in the V2 and C2 regions of human immunodeficiency virus type 1 CRF01_AE envelope glycoprotein gp120 regulate viral neutralization susceptibility to the human monoclonal antibody specific for the CD4 binding domain. J. Virol. 84:4311-4320.
    • (2010) J. Virol. , vol.84 , pp. 4311-4320
    • Utachee, P.1
  • 63
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, et al. 2009. Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326:285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1
  • 64
    • 0037456827 scopus 로고    scopus 로고
    • Antibody neutralization and escape by HIV-1
    • Wei X, et al. 2003. Antibody neutralization and escape by HIV-1. Nature 422:307-312.
    • (2003) Nature , vol.422 , pp. 307-312
    • Wei, X.1
  • 65
    • 0023018865 scopus 로고
    • Variable and conserved neutralization antigens of human immunodeficiency virus
    • Weiss RA, et al. 1986. Variable and conserved neutralization antigens of human immunodeficiency virus. Nature 324:572-575.
    • (1986) Nature , vol.324 , pp. 572-575
    • Weiss, R.A.1
  • 66
    • 33846623260 scopus 로고    scopus 로고
    • Development and characterization of a novel single-cycle recombinant-virus assay to determine human immunodeficiency virus type 1 coreceptor tropism
    • Whitcomb JM, et al. 2007. Development and characterization of a novel single-cycle recombinant-virus assay to determine human immunodeficiency virus type 1 coreceptor tropism. Antimicrob. Agents Chemother. 51:566-575.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 566-575
    • Whitcomb, J.M.1
  • 67
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu X, et al. 2010. Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 329:856-861.
    • (2010) Science , vol.329 , pp. 856-861
    • Wu, X.1
  • 68
    • 70350320690 scopus 로고    scopus 로고
    • Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment
    • Wu X, et al. 2009. Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment. J. Virol. 83:10892-10907.
    • (2009) J. Virol. , vol.83 , pp. 10892-10907
    • Wu, X.1
  • 69
    • 80052942203 scopus 로고    scopus 로고
    • Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    • Wu X, et al. 2011. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 333:1593-1602.
    • (2011) Science , vol.333 , pp. 1593-1602
    • Wu, X.1
  • 70
    • 0036436313 scopus 로고    scopus 로고
    • Characterization of CD4-induced epitopes on the HIV type 1 gp120 envelope glycoprotein recognized by neutralizing human monoclonal antibodies
    • Xiang SH, Doka N, Choudhary RK, Sodroski J, Robinson JE. 2002. Characterization of CD4-induced epitopes on the HIV type 1 gp120 envelope glycoprotein recognized by neutralizing human monoclonal antibodies. AIDS Res. Hum. Retroviruses 18:1207-1217.
    • (2002) AIDS Res. Hum. Retroviruses , vol.18 , pp. 1207-1217
    • Xiang, S.H.1    Doka, N.2    Choudhary, R.K.3    Sodroski, J.4    Robinson, J.E.5
  • 71
    • 77949401834 scopus 로고    scopus 로고
    • A V3 loop-dependent gp120 element disrupted by CD4 binding stabilizes the human immunodeficiency virus envelope glycoprotein trimer
    • Xiang SH, et al. 2010. A V3 loop-dependent gp120 element disrupted by CD4 binding stabilizes the human immunodeficiency virus envelope glycoprotein trimer. J. Virol. 84:3147-3161.
    • (2010) J. Virol. , vol.84 , pp. 3147-3161
    • Xiang, S.H.1
  • 72
    • 33847101745 scopus 로고    scopus 로고
    • Structural definition of a conserved neutralization epitope on HIV-1 gp120
    • Zhou T, et al. 2007. Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature 445:732-737.
    • (2007) Nature , vol.445 , pp. 732-737
    • Zhou, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.