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Volumn 85, Issue 19, 2011, Pages 9887-9898

Cross-Clade HIV-1 neutralizing antibodies induced with V3-scaffold protein immunogens following priming with gp120 DNA

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CHOLERA TOXIN B SUBUNIT; GLYCOPROTEIN GP 120; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; NEUTRALIZING ANTIBODY; PROLINE; SCAFFOLD PROTEIN; VIRUS ANTIGEN; VIRUS ENVELOPE PROTEIN;

EID: 80053952246     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05086-11     Document Type: Article
Times cited : (52)

References (74)
  • 2
    • 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. 2007. 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. 178:4424-4435.
    • (2007) J. Immunol. , vol.178 , pp. 4424-4435
    • Alam, S.M.1
  • 3
    • 77954191991 scopus 로고    scopus 로고
    • Structural conservation predominates over sequence variability in the crown of HIV-1'S V3 loop
    • Almond, D., et al. 2010. Structural conservation predominates over sequence variability in the crown of HIV-1'S V3 loop. AIDS Res. Hum. Retroviruses 26:717-723.
    • (2010) AIDS Res. Hum. Retroviruses , vol.26 , pp. 717-723
    • Almond, D.1
  • 4
    • 0031968725 scopus 로고    scopus 로고
    • Passive immunization with a human immunodeficiency virus type-1 neutralizing monoclonal antibody in Hu-PBL-SCID mice: isolation of a neutralization escape variant
    • Andrus, L., et al. 1998. Passive immunization with a human immunodeficiency virus type-1 neutralizing monoclonal antibody in Hu-PBL-SCID mice: isolation of a neutralization escape variant. J. Infect. Dis. 177:889-897.
    • (1998) J. Infect. Dis. , vol.177 , pp. 889-897
    • Andrus, L.1
  • 5
    • 0028839185 scopus 로고
    • Characterization of an internal permissive site in the cholera toxin B-subunit and insertion of epitopes from human immunodeficiency virus-1, hepatitis B virus and enterotoxigenic Escherichia coli
    • Backstrom, M., J. Holmgren, F. Schodel, and M. Lebens. 1995. Characterization of an internal permissive site in the cholera toxin B-subunit and insertion of epitopes from human immunodeficiency virus-1, hepatitis B virus and enterotoxigenic Escherichia coli. Gene 165:163-171.
    • (1995) Gene , vol.165 , pp. 163-171
    • Backstrom, M.1    Holmgren, J.2    Schodel, F.3    Lebens, M.4
  • 6
    • 0028109491 scopus 로고
    • Insertion of a HIV-1-neutralizing epitope in a surface-exposed internal region of the cholera toxin B-subunit
    • Backstrom, M., M. Lebens, F. Schodel, and J. Holmgren. 1994. Insertion of a HIV-1-neutralizing epitope in a surface-exposed internal region of the cholera toxin B-subunit. Gene 149:211-217.
    • (1994) Gene , vol.149 , pp. 211-217
    • Backstrom, M.1    Lebens, M.2    Schodel, F.3    Holmgren, J.4
  • 7
    • 77952688015 scopus 로고    scopus 로고
    • Antibody-mediated protection against mucosal simian-human immunodeficiency virus challenge of macaques immunized with alphavirus replicon particles and boosted with trimeric envelope glycoprotein in MF59 adjuvant
    • Barnett, S. W., et al. 2010. Antibody-mediated protection against mucosal simian-human immunodeficiency virus challenge of macaques immunized with alphavirus replicon particles and boosted with trimeric envelope glycoprotein in MF59 adjuvant. J. Virol. 84:5975-5985.
    • (2010) J. Virol. , vol.84 , pp. 5975-5985
    • Barnett, S.W.1
  • 8
    • 21644445378 scopus 로고    scopus 로고
    • Evaluating the immunogenicity of a disulfidestabilized, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1
    • Beddows, S., et al. 2005. Evaluating the immunogenicity of a disulfidestabilized, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1. J. Virol. 79:8812-8827.
    • (2005) J. Virol. , vol.79 , pp. 8812-8827
    • Beddows, S.1
  • 9
    • 0028024901 scopus 로고
    • Neutralizing antibodies to HIV-1 in seronegative volunteers immunized with recombinant gp120 from the MN strain of HIV-1
    • Belshe, R. B., et al. 1994. Neutralizing antibodies to HIV-1 in seronegative volunteers immunized with recombinant gp120 from the MN strain of HIV-1. NIAID AIDS Vaccine Clinical Trials Network. JAMA 272:475-480.
    • (1994) NIAID AIDS Vaccine Clinical Trials Network. JAMA , vol.272 , pp. 475-480
    • Belshe, R.B.1
  • 10
    • 0028213153 scopus 로고
    • Comparison of the immune response to recombinant gp120 in humans and chimpanzees
    • Berman, P. W., et al. 1994. Comparison of the immune response to recombinant gp120 in humans and chimpanzees. AIDS 8:591-601.
    • (1994) AIDS , vol.8 , pp. 591-601
    • Berman, P.W.1
  • 11
    • 77953752637 scopus 로고    scopus 로고
    • Vaccination with peptide mimetics of the gp41 prehairpin fusion intermediate yields neutralizing antisera against HIV-1 isolates
    • Bianchi, E., et al. 2010. Vaccination with peptide mimetics of the gp41 prehairpin fusion intermediate yields neutralizing antisera against HIV-1 isolates. Proc. Natl. Acad. Sci. U. S. A. 107:10655-10660.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 10655-10660
    • Bianchi, E.1
  • 12
    • 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. 2008. Profiling the specificity of neutralizing antibodies in a large panel of plasmas from patients chronically infected with human immunodeficiency virus type 1 subtypes B and C. J. Virol. 82:11651-11668.
    • (2008) J. Virol. , vol.82 , pp. 11651-11668
    • Binley, J.M.1
  • 13
    • 70350714115 scopus 로고    scopus 로고
    • Structural basis of the cross-reactivity of genetically related human anti-HIV-1 monoclonal antibodies: implications for design of V3-based immunogens
    • Burke, V., et al. 2009. Structural basis of the cross-reactivity of genetically related human anti-HIV-1 monoclonal antibodies: implications for design of V3-based immunogens. Structure 17:1538-1546.
    • (2009) Structure , vol.17 , pp. 1538-1546
    • Burke, V.1
  • 14
    • 64849086846 scopus 로고    scopus 로고
    • Worldwide distribution of neutralizing 447-52D and 2219 antibody epitopes in HIV-1
    • Cardozo, T., et al. 2009. Worldwide distribution of neutralizing 447-52D and 2219 antibody epitopes in HIV-1. AIDS Res. Hum. Retroviruses 25:441-450.
    • (2009) AIDS Res. Hum. Retroviruses , vol.25 , pp. 441-450
    • Cardozo, T.1
  • 15
    • 0034703835 scopus 로고    scopus 로고
    • Antigenicity and immunogenicity of the HIV-1 gp41 epitope ELDKWA inserted into permissive sites of the MalE protein
    • Coeffier, E., et al. 2000. Antigenicity and immunogenicity of the HIV-1 gp41 epitope ELDKWA inserted into permissive sites of the MalE protein. Vaccine 19:684-693.
    • (2000) Vaccine , vol.19 , pp. 684-693
    • Coeffier, E.1
  • 16
    • 77956317558 scopus 로고    scopus 로고
    • Computational design of epitope-scaffolds allows induction of antibodies specific for a poorly immunogenic HIV vaccine epitope
    • Correia, B. E., et al. 2010. Computational design of epitope-scaffolds allows induction of antibodies specific for a poorly immunogenic HIV vaccine epitope. Structure 18:1116-1126.
    • (2010) Structure , vol.18 , pp. 1116-1126
    • Correia, B.E.1
  • 17
    • 78651388412 scopus 로고    scopus 로고
    • Non-neutralizing HIV-1 gp41 envelope cluster II human monoclonal antibodies show polyreactivity for binding to phospholipid and protein autoantigens
    • Dennison, S. M., et al. 2011. Non-neutralizing HIV-1 gp41 envelope cluster II human monoclonal antibodies show polyreactivity for binding to phospholipid and protein autoantigens. J. Virol. 85:1340-1347.
    • (2011) J. Virol , vol.85 , pp. 1340-1347
    • Dennison, S.M.1
  • 18
    • 45749150744 scopus 로고    scopus 로고
    • Structure determination of an anti-HIV-1 Fab 447-52D-peptide complex from an epitaxially twinned data set
    • Dhillon, A. K., et al. 2008. Structure determination of an anti-HIV-1 Fab 447-52D-peptide complex from an epitaxially twinned data set. Acta Crystallogr. D Biol. Crystallogr. 64:792-802.
    • (2008) Acta Crystallogr. D Biol. Crystallogr. , vol.64 , pp. 792-802
    • Dhillon, A.K.1
  • 19
    • 0029812316 scopus 로고    scopus 로고
    • Immunogenic presentation of a conserved gp41 epitope of human immunodeficiency virus type 1 on recombinant surface antigen of hepatitis B virus
    • Eckhart, L., et al. 1996. Immunogenic presentation of a conserved gp41 epitope of human immunodeficiency virus type 1 on recombinant surface antigen of hepatitis B virus. J. Gen. Virol. 77:2001-2008.
    • (1996) J. Gen. Virol. , vol.77 , pp. 2001-2008
    • Eckhart, L.1
  • 20
    • 33646723290 scopus 로고    scopus 로고
    • Anti-V3 humanized antibody KD-247 effectively suppresses ex vivo generation of human immunodeficiency virus type 1 and affords sterile protection of monkeys against a heterologous simian/human immunodeficiency virus infection
    • Eda, Y., et al. 2006. Anti-V3 humanized antibody KD-247 effectively suppresses ex vivo generation of human immunodeficiency virus type 1 and affords sterile protection of monkeys against a heterologous simian/human immunodeficiency virus infection. J. Virol. 80:5563-5570.
    • (2006) J. Virol. , vol.80 , pp. 5563-5570
    • Eda, Y.1
  • 21
    • 0026557112 scopus 로고
    • Prevention of HIV-1 infection in chimpanzees by gp120 V3 domain-specific monoclonal antibody
    • Emini, E. A., et al. 1992. Prevention of HIV-1 infection in chimpanzees by gp120 V3 domain-specific monoclonal antibody. Nature 355:728-730.
    • (1992) Nature , vol.355 , pp. 728-730
    • Emini, E.A.1
  • 22
    • 84887212581 scopus 로고    scopus 로고
    • International Network for Comparison of HIV Neutralization Assays: the NeutNet Report
    • Fenyo, E. M., et al. 2009. International Network for Comparison of HIV Neutralization Assays: the NeutNet Report. PLoS One 4:e4505.
    • (2009) PLoS One , vol.4
    • Fenyo, E.M.1
  • 23
    • 34248168722 scopus 로고    scopus 로고
    • Recombinant gp120 vaccine-induced antibodies inhibit clinical strains of HIV-1 in the presence of Fc receptor-bearing effector cells and correlate inversely with HIV infection rate
    • Forthal, D. N., P. B. Gilbert, G. Landucci, and T. Phan. 2007. Recombinant gp120 vaccine-induced antibodies inhibit clinical strains of HIV-1 in the presence of Fc receptor-bearing effector cells and correlate inversely with HIV infection rate. J. Immunol. 178:6596-6603.
    • (2007) J. Immunol. , vol.178 , pp. 6596-6603
    • Forthal, D.N.1    Gilbert, P.B.2    Landucci, G.3    Phan, T.4
  • 24
    • 0028950509 scopus 로고
    • Preand postexposure protection against human immunodeficiency virus type 1 infection mediated by a monoclonal antibody
    • Gauduin, M. C., J. T. Safrit, R. Weir, M. S. Fung, and R. A. Koup. 1995. Preand postexposure protection against human immunodeficiency virus type 1 infection mediated by a monoclonal antibody. J. Infect. Dis. 171:1203-1209.
    • (1995) J. Infect. Dis. , vol.171 , pp. 1203-1209
    • Gauduin, M.C.1    Safrit, J.T.2    Weir, R.3    Fung, M.S.4    Koup, R.A.5
  • 25
    • 77954722964 scopus 로고    scopus 로고
    • Magnitude and breadth of a nonprotective neutralizing antibody response in an efficacy trial of a candidate HIV-1 gp120 vaccine
    • Gilbert, P., et al. 2010. Magnitude and breadth of a nonprotective neutralizing antibody response in an efficacy trial of a candidate HIV-1 gp120 vaccine. J. Infect. Dis. 202:595-605.
    • (2010) J. Infect. Dis. , vol.202 , pp. 595-605
    • Gilbert, P.1
  • 26
    • 13944250922 scopus 로고    scopus 로고
    • Correlation between immunologic responses to a recombinant glycoprotein 120 vaccine and incidence of HIV-1 infection in a phase 3 HIV-1 preventive vaccine trial
    • Gilbert, P. B., et al. 2005. Correlation between immunologic responses to a recombinant glycoprotein 120 vaccine and incidence of HIV-1 infection in a phase 3 HIV-1 preventive vaccine trial. J. Infect. Dis. 191:666-677.
    • (2005) J. Infect. Dis. , vol.191 , pp. 666-677
    • Gilbert, P.B.1
  • 27
    • 10744228558 scopus 로고    scopus 로고
    • The V3 loop is accessible on the surface of most human immunodeficiency virus type 1 primary isolates and serves as a neutralization epitope
    • Gorny, M. K., et al. 2004. The V3 loop is accessible on the surface of most human immunodeficiency virus type 1 primary isolates and serves as a neutralization epitope. J. Virol. 78:2394-2404.
    • (2004) J. Virol , vol.78 , pp. 2394-2404
    • Gorny, M.K.1
  • 28
    • 59249105235 scopus 로고    scopus 로고
    • Preferential use of the VH5-51 gene segment by the human immune response to code for antibodies against the V3 domain of HIV-1
    • Gorny, M. K., et al. 2009. Preferential use of the VH5-51 gene segment by the human immune response to code for antibodies against the V3 domain of HIV-1. Mol. Immunol. 46:917-926.
    • (2009) Mol. Immunol. , vol.46 , pp. 917-926
    • Gorny, M.K.1
  • 29
    • 0036720793 scopus 로고    scopus 로고
    • Human monoclonal antibodies specific for conformation-sensitive epitopes of V3 neutralize HIV-1 primary isolates from various clades
    • Gorny, M. K., et al. 2002. Human monoclonal antibodies specific for conformation-sensitive epitopes of V3 neutralize HIV-1 primary isolates from various clades. J. Virol. 76:9035-9045.
    • (2002) J. Virol. , vol.76 , pp. 9035-9045
    • Gorny, M.K.1
  • 30
    • 33745785048 scopus 로고    scopus 로고
    • Cross-clade neutralizing activity of human anti-V3 monoclonal antibodies derived from the cells of individuals infected with non-B clades of HIV-1
    • Gorny, M. K., et al. 2006. Cross-clade neutralizing activity of human anti-V3 monoclonal antibodies derived from the cells of individuals infected with non-B clades of HIV-1. J. Virol. 80:6865-6872.
    • (2006) J. Virol. , vol.80 , pp. 6865-6872
    • Gorny, M.K.1
  • 31
    • 79551556431 scopus 로고    scopus 로고
    • Heterologous epitope-scaffold prime: boosting immuno-focuses B cell responses to the HIV-1 gp41 2F5 neutralization determinant
    • Guenaga, J., et al. 2011. Heterologous epitope-scaffold prime: boosting immuno-focuses B cell responses to the HIV-1 gp41 2F5 neutralization determinant. PLoS One 6:e16074.
    • (2011) PLoS One , vol.6
    • Guenaga, J.1
  • 32
    • 0026555178 scopus 로고
    • Native but not denatured recombinant human immunodeficiency virus type 1 gp120 generates broad-spectrum neutralizing antibodies in baboons
    • Haigwood, N. L., et al. 1992. Native but not denatured recombinant human immunodeficiency virus type 1 gp120 generates broad-spectrum neutralizing antibodies in baboons. J. Virol. 66:172-182.
    • (1992) J. Virol. , vol.66 , pp. 172-182
    • Haigwood, N.L.1
  • 34
    • 77954110431 scopus 로고    scopus 로고
    • Anti-V3 monoclonal antibodies display broad neutralizing activities against multiple HIV-1 subtypes
    • Hioe, C. E., et al. 2010. Anti-V3 monoclonal antibodies display broad neutralizing activities against multiple HIV-1 subtypes. PLoS One 5:e10254.
    • (2010) PLoS One , vol.5
    • Hioe, C.E.1
  • 35
    • 77952922044 scopus 로고    scopus 로고
    • Simultaneous evaluation of the magnitude and breadth of a left and right censored multivariate response, with application to HIV vaccine development
    • Huang, Y., P. B. Gilbert, D. C. Montefiori, and S. G. Self. 2009. Simultaneous evaluation of the magnitude and breadth of a left and right censored multivariate response, with application to HIV vaccine development. Stat. Biopharm. Res. 1:81-91.
    • (2009) Stat. Biopharm. Res. , vol.1 , pp. 81-91
    • Huang, Y.1    Gilbert, P.B.2    Montefiori, D.C.3    Self, S.G.4
  • 36
    • 77955417928 scopus 로고    scopus 로고
    • Conserved structural elements in the V3 crown of HIV-1 GP120
    • Jiang, X., et al. 2010. Conserved structural elements in the V3 crown of HIV-1 GP120. Nat. Struct. Mol. Biol. 17:955-961.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 955-961
    • Jiang, X.1
  • 37
    • 67650741139 scopus 로고    scopus 로고
    • Structural and immunogenicity studies of a cleaved, stabilized envelope trimer derived from subtype A HIV-1
    • Kang, Y. K., et al. 2009. Structural and immunogenicity studies of a cleaved, stabilized envelope trimer derived from subtype A HIV-1. Vaccine 27:5120-5132.
    • (2009) Vaccine , vol.27 , pp. 5120-5132
    • Kang, Y.K.1
  • 39
    • 0037069682 scopus 로고    scopus 로고
    • HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites
    • Kwong, P. D., et al. 2002. HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature 420:678-682.
    • (2002) Nature , vol.420 , pp. 678-682
    • Kwong, P.D.1
  • 40
    • 17344391461 scopus 로고    scopus 로고
    • Safety and pharmacokinetics of hyperimmune anti-human immunodeficiency virus (HIV) immunoglobulin administered to HIV-infected pregnant women and their newborns
    • Lambert, J. S., et al. 1997. Safety and pharmacokinetics of hyperimmune anti-human immunodeficiency virus (HIV) immunoglobulin administered to HIV-infected pregnant women and their newborns. J. Infect. Dis. 175:283-291.
    • (1997) J. Infect. Dis. , vol.175 , pp. 283-291
    • Lambert, J.S.1
  • 41
    • 34247166722 scopus 로고    scopus 로고
    • Antigenic and immunogenic study of membrane-proximal external region-grafted gp120 antigens by a DNA prime-protein boost immunization strategy
    • Law, M., R. M. Cardoso, I. A. Wilson, and D. R. Burton. 2007. Antigenic and immunogenic study of membrane-proximal external region-grafted gp120 antigens by a DNA prime-protein boost immunization strategy. J. Virol. 81:4272-4285.
    • (2007) J. Virol. , vol.81 , pp. 4272-4285
    • Law, M.1    Cardoso, R.M.2    Wilson, I.A.3    Burton, D.R.4
  • 42
    • 23244434512 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 env clones from acute and early subtype B infections for standardized assessments of vaccineelicited 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 vaccineelicited neutralizing antibodies. J. Virol. 79:10108-10125.
    • (2005) J. Virol. , vol.79 , pp. 10108-10125
    • Li, M.1
  • 43
    • 33751224478 scopus 로고    scopus 로고
    • Genetic and neutralization properties of subtype C human immunodeficiency virus type 1 molecular env clones from acute and early heterosexually acquired infections in Southern Africa
    • Li, M., et al. 2006. Genetic and neutralization properties of subtype C human immunodeficiency virus type 1 molecular env clones from acute and early heterosexually acquired infections in Southern Africa. J. Virol. 80:11776-11790.
    • (2006) J. Virol. , vol.80 , pp. 11776-11790
    • Li, M.1
  • 44
    • 67049086871 scopus 로고    scopus 로고
    • Heterologous prime-boost vaccination
    • Lu, S. 2009. Heterologous prime-boost vaccination. Curr. Opin. Immunol. 21:346-351.
    • (2009) Curr. Opin. Immunol. , vol.21 , pp. 346-351
    • Lu, S.1
  • 45
    • 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. 2000. Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus by passive infusion of neutralizing antibodies. Nat. Med. 6:207-210.
    • (2000) Nat. Med. , vol.6 , pp. 207-210
    • Mascola, J.R.1
  • 46
    • 58149487629 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 env trimer immunization of macaques and impact of priming with viral vector or stabilized core protein
    • Morner, A., et al. 2009. Human immunodeficiency virus type 1 env trimer immunization of macaques and impact of priming with viral vector or stabilized core protein. J. Virol. 83:540-551.
    • (2009) J. Virol. , vol.83 , pp. 540-551
    • Morner, A.1
  • 47
    • 77952299639 scopus 로고    scopus 로고
    • An optimally constrained V3 peptide is a better immunogen than its linear homolog or HIV-1 gp120
    • Moseri, A., et al. 2010. An optimally constrained V3 peptide is a better immunogen than its linear homolog or HIV-1 gp120. Virology 401:293-304.
    • (2010) Virology , vol.401 , pp. 293-304
    • Moseri, A.1
  • 48
    • 0028235930 scopus 로고
    • Cross-neutralizing antibodies against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS
    • Muster, T., et al. 1994. Cross-neutralizing antibodies against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS. J. Virol. 68:4031-4034.
    • (1994) J. Virol. , vol.68 , pp. 4031-4034
    • Muster, T.1
  • 49
    • 77949370078 scopus 로고    scopus 로고
    • Breadth of neutralizing antibodies elicited by stable, homogeneous clade A and clade C HIV-1 gp140 envelope trimers in guinea pigs
    • Nkolola, J. P., et al. 2010. Breadth of neutralizing antibodies elicited by stable, homogeneous clade A and clade C HIV-1 gp140 envelope trimers in guinea pigs. J. Virol. 84:3270-3279.
    • (2010) J. Virol. , vol.84 , pp. 3270-3279
    • Nkolola, J.P.1
  • 50
    • 78149242586 scopus 로고    scopus 로고
    • Elicitation of structure-specific antibodies by epitope scaffolds
    • Ofek, G., et al. 2010. Elicitation of structure-specific antibodies by epitope scaffolds. Proc. Natl. Acad. Sci. U. S. A. 107:17880-17887.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 17880-17887
    • Ofek, G.1
  • 51
    • 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., et al. 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
  • 52
    • 33845433434 scopus 로고    scopus 로고
    • Randomized, double-blind, placebo-controlled efficacy trial of a bivalent recombinant glycoprotein 120 HIV-1 vaccine among injection drug users in Bangkok
    • Pitisuttithum, P., et al. 2006. Randomized, double-blind, placebo-controlled efficacy trial of a bivalent recombinant glycoprotein 120 HIV-1 vaccine among injection drug users in Bangkok, Thailand. J. Infect. Dis. 194:1661-1671.
    • (2006) Thailand. J. Infect. Dis. , vol.194 , pp. 1661-1671
    • Pitisuttithum, P.1
  • 53
    • 34248194943 scopus 로고    scopus 로고
    • Structure of a high-affinity "mimotope" peptide bound to HIV-1-neutralizing antibody b12 explains its inability to elicit gp120 cross-reactive antibodies
    • Saphire, E. O., et al. 2007. Structure of a high-affinity "mimotope" peptide bound to HIV-1-neutralizing antibody b12 explains its inability to elicit gp120 cross-reactive antibodies. J. Mol. Biol. 369:696-709.
    • (2007) J. Mol. Biol. , vol.369 , pp. 696-709
    • Saphire, E.O.1
  • 54
    • 58149487645 scopus 로고    scopus 로고
    • Factors associated with the development of crossreactive neutralizing antibodies during human immunodeficiency virus type 1 infection
    • Sather, D. N., 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
  • 55
    • 63849131879 scopus 로고    scopus 로고
    • Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals
    • Scheid, J. F., et al. 2009. Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals. Nature 458:636-640.
    • (2009) Nature , vol.458 , pp. 636-640
    • Scheid, J.F.1
  • 56
    • 73949127978 scopus 로고    scopus 로고
    • Tiered categorization of a diverse panel of HIV-1 Env pseudoviruses for assessment of neutralizing antibodies
    • Seaman, M. S., 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
  • 57
    • 25144477447 scopus 로고    scopus 로고
    • Comparing antigenicity and immunogenicity of engineered gp120
    • Selvarajah, S., et al. 2005. Comparing antigenicity and immunogenicity of engineered gp120. J. Virol. 79:12148-12163.
    • (2005) J. Virol. , vol.79 , pp. 12148-12163
    • Selvarajah, S.1
  • 58
    • 39549097297 scopus 로고    scopus 로고
    • Focused dampening of antibody response to the immunodominant variable loops by engineered soluble gp140
    • Selvarajah, S., et al. 2008. Focused dampening of antibody response to the immunodominant variable loops by engineered soluble gp140. AIDS Res. Hum. Retroviruses 24:301-314.
    • (2008) AIDS Res. Hum. Retroviruses , vol.24 , pp. 301-314
    • Selvarajah, S.1
  • 59
    • 77957840131 scopus 로고    scopus 로고
    • Comparative immunogenicity of HIV-1 clade C envelope proteins for prime/boost studies
    • Smith, D. H., et al. 2010. Comparative immunogenicity of HIV-1 clade C envelope proteins for prime/boost studies. PLoS One 5:e12076.
    • (2010) PLoS One , vol.5
    • Smith, D.H.1
  • 60
    • 1242351232 scopus 로고    scopus 로고
    • Structural rationale for the broad neutralization of HIV-1 by human antibody 447-52D
    • Stanfield, R. L., M. K. Gorny, C. Williams, S. Zolla-Pazner, and I. A. Wilson. 2004. Structural rationale for the broad neutralization of HIV-1 by human antibody 447-52D. Structure 12:193-204.
    • (2004) Structure , vol.12 , pp. 193-204
    • Stanfield, R.L.1    Gorny, M.K.2    Williams, C.3    Zolla-Pazner, S.4    Wilson, I.A.5
  • 61
    • 33744933182 scopus 로고    scopus 로고
    • Crystal structures of HIV-1 neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity
    • Stanfield, R. L., M. K. Gorny, S. Zolla-Pazner, and I. A. Wilson. 2006. Crystal structures of HIV-1 neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity. J. Virol. 80:6093-6105.
    • (2006) J. Virol. , vol.80 , pp. 6093-6105
    • Stanfield, R.L.1    Gorny, M.K.2    Zolla-Pazner, S.3    Wilson, I.A.4
  • 62
    • 34347347035 scopus 로고    scopus 로고
    • The impact of an AIDS vaccine in developing countries: a new model and initial results
    • Stover, J., L. Bollinger, R. Hecht, C. Williams, and E. Roca. 2007. The impact of an AIDS vaccine in developing countries: a new model and initial results. Health Aff. (Millwood) 26:1147-1158.
    • (2007) Health Aff. (Millwood) , vol.26 , pp. 1147-1158
    • Stover, J.1    Bollinger, L.2    Hecht, R.3    Williams, C.4    Roca, E.5
  • 63
    • 77956261658 scopus 로고    scopus 로고
    • Soluble HIV-1 Env trimers in adjuvant elicit potent and diverse functional B cell responses in primates
    • Sundling, C., et al. 2010. Soluble HIV-1 Env trimers in adjuvant elicit potent and diverse functional B cell responses in primates. J. Exp. Med. 207:2003-2017.
    • (2010) J. Exp. Med , vol.207 , pp. 2003-2017
    • Sundling, C.1
  • 64
    • 78650833474 scopus 로고    scopus 로고
    • Comparative magnitude of cross-strain conservation of HIV variable loop neutralization epitopes
    • Swetnam, J., E. Shmelkov, S. Zolla-Pazner, and T. Cardozo. 2010. Comparative magnitude of cross-strain conservation of HIV variable loop neutralization epitopes. PLoS One 5:e15994.
    • (2010) PLoS One , vol.5
    • Swetnam, J.1    Shmelkov, E.2    Zolla-Pazner, S.3    Cardozo, T.4
  • 65
    • 77955517998 scopus 로고    scopus 로고
    • Strategies for eliciting HIV-1 inhibitory antibodies
    • Tomaras, G. D., and B. F. Haynes. 2010. Strategies for eliciting HIV-1 inhibitory antibodies. Curr. Opin. HIV AIDS 5:421-427.
    • (2010) Curr. Opin. HIV AIDS , vol.5 , pp. 421-427
    • Tomaras, G.D.1    Haynes, B.F.2
  • 66
    • 77955657135 scopus 로고    scopus 로고
    • Structure-guided design and immunological characterization of immunogens presenting the HIV-1 gp120 V3 loop on a CTB scaffold
    • Totrov, M., et al. 2010. Structure-guided design and immunological characterization of immunogens presenting the HIV-1 gp120 V3 loop on a CTB scaffold. Virology 405:513-523.
    • (2010) Virology , vol.405 , pp. 513-523
    • Totrov, M.1
  • 67
    • 79955381435 scopus 로고    scopus 로고
    • Two closely related Env antigens from the same patient elicited different spectra of neutralizing antibodies against heterologous HIV-1 isolates
    • Vaine, M., et al. 2011. Two closely related Env antigens from the same patient elicited different spectra of neutralizing antibodies against heterologous HIV-1 isolates. J. Virol. 85:4927-4936.
    • (2011) J. Virol. , vol.85 , pp. 4927-4936
    • Vaine, M.1
  • 68
    • 0034856156 scopus 로고    scopus 로고
    • Additive effects characterize the interaction of antibodies involved in neutralization of the primary dualtropic human immunodeficiency virus type 1 isolate 89
    • Verrier, F., A. Nadas, M. K. Gorny, and S. Zolla-Pazner. 2001. Additive effects characterize the interaction of antibodies involved in neutralization of the primary dualtropic human immunodeficiency virus type 1 isolate 89.6. J. Virol. 75:9177-9186.
    • (2001) 6. J. Virol. , vol.75 , pp. 9177-9186
    • Verrier, F.1    Nadas, A.2    Gorny, M.K.3    Zolla-Pazner, S.4
  • 69
    • 76449108010 scopus 로고    scopus 로고
    • Neutralizing antibody titers conferring protection to macaques from a simian/human immunodeficiency virus challenge using the TZM-bl assay
    • Willey, R., M. C. Nason, Y. Nishimura, D. A. Follmann, and M. A. Martin. 2010. Neutralizing antibody titers conferring protection to macaques from a simian/human immunodeficiency virus challenge using the TZM-bl assay. AIDS Res. Hum. Retroviruses 26:89-98.
    • (2010) AIDS Res. Hum. Retroviruses 26 , pp. 89-98
    • Willey, R.1    Nason, M.C.2    Nishimura, Y.3    Follmann, D.A.4    Martin, M.A.5
  • 70
    • 34547154404 scopus 로고    scopus 로고
    • Extensively cross-reactive anti-HIV-1 neutralizing antibodies induced by gp140 immunization
    • Zhang, P. F., et al. 2007. Extensively cross-reactive anti-HIV-1 neutralizing antibodies induced by gp140 immunization. Proc. Natl. Acad. Sci. U. S. A. 104:10193-10198.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 10193-10198
    • Zhang, P.F.1
  • 71
    • 77954100808 scopus 로고    scopus 로고
    • Structure-function relationships of HIV-1 envelope sequence-variable regions provide a paradigm for vaccine design
    • Zolla-Pazner, S., and T. Cardozo. 2010. Structure-function relationships of HIV-1 envelope sequence-variable regions provide a paradigm for vaccine design. Nat. Rev. Immunol. 10:527-535.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 527-535
    • Zolla-Pazner, S.1    Cardozo, T.2
  • 72
    • 69249210887 scopus 로고    scopus 로고
    • Cross-clade neutralizing antibodies against HIVI-1 induced in rabbits by focusing the immune response on a neutralizing epitope
    • Zolla-Pazner, S., et al. 2009. Cross-clade neutralizing antibodies against HIVI-1 induced in rabbits by focusing the immune response on a neutralizing epitope. Virology 392:82-93.
    • (2009) Virology , vol.392 , pp. 82-93
    • Zolla-Pazner, S.1
  • 73
    • 39449107834 scopus 로고    scopus 로고
    • Focusing the immune response on the V3 loop, a neutralizing epitope of the HIV-1 gp120 envelope
    • Zolla-Pazner, S., et al. 2008. Focusing the immune response on the V3 loop, a neutralizing epitope of the HIV-1 gp120 envelope. Virology 372:233-246.
    • (2008) Virology , vol.372 , pp. 233-246
    • Zolla-Pazner, S.1
  • 74
    • 0035202616 scopus 로고    scopus 로고
    • Neutralization synergy of human immunodeficiency virus type 1 primary isolates by cocktails of broadly neutralizing antibodies
    • Zwick, M. B., et al. 2001. Neutralization synergy of human immunodeficiency virus type 1 primary isolates by cocktails of broadly neutralizing antibodies. J. Virol. 75:12198-12208.
    • (2001) J. Virol. , vol.75 , pp. 12198-12208
    • Zwick, M.B.1


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