메뉴 건너뛰기




Volumn 79, Issue 2, 2005, Pages 1252-1261

Anti-human immunodeficiency virus type 1 (HIV-1) antibodies 2F5 and 4E10 require surprisingly few crucial residues in the membrane-proximal external region of glycoprotein gp41 to neutralize HIV-1

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ANTIGEN; ASPARTIC ACID; EPITOPE; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; GLYCOPROTEIN GP 41 MEMBRANE PROXIMAL EXTERNAL REGION; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; LYSINE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 2F5; MONOCLONAL ANTIBODY 4E10; MONOCLONAL ANTIBODY B12; NEUTRALIZING ANTIBODY; PEPTIDE; PEPTIDE T20; PHENYLALANINE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 11144227042     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.2.1252-1261.2005     Document Type: Article
Times cited : (237)

References (81)
  • 1
    • 0037067741 scopus 로고    scopus 로고
    • HIV-1 gp41 envelope residues 650-685 exposed on native virus act as a lectin to bind epithelial cell galactosyl ceramide
    • Alfsen, A., and M. Bomsel. 2002. HIV-1 gp41 envelope residues 650-685 exposed on native virus act as a lectin to bind epithelial cell galactosyl ceramide. J. Biol. Chem. 277:25649-25659.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25649-25659
    • Alfsen, A.1    Bomsel, M.2
  • 3
    • 0038076112 scopus 로고    scopus 로고
    • Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions
    • Binley, J. M., C. S. Cayanan, C. Wiley, N. Schulke, W. C. Olson, and D. R. Burton. 2003. Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions. J. Virol. 77:5678-5684.
    • (2003) J. Virol. , vol.77 , pp. 5678-5684
    • Binley, J.M.1    Cayanan, C.S.2    Wiley, C.3    Schulke, N.4    Olson, W.C.5    Burton, D.R.6
  • 4
    • 0029957873 scopus 로고    scopus 로고
    • Human antibody responses to HIV type 1 glycoprotein 41 cloned in phage display libraries suggest three major epitopes are recognized and give evidence for conserved antibody motifs in antigen binding
    • Binley, J. M., H. J. Ditzel, C. F. Barbas, 3rd, N. Sullivan, J. Sodroski, P. W. Parren, and D. R. Burton. 1996. Human antibody responses to HIV type 1 glycoprotein 41 cloned in phage display libraries suggest three major epitopes are recognized and give evidence for conserved antibody motifs in antigen binding. AIDS Res. Hum. Retroviruses 12:911-924.
    • (1996) AIDS Res. Hum. Retroviruses , vol.12 , pp. 911-924
    • Binley, J.M.1    Ditzel, H.J.2    Barbas III, C.F.3    Sullivan, N.4    Sodroski, J.5    Parren, P.W.6    Burton, D.R.7
  • 5
    • 0037159248 scopus 로고    scopus 로고
    • A monomeric 3(10)-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41
    • Biron, Z., S. Khare, A. O. Samson, Y. Hayek, F. Naider, and J. Anglister. 2002. A monomeric 3(10)-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41. Biochemistry 41:12687-12696.
    • (2002) Biochemistry , vol.41 , pp. 12687-12696
    • Biron, Z.1    Khare, S.2    Samson, A.O.3    Hayek, Y.4    Naider, F.5    Anglister, J.6
  • 7
    • 0038082126 scopus 로고    scopus 로고
    • Multiple interactions across the surface of the gp120 core structure determine the global neutralization resistance phenotype of human immunodeficiency virus type 1
    • Bouma, P., M. Leavitt, P. F. Zhang, I. A. Sidorov, D. S. Dimitrov, and G. V. Quinnan, Jr. 2003. Multiple interactions across the surface of the gp120 core structure determine the global neutralization resistance phenotype of human immunodeficiency virus type 1. J. Virol. 77:8061-8071.
    • (2003) J. Virol. , vol.77 , pp. 8061-8071
    • Bouma, P.1    Leavitt, M.2    Zhang, P.F.3    Sidorov, I.A.4    Dimitrov, D.S.5    Quinnan Jr., G.V.6
  • 12
    • 0027499917 scopus 로고
    • Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein
    • Cao, J., L. Bergeron, E. Helseth, M. Thali, H. Repke, and J. Sodroski. 1993. Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein. J. Virol. 67: 2747-2755.
    • (1993) J. Virol. , vol.67 , pp. 2747-2755
    • Cao, J.1    Bergeron, L.2    Helseth, E.3    Thali, M.4    Repke, H.5    Sodroski, J.6
  • 13
    • 10044240082 scopus 로고    scopus 로고
    • Structural insights for 4E10 antibody neutralization on HIV-1
    • 18-21 Sept. 2003, New York, N.Y. (abstract)
    • Cardoso, R., M. Zwick, R. Kunert, H. Katinger, D. R. Burton, and I. Wilson. 2003. Structural insights for 4E10 antibody neutralization on HIV-1. AIDS Vaccine 2003, 18-21 Sept. 2003, New York, N.Y. (abstract).
    • (2003) AIDS Vaccine 2003
    • Cardoso, R.1    Zwick, M.2    Kunert, R.3    Katinger, H.4    Burton, D.R.5    Wilson, I.6
  • 14
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., D. Fass, J. M. Berger, and P. S. Kim. 1997. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89:263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 17
    • 0028842207 scopus 로고
    • Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes
    • Connor, R. I., B. K. Chen, S. Choe, and N. R. Landau. 1995. Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes. Virology 206:935-944.
    • (1995) Virology , vol.206 , pp. 935-944
    • Connor, R.I.1    Chen, B.K.2    Choe, S.3    Landau, N.R.4
  • 18
    • 1242342052 scopus 로고    scopus 로고
    • Binding of the 2F5 monoclonal antibody to native and fusion-intermediate forms of human immunodeficiency virus type 1 gp41: Implications for fusion-inducing conformational changes
    • de Rosny, E., R. Vassell, S. Jiang, R. Kunert, and C. D. Weiss. 2004. Binding of the 2F5 monoclonal antibody to native and fusion-intermediate forms of human immunodeficiency virus type 1 gp41: implications for fusion-inducing conformational changes. J. Virol. 78:2627-2631.
    • (2004) J. Virol. , vol.78 , pp. 2627-2631
    • De Rosny, E.1    Vassell, R.2    Jiang, S.3    Kunert, R.4    Weiss, C.D.5
  • 19
    • 0345060499 scopus 로고    scopus 로고
    • Role of the fusion peptide and membrane-proximal domain in HIV-1 envelope glycoprotein-mediated membrane fusion
    • Dimitrov, A. S., S. S. Rawat, S. Jiang, and R. Blumenthal. 2003. Role of the fusion peptide and membrane-proximal domain in HIV-1 envelope glycoprotein-mediated membrane fusion. Biochemistry 42:14150-14158.
    • (2003) Biochemistry , vol.42 , pp. 14150-14158
    • Dimitrov, A.S.1    Rawat, S.S.2    Jiang, S.3    Blumenthal, R.4
  • 20
    • 0030985017 scopus 로고    scopus 로고
    • Evaluation of monoclonal antibodies to human immunodeficiency virus type 1 primary isolates by neutralization assays: Performance criteria for selecting candidate antibodies for clinical trials
    • AIDS Clinical Trials Group Antibody Selection Working Group
    • D'Souza, M. P., D. Livnat, J. A. Bradac, and S. H. Bridges. 1997. Evaluation of monoclonal antibodies to human immunodeficiency virus type 1 primary isolates by neutralization assays: performance criteria for selecting candidate antibodies for clinical trials. AIDS Clinical Trials Group Antibody Selection Working Group. J. Infect. Dis. 175:1056-1062.
    • (1997) J. Infect. Dis. , vol.175 , pp. 1056-1062
    • D'Souza, M.P.1    Livnat, D.2    Bradac, J.A.3    Bridges, S.H.4
  • 21
    • 0030997127 scopus 로고    scopus 로고
    • Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein
    • Earl, P. L., C. C. Broder, R. W. Doms, and B. Moss. 1997. Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein. J. Virol. 71:2674-2684.
    • (1997) J. Virol. , vol.71 , pp. 2674-2684
    • Earl, P.L.1    Broder, C.C.2    Doms, R.W.3    Moss, B.4
  • 22
    • 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., W. Raffelsberger, B. Ferko, A. Klima, M. Purtscher, H. Katinger, and F. Ruker. 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    Raffelsberger, W.2    Ferko, B.3    Klima, A.4    Purtscher, M.5    Katinger, H.6    Ruker, F.7
  • 23
    • 0036668251 scopus 로고    scopus 로고
    • Neutralizing antibodies against HIV - Back in the major leagues?
    • Ferrantelli, F., and R. M. Ruprecht. 2002. Neutralizing antibodies against HIV - back in the major leagues? Curr. Opin. Immunol. 14:495-502.
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 495-502
    • Ferrantelli, F.1    Ruprecht, R.M.2
  • 24
    • 0034759248 scopus 로고    scopus 로고
    • Antigenic properties of the human immunodeficiency virus envelope during cell-cell fusion
    • Finnegan, C. M., W. Berg, G. K. Lewis, and A. L. DeVico. 2001. Antigenic properties of the human immunodeficiency virus envelope during cell-cell fusion. J. Virol. 75:11096-11105.
    • (2001) J. Virol. , vol.75 , pp. 11096-11105
    • Finnegan, C.M.1    Berg, W.2    Lewis, G.K.3    DeVico, A.L.4
  • 25
    • 0036633932 scopus 로고    scopus 로고
    • Genetic evidence that interhelical packing interactions in the gp41 core are critical for transition of the human immunodeficiency virus type 1 envelope glycoprotein to the fusion-active state
    • Follis, K. E., S. J. Larson, M. Lu, and J. H. Nunberg. 2002. Genetic evidence that interhelical packing interactions in the gp41 core are critical for transition of the human immunodeficiency virus type 1 envelope glycoprotein to the fusion-active state. J. Virol. 76:7356-7362.
    • (2002) J. Virol. , vol.76 , pp. 7356-7362
    • Follis, K.E.1    Larson, S.J.2    Lu, M.3    Nunberg, J.H.4
  • 26
    • 0034749280 scopus 로고    scopus 로고
    • In vivo attenuation of simian immunodeficiency virus by disruption of a tyrosine-dependent sorting signal in the envelope glycoprotein cytoplasmic tail
    • Fultz, P. N., P. J. Vance, M. J. Endres, B. Tao, J. D. Dvorin, I. C. Davis, J. D. Lifson, D. C. Montefiori, M. Marsh, M. H. Malim, and J. A. Hoxie. 2001. In vivo attenuation of simian immunodeficiency virus by disruption of a tyrosine-dependent sorting signal in the envelope glycoprotein cytoplasmic tail. J. Virol. 75:278-291.
    • (2001) J. Virol. , vol.75 , pp. 278-291
    • Fultz, P.N.1    Vance, P.J.2    Endres, M.J.3    Tao, B.4    Dvorin, J.D.5    Davis, I.C.6    Lifson, J.D.7    Montefiori, D.C.8    Marsh, M.9    Malim, M.H.10    Hoxie, J.A.11
  • 27
    • 0034046091 scopus 로고    scopus 로고
    • Recognition by human monoclonal antibodies of free and complexed peptides representing the prefusogenic and fusogenic forms of human immunodeficiency virus type 1 gp41
    • Gorny, M. K., and S. Zolla-Pazner. 2000. Recognition by human monoclonal antibodies of free and complexed peptides representing the prefusogenic and fusogenic forms of human immunodeficiency virus type 1 gp41. J. Virol. 74:6186-6192.
    • (2000) J. Virol. , vol.74 , pp. 6186-6192
    • Gorny, M.K.1    Zolla-Pazner, S.2
  • 28
    • 0036121261 scopus 로고    scopus 로고
    • Solid-phase proteoliposomes containing human immunodeficiency virus envelope glycoproteins
    • Grundner, C., T. Mirzabekov, J. Sodroski, and R. Wyatt. 2002. Solid-phase proteoliposomes containing human immunodeficiency virus envelope glycoproteins. J. Virol. 76:3511-3521.
    • (2002) J. Virol. , vol.76 , pp. 3511-3521
    • Grundner, C.1    Mirzabekov, T.2    Sodroski, J.3    Wyatt, R.4
  • 29
    • 0037195784 scopus 로고    scopus 로고
    • Enhancement of alpha-helicity in the HIV-1 inhibitory peptide DP178 leads to an increased affinity for human monoclonal antibody 2F5 but does not elicit neutralizing responses in vitro. Implications for vaccine design
    • Joyce, J. G., W. M. Hurni, M. J. Bogusky, V. M. Garsky, X. Liang, M. P. Citron, R. C. Danzeisen, M. D. Miller, J. W. Shiver, and P. M. Keller. 2002. Enhancement of alpha-helicity in the HIV-1 inhibitory peptide DP178 leads to an increased affinity for human monoclonal antibody 2F5 but does not elicit neutralizing responses in vitro. Implications for vaccine design. J. Biol. Chem. 277:45811-45820.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45811-45820
    • Joyce, J.G.1    Hurni, W.M.2    Bogusky, M.J.3    Garsky, V.M.4    Liang, X.5    Citron, M.P.6    Danzeisen, R.C.7    Miller, M.D.8    Shiver, J.W.9    Keller, P.M.10
  • 34
    • 0033575483 scopus 로고    scopus 로고
    • Epitope insertion into variable loops of HIV-1 gp120 as a potential means to improve immunogenicity of viral envelope protein
    • Liang, X., S. Munshi, J. Shendure, G. Mark, 3rd, M. E. Davies, D. C. Freed, D. C. Montefiori, and J. W. Shiver. 1999. Epitope insertion into variable loops of HIV-1 gp120 as a potential means to improve immunogenicity of viral envelope protein. Vaccine 17:2862-2872.
    • (1999) Vaccine , vol.17 , pp. 2862-2872
    • Liang, X.1    Munshi, S.2    Shendure, J.3    Mark III, G.4    Davies, M.E.5    Freed, D.C.6    Montefiori, D.C.7    Shiver, J.W.8
  • 35
    • 0034881226 scopus 로고    scopus 로고
    • Chimeric plant virus particles as immunogens for inducing murine and human immune responses against human immunodeficiency virus type 1
    • Marusic, C., P. Rizza, L. Lattanzi, C. Mancini, M. Spada, F. Belardelli, E. Benvenuto, and I. Capone. 2001. Chimeric plant virus particles as immunogens for inducing murine and human immune responses against human immunodeficiency virus type 1. J. Virol. 75:8434-8439.
    • (2001) J. Virol. , vol.75 , pp. 8434-8439
    • Marusic, C.1    Rizza, P.2    Lattanzi, L.3    Mancini, C.4    Spada, M.5    Belardelli, F.6    Benvenuto, E.7    Capone, I.8
  • 36
    • 0037405488 scopus 로고    scopus 로고
    • Defining the protective antibody response for HIV-1
    • Mascola, J. R. 2003. Defining the protective antibody response for HIV-1. Curr. Mol. Med. 3:209-216.
    • (2003) Curr. Mol. Med. , vol.3 , pp. 209-216
    • Mascola, J.R.1
  • 37
    • 1842562419 scopus 로고    scopus 로고
    • N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies
    • McCaffrey, R. A., C. Saunders, M. Hensel, and L. Stamatatos. 2004. N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies. J. Virol. 78:3279-3295.
    • (2004) J. Virol. , vol.78 , pp. 3279-3295
    • McCaffrey, R.A.1    Saunders, C.2    Hensel, M.3    Stamatatos, L.4
  • 39
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan, G. B., R. M. Markosyan, H. Hemmati, M. K. Delmedico, D. M. Lambert, and F. S. Cohen. 2000. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J. Cell Biol. 151:413-423.
    • (2000) J. Cell Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 40
    • 1842505038 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1-neutralizing monoclonal antibody 2F5 is multispecific for sequences flanking the DKW core epitope
    • Menendez, A., K. C. Chow, O. C. Pan, and J. K. Scott. 2004. Human immunodeficiency virus type 1-neutralizing monoclonal antibody 2F5 is multispecific for sequences flanking the DKW core epitope. J. Mol. Biol. 338: 311-327.
    • (2004) J. Mol. Biol. , vol.338 , pp. 311-327
    • Menendez, A.1    Chow, K.C.2    Pan, O.C.3    Scott, J.K.4
  • 42
    • 0343365487 scopus 로고    scopus 로고
    • Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion
    • Munoz-Barroso, I., K. Salzwedel, E. Hunter, and R. Blumenthal. 1999. Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion. J. Virol. 73:6089-6092.
    • (1999) J. Virol. , vol.73 , pp. 6089-6092
    • Munoz-Barroso, I.1    Salzwedel, K.2    Hunter, E.3    Blumenthal, R.4
  • 43
    • 0028235930 scopus 로고
    • Cross-neutralizing activity against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS
    • Muster, T., R. Guinea, A. Trkola, M. Purtscher, A. Klima, F. Steindl, P. Palese, and H. Katinger. 1994. Cross-neutralizing activity 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    Guinea, R.2    Trkola, A.3    Purtscher, M.4    Klima, A.5    Steindl, F.6    Palese, P.7    Katinger, H.8
  • 45
    • 0025721018 scopus 로고
    • A broadly neutralizing monoclonal antibody that recognizes the V3 region of human immunodeficiency virus type 1 glycoprotein gp120
    • Ohno, T., M. Terada, Y. Yoneda, K. W. Shea, R. F. Chambers, D. M. Stroka, M. Nakamura, and D. W. Kufe. 1991. A broadly neutralizing monoclonal antibody that recognizes the V3 region of human immunodeficiency virus type 1 glycoprotein gp120. Proc. Natl. Acad. Sci. USA 88:10726-10729.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10726-10729
    • Ohno, T.1    Terada, M.2    Yoneda, Y.3    Shea, K.W.4    Chambers, R.F.5    Stroka, D.M.6    Nakamura, M.7    Kufe, D.W.8
  • 47
    • 11144245343 scopus 로고    scopus 로고
    • October 2000. World Intellectual Property Organization. Patent WO-00/61618
    • Pai, E. F., M. H. Klein, P. Chong, and A. Pedyczak. October 2000. World Intellectual Property Organization. Patent WO-00/61618.
    • Pai, E.F.1    Klein, M.H.2    Chong, P.3    Pedyczak, A.4
  • 48
    • 0038414622 scopus 로고    scopus 로고
    • Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design
    • Pantophlet, R., I. A. Wilson, and D. R. Burton. 2003. Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design. J. Virol. 77:5889-5901.
    • (2003) J. Virol. , vol.77 , pp. 5889-5901
    • Pantophlet, R.1    Wilson, I.A.2    Burton, D.R.3
  • 49
    • 0034755554 scopus 로고    scopus 로고
    • Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus type 1 for the neutralizing monoclonal antibody 2F5
    • Parker, C. E., L. J. Deterding, C. Hager-Braun, J. M. Binley, N. Schulke, H. Katinger, J. P. Moore, and K. B. Tomer. 2001. Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus type 1 for the neutralizing monoclonal antibody 2F5. J. Virol. 75:10906-10911.
    • (2001) J. Virol. , vol.75 , pp. 10906-10911
    • Parker, C.E.1    Deterding, L.J.2    Hager-Braun, C.3    Binley, J.M.4    Schulke, N.5    Katinger, H.6    Moore, J.P.7    Tomer, K.B.8
  • 50
    • 0036935266 scopus 로고    scopus 로고
    • The N-linked glycan g15 within the V3 loop of the HIV-1 external glycoprotein gp120 affects coreceptor usage, cellular tropism, and neutralization
    • Polzer, S., M. T. Dittmar, H. Schmitz, and M. Schreiber. 2002. The N-linked glycan g15 within the V3 loop of the HIV-1 external glycoprotein gp120 affects coreceptor usage, cellular tropism, and neutralization. Virology 304: 70-80.
    • (2002) Virology , vol.304 , pp. 70-80
    • Polzer, S.1    Dittmar, M.T.2    Schmitz, H.3    Schreiber, M.4
  • 52
    • 2442731886 scopus 로고    scopus 로고
    • Expression and characterization of HIV type 1 envelope protein associated with a broadly reactive neutralizing antibody response
    • Quinnan, G. V., Jr., P. F. Zhang, D. W. Fu, M. Dong, and H. J. Alter. 1999. Expression and characterization of HIV type 1 envelope protein associated with a broadly reactive neutralizing antibody response. AIDS Res. Hum. Retroviruses 15:561-570.
    • (1999) AIDS Res. Hum. Retroviruses , vol.15 , pp. 561-570
    • Quinnan Jr., G.V.1    Zhang, P.F.2    Fu, D.W.3    Dong, M.4    Alter, H.J.5
  • 54
    • 0037389643 scopus 로고    scopus 로고
    • Rapid evolution of the neutralizing antibody response to HIV type 1 infection
    • Richman, D. D., T. Wrin, S. J. Little, and C. J. Petropoulos. 2003. Rapid evolution of the neutralizing antibody response to HIV type 1 infection. Proc. Natl. Acad. Sci. USA 100:4144-4149.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4144-4149
    • Richman, D.D.1    Wrin, T.2    Little, S.J.3    Petropoulos, C.J.4
  • 55
    • 0028291731 scopus 로고
    • Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1
    • Roben, P., J. P. Moore, M. Thali, J. Sodroski, C. F. Barbas, 3rd, and D. R. Burton. 1994. Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1. J. Virol. 68:4821-4828.
    • (1994) J. Virol. , vol.68 , pp. 4821-4828
    • Roben, P.1    Moore, J.P.2    Thali, M.3    Sodroski, J.4    Barbas III, C.F.5    Burton, D.R.6
  • 56
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root, M. J., M. S. Kay, and P. S. Kim. 2001. Protein design of an HIV-1 entry inhibitor. Science 291:884-888.
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 58
    • 0032980413 scopus 로고    scopus 로고
    • A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity
    • Salzwedel, K., J. T. West, and E. Hunter. 1999. A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity. J. Virol. 73:2469-2480.
    • (1999) J. Virol. , vol.73 , pp. 2469-2480
    • Salzwedel, K.1    West, J.T.2    Hunter, E.3
  • 60
    • 0028801450 scopus 로고
    • Epitope exposure on functional, oligomeric HIV-1 gp41 molecules
    • Sattentau, Q. J., S. Zolla-Pazner, and P. Poignard. 1995. Epitope exposure on functional, oligomeric HIV-1 gp41 molecules. Virology 206:713-717.
    • (1995) Virology , vol.206 , pp. 713-717
    • Sattentau, Q.J.1    Zolla-Pazner, S.2    Poignard, P.3
  • 61
    • 0035859948 scopus 로고    scopus 로고
    • The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles
    • Schibli, D. J., R. C. Montelaro, and H. J. Vogel. 2001. The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles. Biochemistry 40: 9570-9578.
    • (2001) Biochemistry , vol.40 , pp. 9570-9578
    • Schibli, D.J.1    Montelaro, R.C.2    Vogel, H.J.3
  • 62
    • 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., R. Kunert, M. Purtscher, S. Wolbank, R. Voglauer, F. Steindl, and H. Katinger. 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    Kunert, R.2    Purtscher, M.3    Wolbank, S.4    Voglauer, R.5    Steindl, F.6    Katinger, H.7
  • 63
    • 0033869815 scopus 로고    scopus 로고
    • Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: Putative role during viral fusion
    • Suarez, T., W. R. Gallaher, A. Agirre, F. M. Goni, and J. L. Nieva. 2000. Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusion. J. Virol. 74:8038-8047.
    • (2000) J. Virol , vol.74 , pp. 8038-8047
    • Suarez, T.1    Gallaher, W.R.2    Agirre, A.3    Goni, F.M.4    Nieva, J.L.5
  • 64
    • 0031902829 scopus 로고    scopus 로고
    • CD4-Induced conformational changes in the human immunodeficiency virus type 1 gp120 glycoprotein: Consequences for virus entry and neutralization
    • Sullivan, N., Y. Sun, Q. Sattentau, M. Thali, D. Wu, G. Denisova, J. Gershoni, J. Robinson, J. Moore, and J. Sodroski. 1998. CD4-Induced conformational changes in the human immunodeficiency virus type 1 gp120 glycoprotein: consequences for virus entry and neutralization. J. Virol. 72: 4694-4703.
    • (1998) J. Virol. , vol.72 , pp. 4694-4703
    • Sullivan, N.1    Sun, Y.2    Sattentau, Q.3    Thali, M.4    Wu, D.5    Denisova, G.6    Gershoni, J.7    Robinson, J.8    Moore, J.9    Sodroski, J.10
  • 65
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan, K., J. Liu, J. Wang, S. Shen, and M. Lu. 1997. Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. USA 94: 12303-12308.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3    Shen, S.4    Lu, M.5
  • 66
    • 0027976321 scopus 로고
    • Resistance to neutralization by broadly reactive antibodies to the human immunodeficiency virus type 1 gp120 glycoprotein conferred by a gp41 amino acid change
    • Thali, M., M. Charles, C. Furman, L. Cavacini, M. Posner, J. Robinson, and J. Sodroski. 1994. Resistance to neutralization by broadly reactive antibodies to the human immunodeficiency virus type 1 gp120 glycoprotein conferred by a gp41 amino acid change. J. Virol. 68:674-680.
    • (1994) J. Virol. , vol.68 , pp. 674-680
    • Thali, M.1    Charles, M.2    Furman, C.3    Cavacini, L.4    Posner, M.5    Robinson, J.6    Sodroski, J.7
  • 67
    • 0036001491 scopus 로고    scopus 로고
    • Structure-affinity relationships in the gp41 ELDKWA epitope for the HIV-1 neutralizing monoclonal antibody 2F5: Effects of side-chain and backbone modifications and conformational constraints
    • Tian, Y., C. V. Ramesh, X. Ma, S. Naqvi, T. Patel, T. Cenizal, M. Tiscione, K. Diaz, T. Crea, E. Arnold, G. F. Arnold, and J. W. Taylor. 2002. Structure-affinity relationships in the gp41 ELDKWA epitope for the HIV-1 neutralizing monoclonal antibody 2F5: effects of side-chain and backbone modifications and conformational constraints. J. Peptide Res. 59:264-276.
    • (2002) J. Peptide Res. , vol.59 , pp. 264-276
    • Tian, Y.1    Ramesh, C.V.2    Ma, X.3    Naqvi, S.4    Patel, T.5    Cenizal, T.6    Tiscione, M.7    Diaz, K.8    Crea, T.9    Arnold, E.10    Arnold, G.F.11    Taylor, J.W.12
  • 70
    • 0029861654 scopus 로고    scopus 로고
    • Resistance of human immunodeficiency virus type 1 to neutralization by natural antisera occurs through single amino acid substitutions that cause changes in antibody binding at multiple sites
    • Watkins, B. A., S. Buge, K. Aldrich, A. E. Davis, J. Robinson, M. S. Reitz, Jr., and M. Robert-Guroff. 1996. Resistance of human immunodeficiency virus type 1 to neutralization by natural antisera occurs through single amino acid substitutions that cause changes in antibody binding at multiple sites. J. Virol. 70:8431-8437.
    • (1996) J. Virol. , vol.70 , pp. 8431-8437
    • Watkins, B.A.1    Buge, S.2    Aldrich, K.3    Davis, A.E.4    Robinson, J.5    Reitz Jr., M.S.6    Robert-Guroff, M.7
  • 73
    • 0036122454 scopus 로고    scopus 로고
    • Mutation of the dominant endocytosis motif in human immunodeficiency virus type 1 gp41 can complement matrix mutations without increasing Env incorporation
    • West, J. T., S. K. Weldon, S. Wyss, X. Lin, Q. Yu, M. Thali, and E. Hunter. 2002. Mutation of the dominant endocytosis motif in human immunodeficiency virus type 1 gp41 can complement matrix mutations without increasing Env incorporation. J. Virol. 76:3338-3349.
    • (2002) J. Virol. , vol.76 , pp. 3338-3349
    • West, J.T.1    Weldon, S.K.2    Wyss, S.3    Lin, X.4    Yu, Q.5    Thali, M.6    Hunter, E.7
  • 74
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild, C. T., D. C. Shugars, T. K. Greenwell, C. B. McDanal, and T. J. Matthews. 1994. Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. USA 91:9770-9774.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 75
    • 0026055421 scopus 로고
    • Epitope mapping of two immunodominant domains of gp41, the transmembrane protein of human immunodeficiency virus type 1, using ten human monoclonal antibodies
    • Xu, J. Y., M. K. Gorny, T. Palker, S. Karwowska, and S. Zolla-Pazner. 1991. Epitope mapping of two immunodominant domains of gp41, the transmembrane protein of human immunodeficiency virus type 1, using ten human monoclonal antibodies. J. Virol. 65:4832-4838.
    • (1991) J. Virol. , vol.65 , pp. 4832-4838
    • Xu, J.Y.1    Gorny, M.K.2    Palker, T.3    Karwowska, S.4    Zolla-Pazner, S.5
  • 76
    • 0029564921 scopus 로고
    • CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range
    • Yang, W. P., K. Green, S. Pinz-Sweeney, A. T. Briones, D. R. Burton, and C. F. Barbas 3rd. 1995. CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range. J. Mol. Biol. 254:392-403.
    • (1995) J. Mol. Biol. , vol.254 , pp. 392-403
    • Yang, W.P.1    Green, K.2    Pinz-Sweeney, S.3    Briones, A.T.4    Burton, D.R.5    Barbas III, C.F.6
  • 77
    • 3242660762 scopus 로고    scopus 로고
    • Induction of mucosal and systemic neutralizing antibodies against human immunodeficiency virus type 1 (HIV-1) by oral immunization with bovine Papillomavirus-HIV-1 gp41 chimeric virus-like particles
    • Zhang, H., Y. Huang, R. Fayad, G. T. Spear, and L. Qiao. 2004. Induction of mucosal and systemic neutralizing antibodies against human immunodeficiency virus type 1 (HIV-1) by oral immunization with bovine Papillomavirus-HIV-1 gp41 chimeric virus-like particles. J. Virol. 78:8342-8348.
    • (2004) J. Virol. , vol.78 , pp. 8342-8348
    • Zhang, H.1    Huang, Y.2    Fayad, R.3    Spear, G.T.4    Qiao, L.5
  • 78
    • 0038618737 scopus 로고    scopus 로고
    • A novel human antibody against human immunodeficiency virus type 1 gp120 is V1, V2, and V3 loop dependent and helps delimit the epitope of the broadly neutralizing antibody immunoglobulin G1 b12
    • Zwick, M. B., R. Kelleher, R. Jensen, A. F. Labrijn, M. Wang, G. V. Quinnan, Jr., P. W. Parren, and D. R. Burton. 2003. A novel human antibody against human immunodeficiency virus type 1 gp120 is V1, V2, and V3 loop dependent and helps delimit the epitope of the broadly neutralizing antibody immunoglobulin G1 b12. J. Virol. 77:6965-6978.
    • (2003) J. Virol. , vol.77 , pp. 6965-6978
    • Zwick, M.B.1    Kelleher, R.2    Jensen, R.3    Labrijn, A.F.4    Wang, M.5    Quinnan Jr., G.V.6    Parren, P.W.7    Burton, D.R.8
  • 81
    • 0035202616 scopus 로고    scopus 로고
    • Neutralization synergy of human immunodeficiency virus type 1 primary isolates by cocktails of broadly neutralizing antibodies
    • Zwick, M. B., M. Wang, P. Poignard, G. Stiegler, H. Katinger, D. R. Burton, and P. W. Parren. 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    Wang, M.2    Poignard, P.3    Stiegler, G.4    Katinger, H.5    Burton, D.R.6    Parren, P.W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.