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Volumn 3, Issue 4 SUPPL., 2004, Pages

Neutralizing antibody responses to HIV: Role in protective immunity and challenges for vaccine design

Author keywords

CD4; HIV; Monomer; Neutralizing antibodies; Trimer

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS VACCINE; NEUTRALIZING ANTIBODY; VIRUS ANTIGEN; VIRUS ENVELOPE PROTEIN;

EID: 4344573018     PISSN: 14760584     EISSN: None     Source Type: Journal    
DOI: 10.1586/14760584.3.4.S33     Document Type: Review
Times cited : (43)

References (185)
  • 1
    • 19144365910 scopus 로고    scopus 로고
    • Immunization with envelope subunit vaccine products elicits neutralizing antibodies against laboratory-adapted but not primary isolates of human immunodeficiency virus Type 1
    • The National Institute of Allergy and Infectious Diseases AIDS Vaccine Evaluation Group
    • Mascola JR et al. Immunization with envelope subunit vaccine products elicits neutralizing antibodies against laboratory-adapted but not primary isolates of human immunodeficiency virus Type 1. The National Institute of Allergy and Infectious Diseases AIDS Vaccine Evaluation Group. J. Infect. Dis. 173(2), 340-348 (1996).
    • (1996) J. Infect. Dis. , vol.173 , Issue.2 , pp. 340-348
    • Mascola, J.R.1
  • 2
    • 0027879388 scopus 로고
    • Summary report: Workshop on the potential risks of antibody-dependent enhancement in human HIV vaccine trials
    • Mascola JR et al. Summary report: workshop on the potential risks of antibody-dependent enhancement in human HIV vaccine trials. AIDS Res. Hum. Retroviruses 9(12), 1175-1184 (1993).
    • (1993) AIDS Res. Hum. Retroviruses , vol.9 , Issue.12 , pp. 1175-1184
    • Mascola, J.R.1
  • 3
    • 0037137536 scopus 로고    scopus 로고
    • Viral evolution and challenges in the development of HIV vaccines
    • Barouch DH, Letvin NL. Viral evolution and challenges in the development of HIV vaccines. Vaccine 20(Suppl. 4), A66-A68 (2002).
    • (2002) Vaccine , vol.20 , Issue.SUPPL. 4
    • Barouch, D.H.1    Letvin, N.L.2
  • 4
    • 0037122796 scopus 로고    scopus 로고
    • Eventual AIDS vaccine failure in a rhesus monkey by viral escape from cytotoxic T-lymphocytes
    • Barouch DH et al. Eventual AIDS vaccine failure in a rhesus monkey by viral escape from cytotoxic T-lymphocytes. Nature 415(6869), 335-339 (2002).
    • (2002) Nature , vol.415 , Issue.6869 , pp. 335-339
    • Barouch, D.H.1
  • 5
    • 0037791747 scopus 로고    scopus 로고
    • Viral escape from dominant simian immunodeficiency virus epitope-specific cytotoxic T-lymphocytes in DNA-vaccinated rhesus monkeys
    • Barouch DH et al. Viral escape from dominant simian immunodeficiency virus epitope-specific cytotoxic T-lymphocytes in DNA-vaccinated rhesus monkeys. J. Virol. 77(13), 7367-7375 (2003).
    • (2003) J. Virol. , vol.77 , Issue.13 , pp. 7367-7375
    • Barouch, D.H.1
  • 6
    • 10744225749 scopus 로고    scopus 로고
    • Multispecific vaccine-induced mucosal cytotoxic T-lymphocytes reduce acute-phase viral replication but fail in long-term control of simian immunodeficiency virus SIVmac239
    • Vogel TU et al. Multispecific vaccine-induced mucosal cytotoxic T-lymphocytes reduce acute-phase viral replication but fail in long-term control of simian immunodeficiency virus SIVmac239. J. Virol. 77(24), 13348-13360 (2003).
    • (2003) J. Virol. , vol.77 , Issue.24 , pp. 13348-13360
    • Vogel, T.U.1
  • 7
    • 0141521639 scopus 로고    scopus 로고
    • Cellular immunity elicited by human immunodeficiency virus type 1/ simian immunodeficiency virus DNA vaccination does not augment the sterile protection afforded by passive infusion of neutralizing antibodies
    • Mascola JR et al. Cellular immunity elicited by human immunodeficiency virus type 1/ simian immunodeficiency virus DNA vaccination does not augment the sterile protection afforded by passive infusion of neutralizing antibodies. J. Virol. 77(19), 10348-10356 (2003).
    • (2003) J. Virol. , vol.77 , Issue.19 , pp. 10348-10356
    • Mascola, J.R.1
  • 8
    • 0029310641 scopus 로고
    • Perspective: Hypothesis: Serum IgG antibody is sufficient to confer protection against infectious diseases by inactivating the inoculum
    • Robbins JB, Schneerson R, Szu SC. Perspective: hypothesis: serum IgG antibody is sufficient to confer protection against infectious diseases by inactivating the inoculum. J. Infect. Dis. 171(6), 1387-1398 (1995).
    • (1995) J. Infect. Dis. , vol.171 , Issue.6 , pp. 1387-1398
    • Robbins, J.B.1    Schneerson, R.2    Szu, S.C.3
  • 9
    • 0035961542 scopus 로고    scopus 로고
    • Overview of the pathogenesis, prophylaxis and therapeusis of viral hepatitis B, with focus on reduction to practical applications
    • Hilleman MR. Overview of the pathogenesis, prophylaxis and therapeusis of viral hepatitis B, with focus on reduction to practical applications. Vaccine 19(15-16), 1837-1848 (2001).
    • (2001) Vaccine , vol.19 , Issue.15-16 , pp. 1837-1848
    • Hilleman, M.R.1
  • 10
    • 0033793926 scopus 로고    scopus 로고
    • Passive immunity in prevention and treatment of infectious diseases
    • Keller MA, Stiehm ER. Passive immunity in prevention and treatment of infectious diseases. Clin. Microbiol. Rev. 13(4), 602-614 (2000).
    • (2000) Clin. Microbiol. Rev. , vol.13 , Issue.4 , pp. 602-614
    • Keller, M.A.1    Stiehm, E.R.2
  • 12
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan DC, Kim PS. HIV entry and its inhibition. Cell 93(5), 681-684 (1998).
    • (1998) Cell , vol.93 , Issue.5 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 13
    • 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 MK, Zolla-Pazner S, 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(13), 6186-6192 (2000).
    • (2000) J. Virol. , vol.74 , Issue.13 , pp. 6186-6192
    • Gorny, M.K.1    Zolla-Pazner, S.2
  • 14
    • 0036278546 scopus 로고    scopus 로고
    • Dissection of human immunodeficiency virus Type 1 entry with neutralizing antibodies to gp41 fusion intermediates
    • Golding H et al. Dissection of human immunodeficiency virus Type 1 entry with neutralizing antibodies to gp41 fusion intermediates. J. Virol. 76(13), 6780-6790 (2002).
    • (2002) J. Virol. , vol.76 , Issue.13 , pp. 6780-6790
    • Golding, H.1
  • 15
    • 0038076112 scopus 로고    scopus 로고
    • Redox-triggered infection by disulfide-shadded human immunodeficiency virus Type 1 pseudovirions
    • Binley JM et al. Redox-triggered infection by disulfide-shadded human immunodeficiency virus Type 1 pseudovirions. J. Virol. 77(10), 5678-5684 (2003).
    • (2003) J. Virol. , vol.77 , Issue.10 , pp. 5678-5684
    • Binley, J.M.1
  • 16
    • 0025315127 scopus 로고
    • Inhibition of human immunodeficiency virus (HIV) infection in vitro by anticarbohydrate monoclonal antibodies: Peripheral glycosylation of HIV envelope glycoprotein gp120 may be a target for virus neutralization
    • Hansen JE et al. Inhibition of human immunodeficiency virus (HIV) infection in vitro by anticarbohydrate monoclonal antibodies: peripheral glycosylation of HIV envelope glycoprotein gp120 may be a target for virus neutralization. J. Virol. 64(6), 2833-2840 (1990).
    • (1990) J. Virol. , vol.64 , Issue.6 , pp. 2833-2840
    • Hansen, J.E.1
  • 17
    • 18244422922 scopus 로고    scopus 로고
    • The broadly neutralizing antihuman immunodeficiency virus Type 1 antibody 2G12 recognizes a cluster of alphal- > 2 mannose residues on the outer face of gp120
    • Scanlan CN et al. The broadly neutralizing antihuman immunodeficiency virus Type 1 antibody 2G12 recognizes a cluster of alphal- > 2 mannose residues on the outer face of gp120. J. Virol. 76(14), 7306-7321 (2002).
    • (2002) J. Virol. , vol.76 , Issue.14 , pp. 7306-7321
    • Scanlan, C.N.1
  • 18
    • 0030726970 scopus 로고    scopus 로고
    • Inhibition of virus attachment to CD4+ target cells is a major mechanism of T-cell line-adapted HIV-1 neutralization
    • Ugolini S et al. Inhibition of virus attachment to CD4+ target cells is a major mechanism of T-cell line-adapted HIV-1 neutralization. J. Exp. Med. 186(8), 1287-1298 (1997).
    • (1997) J. Exp. Med. , vol.186 , Issue.8 , pp. 1287-1298
    • Ugolini, S.1
  • 19
    • 2342455189 scopus 로고    scopus 로고
    • Immunogenicity of constrained monoclonal antibody A32-human immunodeficiency virus (HIV) Env gp120 complexes compared to that of recombinant HIV Type 1 gp120 envelope glycoproteins
    • Liao HX et al. Immunogenicity of constrained monoclonal antibody A32-human immunodeficiency virus (HIV) Env gp120 complexes compared to that of recombinant HIV Type 1 gp120 envelope glycoproteins. J. Virol. 78(10), 5270-5278 (2004).
    • (2004) J. Virol. , vol.78 , Issue.10 , pp. 5270-5278
    • Liao, H.X.1
  • 20
    • 0029987168 scopus 로고    scopus 로고
    • Antibody-dependent cellular cytotoxicity in HIV infections
    • Ahmad A, Menezes J. Antibody-dependent cellular cytotoxicity in HIV infections. FASEB J. 10(2), 258-266 (1996).
    • (1996) FASEB J. , vol.10 , Issue.2 , pp. 258-266
    • Ahmad, A.1    Menezes, J.2
  • 21
    • 0035037372 scopus 로고    scopus 로고
    • Evidence for a correlation between antibody-dependent cellular cytotoxicity-mediating antiHIV-1 antibodies and prognostic predictors of HIV infection
    • Ahmad R et al. Evidence for a correlation between antibody-dependent cellular cytotoxicity-mediating antiHIV-1 antibodies and prognostic predictors of HIV infection. J. Clin. Immunol. 21(3), 227-233 (2001).
    • (2001) J. Clin. Immunol. , vol.21 , Issue.3 , pp. 227-233
    • Ahmad, R.1
  • 22
    • 0036797095 scopus 로고    scopus 로고
    • Phage-displayed mimotopes recognizing a biologically active antiHIV-1 gp120 murine monoclonal antibody
    • Gomez-Roman VR et al. Phage-displayed mimotopes recognizing a biologically active antiHIV-1 gp120 murine monoclonal antibody. J. Acquir. Immune Defic. Syndr. 31(2), 147-153 (2002).
    • (2002) J. Acquir. Immune Defic. Syndr. , vol.31 , Issue.2 , pp. 147-153
    • Gomez-Roman, V.R.1
  • 23
    • 0028092161 scopus 로고
    • Antibodies to the HIV-1 V3 loop in serum from infected persons contribute a major proportion of immune effector functions including complement activation, antibody binding, and neutralization
    • Spear GT et al. Antibodies to the HIV-1 V3 loop in serum from infected persons contribute a major proportion of immune effector functions including complement activation, antibody binding, and neutralization. Virology 204(2), 609-615 (1994).
    • (1994) Virology , vol.204 , Issue.2 , pp. 609-615
    • Spear, G.T.1
  • 24
    • 0024998989 scopus 로고
    • Possible beneficial effects of neutralizing antibodies and antibody-dependent cell-mediated cytotoxicity in human immunodeficiency virus infection
    • Sawyer LA et al. Possible beneficial effects of neutralizing antibodies and antibody-dependent, cell-mediated cytotoxicity in human immunodeficiency virus infection. AIDS Res. Hum. Retroviruses 6(3), 341-356 (1990).
    • (1990) AIDS Res. Hum. Retroviruses , vol.6 , Issue.3 , pp. 341-356
    • Sawyer, L.A.1
  • 25
    • 0034958413 scopus 로고    scopus 로고
    • Antibody from patients with acute human immunodeficiency virus (HIV) infection inhibits primary strains of HIV Type 1 in the presence of natural-killer effector cells
    • Forthal DN, Landucci G, Daar ES. Antibody from patients with acute human immunodeficiency virus (HIV) infection inhibits primary strains of HIV Type 1 in the presence of natural-killer effector cells. J. Virol. 75(15), 6953-6961 (2001).
    • (2001) J. Virol. , vol.75 , Issue.15 , pp. 6953-6961
    • Forthal, D.N.1    Landucci, G.2    Daar, E.S.3
  • 26
    • 0025181668 scopus 로고
    • Antibodies mediating cellular cytotoxicity and neutralization correlate with a better clinical stage in children born to human immunodeficiency virus-infected mothers
    • Ljunggren K et al. Antibodies mediating cellular cytotoxicity and neutralization correlate with a better clinical stage in children born to human immunodeficiency virus-infected mothers. J. Infect. Dis. 161(2), 198-202 (1990).
    • (1990) J. Infect. Dis. , vol.161 , Issue.2 , pp. 198-202
    • Ljunggren, K.1
  • 28
    • 0028847578 scopus 로고
    • Virologic and immunologic characterization of long-term survivors of human immunodeficiency virus Type 1 infection
    • Cao Y et al. Virologic and immunologic characterization of long-term survivors of human immunodeficiency virus Type 1 infection. N. Engl. J. Med. 332(4), 201-208 (1995).
    • (1995) N. Engl. J. Med. , vol.332 , Issue.4 , pp. 201-208
    • Cao, Y.1
  • 29
    • 0023182368 scopus 로고
    • Human immunodeficiency virus neutralizing antibodies recognize several conserved domains on the envelope glycoproteins
    • Ho DD et al. Human immunodeficiency virus neutralizing antibodies recognize several conserved domains on the envelope glycoproteins. J. Virol. 61(6), 2024-2028 (1987).
    • (1987) J. Virol. , vol.61 , Issue.6 , pp. 2024-2028
    • Ho, D.D.1
  • 30
    • 0030901363 scopus 로고    scopus 로고
    • Autologous and heterologous neutralizing antibody responses following initial seroconversion in human immunodeficiency virus Type 1-infected individuals
    • Moog C et al. Autologous and heterologous neutralizing antibody responses following initial seroconversion in human immunodeficiency virus Type 1-infected individuals. J. Virol. 71(5), 3734-3741 (1997).
    • (1997) J. Virol. , vol.71 , Issue.5 , pp. 3734-3741
    • Moog, C.1
  • 31
    • 0030057730 scopus 로고    scopus 로고
    • Neutralizing and infection-enhancing antibody responses to human immunodeficiency virus Type 1 in long-term nonprogressors
    • Montefiori DC et al. Neutralizing and infection-enhancing antibody responses to human immunodeficiency virus Type 1 in long-term nonprogressors. J. Infect. Dis. 173(1), 60-67 (1996).
    • (1996) J. Infect. Dis. , vol.173 , Issue.1 , pp. 60-67
    • Montefiori, D.C.1
  • 32
    • 0028107685 scopus 로고
    • Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies
    • Moore JP et al. Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies. J. Virol. 68(1), 469-484 (1994).
    • (1994) J. Virol. , vol.68 , Issue.1 , pp. 469-484
    • Moore, J.P.1
  • 33
    • 0030764685 scopus 로고    scopus 로고
    • Neutralizing antibody responses to human immunodeficiency virus Type 1 in primary infection and long-term-nonprogressive infection
    • Pilgrim AK et al. Neutralizing antibody responses to human immunodeficiency virus Type 1 in primary infection and long-term-nonprogressive infection. J. Infect. Dis. 176(4), 924-932 (1997).
    • (1997) J. Infect. Dis. , vol.176 , Issue.4 , pp. 924-932
    • Pilgrim, A.K.1
  • 34
    • 0028181249 scopus 로고
    • Neutralizing antibody responses to autologous and heterologous isolares of human immunodeficiency virus
    • Wrin T et al. Neutralizing antibody responses to autologous and heterologous isolares of human immunodeficiency virus. J. Acquir. Immune Defic. Syndr. 7(3), 211-219 (1994).
    • (1994) J. Acquir. Immune Defic. Syndr. , vol.7 , Issue.3 , pp. 211-219
    • Wrin, T.1
  • 35
    • 0030764685 scopus 로고    scopus 로고
    • Neutralizing antibody responses to human immunodeficiency virus Type 1 in primary infection and long-term-nonprogressive infection
    • Pilgrim AK et al. Neutralizing antibody responses to human immunodeficiency virus Type 1 in primary infection and long-term-nonprogressive infection. J. Infect. Dis. 176(4), 924-932 (1997).
    • (1997) J. Infect. Dis. , vol.176 , Issue.4 , pp. 924-932
    • Pilgrim, A.K.1
  • 36
    • 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 BA et al. 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(12), 8431-8437 (1996).
    • (1996) J. Virol. , vol.70 , Issue.12 , pp. 8431-8437
    • Watkins, B.A.1
  • 37
    • 0037389643 scopus 로고    scopus 로고
    • Rapid evolution of the neutralizing antibody response to HIV Type 1 infection
    • Epub 2003 Mar 18
    • Richman DD et al. Rapid evolution of the neutralizing antibody response to HIV Type 1 infection. Proc. Natl Acad. Sci. USA 100(7), 4144-4149 Epub 2003 Mar 18 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , Issue.7 , pp. 4144-4149
    • Richman, D.D.1
  • 38
    • 0037456827 scopus 로고    scopus 로고
    • Antibody neutralization and escape by HIV-1
    • We X et al. Antibody neutralization and escape by HIV-1. Nature 422(6929), 307-312 (2003).
    • (2003) Nature , vol.422 , Issue.6929 , pp. 307-312
    • We, X.1
  • 39
    • 0027397052 scopus 로고
    • Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus Type 1 are highly prevalent in sera of infected humans
    • Moore JP, Ho DD. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus Type 1 are highly prevalent in sera of infected humans. J. Virol. 67(2), 863-875 (1993).
    • (1993) J. Virol. , vol.67 , Issue.2 , pp. 863-875
    • Moore, J.P.1    Ho, D.D.2
  • 40
    • 0029091404 scopus 로고
    • Lack of induction of antibodies specific for conserved, discontinuous epitopes of HIV-1 envelope glycoprotein by candidate AIDS vaccines
    • VanCott TC et al. Lack of induction of antibodies specific for conserved, discontinuous epitopes of HIV-1 envelope glycoprotein by candidate AIDS vaccines. J. Immunol. 155(8), 4100-4110 (1995).
    • (1995) J. Immunol. , vol.155 , Issue.8 , pp. 4100-4110
    • VanCott, T.C.1
  • 41
    • 0036181249 scopus 로고    scopus 로고
    • Viral persistance: HIVs strategies of immune system evasion
    • Johnson WE, Desrosiers RC. Viral persistance: HIVs strategies of immune system evasion. Ann. Rev. Med. 53, 499-518 (2002).
    • (2002) Ann. Rev. Med. , vol.53 , pp. 499-518
    • Johnson, W.E.1    Desrosiers, R.C.2
  • 42
    • 0031798442 scopus 로고    scopus 로고
    • Neutralizing antibodies from the sera of human immunodeficiency virus Type 1-infected individuals bind to monomeric gp120 and oligomeric gp140
    • Stamatos NM et al. Neutralizing antibodies from the sera of human immunodeficiency virus Type 1-infected individuals bind to monomeric gp120 and oligomeric gp140. J. Virol. 72(12), 9656-9667 (1998).
    • (1998) J. Virol. , vol.72 , Issue.12 , pp. 9656-9667
    • Stamatos, N.M.1
  • 43
    • 0026044947 scopus 로고
    • Neutralization of divergent HIV-1 isolates by conformation-dependent human antibodies to Gp120
    • Steimer KS et al. Neutralization of divergent HIV-1 isolates by conformation-dependent human antibodies to Gp120. Science 254, 105-108 (1991).
    • (1991) Science , vol.254 , pp. 105-108
    • Steimer, K.S.1
  • 44
    • 0026655937 scopus 로고
    • Recombinant human Fab fragments neutralize human Type 1 immunodeficiency virus in vitro
    • Barbas CF 3rd et al. Recombinant human Fab fragments neutralize human Type 1 immunodeficiency virus in vitro. Proc. Natl Acad. Sci. USA 89(19), 9339-9343 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , Issue.19 , pp. 9339-9343
    • Barbas III, C.F.1
  • 45
    • 0027256814 scopus 로고
    • Characterization of conserved human immunodeficiency virus Type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali M et al. Characterization of conserved human immunodeficiency virus Type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol. 67(7), 3978-3988 (1993).
    • (1993) J. Virol. , vol.67 , Issue.7 , pp. 3978-3988
    • Thali, M.1
  • 46
    • 9044241681 scopus 로고    scopus 로고
    • Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus Type 1
    • Trkola A et al. Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus Type 1. J. Virol. 70(2), 1100-1108 (1996).
    • (1996) J. Virol. , vol.70 , Issue.2 , pp. 1100-1108
    • Trkola, A.1
  • 47
    • 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. Identification and characterization of a neutralization site within the second variable region of human immunodeficiency virus Type 1 gp120. J. Virol. 66(2), 848-856 (1992).
    • (1992) J. Virol. , vol.66 , Issue.2 , pp. 848-856
    • Fung, M.S.1
  • 48
    • 0028027741 scopus 로고
    • Human antiV2 monoclonal antibody that neutralizes primary but not laboratory isolates of human immunodeficiency virus Type 1
    • Gorny MK et al. Human antiV2 monoclonal antibody that neutralizes primary but not laboratory isolates of human immunodeficiency virus Type 1. J. Virol. 68(12), 8312-8320 (1994).
    • (1994) J. Virol. , vol.68 , Issue.12 , pp. 8312-8320
    • Gorny, M.K.1
  • 49
    • 0005848581 scopus 로고
    • Principal neutralizing domain of the human immunodeficiency virus Type 1 envelope protein
    • Javaherian K et al. Principal neutralizing domain of the human immunodeficiency virus Type 1 envelope protein. Proc. Natl Acad. Sci. USA 86(17), 6768-6772 (1989).
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , Issue.17 , pp. 6768-6772
    • Javaherian, K.1
  • 50
    • 0022995585 scopus 로고
    • HTLV-III/LAV-neutralizing antibodies to an E coli-produced fragment of the virus envelope
    • Putney SD et al. HTLV-III/LAV-neutralizing antibodies to an E coli-produced fragment of the virus envelope. Science 234(4782), 1392-1395 (1986).
    • (1986) Science , vol.234 , Issue.4782 , pp. 1392-1395
    • Putney, S.D.1
  • 51
    • 0026356679 scopus 로고
    • Production of site-selected neutralizing human monoclonal antibodies against the third variable domain of the human immunodeficiency virus Type 1 envelope glycoprotein
    • Gorny MK et al. Production of site-selected neutralizing human monoclonal antibodies against the third variable domain of the human immunodeficiency virus Type 1 envelope glycoprotein. Proc Natl Acad. Sci. USA 88(8), 3238-3242 (1991).
    • (1991) Proc Natl Acad. Sci. USA , vol.88 , Issue.8 , pp. 3238-3242
    • Gorny, M.K.1
  • 52
    • 0024244253 scopus 로고
    • Immunodominant B-cell epitopes of the HIV-1 envelope recognized by infected and immunized hosts
    • Goudsmit J. Immunodominant B-cell epitopes of the HIV-1 envelope recognized by infected and immunized hosts. AIDS 2(Suppl. 1), S41-S45 (1988).
    • (1988) AIDS , vol.2 , Issue.SUPPL. 1
    • Goudsmit, J.1
  • 53
    • 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 JY et al. 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(9), 4832-4838 (1991).
    • (1991) J. Virol. , vol.65 , Issue.9 , pp. 4832-4838
    • Xu, J.Y.1
  • 54
    • 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 JM et al. 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(10), 911-924 (1996).
    • (1996) AIDS Res. Hum. Retroviruses , vol.12 , Issue.10 , pp. 911-924
    • Binley, J.M.1
  • 55
    • 0026693317 scopus 로고
    • Production of human monoclonal antibodies specific for conformational and linear non-V3 epitope of gp120
    • Karwowska S et al. Production of human monoclonal antibodies specific for conformational and linear non-V3 epitope of gp120. AIDS Res. Hum. Retroviruses 8(6) 1099-1106 (1992).
    • (1992) AIDS Res. Hum. Retroviruses , vol.8 , Issue.6 , pp. 1099-1106
    • Karwowska, S.1
  • 56
    • 0027454080 scopus 로고
    • A potent, neutralizing human monoclonal antibody against a unique epitope overlapping the CD4-binding site of HIV-1 gp120 that is broadly conserved across North American and African virus isolates
    • Pinter A et al. A potent, neutralizing human monoclonal antibody against a unique epitope overlapping the CD4-binding site of HIV-1 gp120 that is broadly conserved across North American and African virus isolates. AIDS Res. Hum. Retroviruses 9(10), 985-996 (1993).
    • (1993) AIDS Res. Hum. Retroviruses , vol.9 , Issue.10 , pp. 985-996
    • Pinter, A.1
  • 58
    • 0028865465 scopus 로고
    • Cross-clade neutralization of primary isolates of human immunodeficiency virus Type 1 by human monoclonal antibodies and tetrameric CD4-IgG
    • Trkola A et al. Cross-clade neutralization of primary isolates of human immunodeficiency virus Type 1 by human monoclonal antibodies and tetrameric CD4-IgG. J. Virol. 69(11), 6609-6617 (1995).
    • (1995) J. Virol. , vol.69 , Issue.11 , pp. 6609-6617
    • Trkola, A.1
  • 59
    • 0030935398 scopus 로고    scopus 로고
    • Recombinant human monoclonal antibody IgG1b12 neutralizes diverse human immunodeficiency virus Type 1 primary isolates
    • Kessler JA 2nd et al. Recombinant human monoclonal antibody IgG1b12 neutralizes diverse human immunodeficiency virus Type 1 primary isolates. AIDS Res. Hum. Retroviruses 13(7), 575-582 (1997).
    • (1997) AIDS Res. Hum. Retroviruses , vol.13 , Issue.7 , pp. 575-582
    • Kessler II, J.A.1
  • 60
    • 0030825573 scopus 로고    scopus 로고
    • Neutralization of HIV-1 primary isolates by polyclonal and monoclonal human antibodies
    • Hioe CE et al. Neutralization of HIV-1 primary isolates by polyclonal and monoclonal human antibodies. Int. Immunol. 9(9), 1281-1290 (1997).
    • (1997) Int. Immunol. , vol.9 , Issue.9 , pp. 1281-1290
    • Hioe, C.E.1
  • 61
    • 0029091806 scopus 로고
    • Neutralization of primary HIV-1 isolates by anti-envelope monoclonal antibodies
    • D'Souza MP et al. Neutralization of primary HIV-1 isolates by anti-envelope monoclonal antibodies. AIDS 9(8), 867-874 (1995).
    • (1995) AIDS , vol.9 , Issue.8 , pp. 867-874
    • D'Souza, M.P.1
  • 62
    • 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 et al. 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(8), 4821-4828 (1994).
    • (1994) J. Virol. , vol.68 , Issue.8 , pp. 4821-4828
    • Roben, P.1
  • 63
    • 0034631428 scopus 로고    scopus 로고
    • AntiCD4-binding domain antibodies complexed with HIV Type 1 glycoprotein 120 inhibit CD4+ T-cell-proliferative responses to glycoprotein 120
    • Hioe CE et al. AntiCD4-binding domain antibodies complexed with HIV Type 1 glycoprotein 120 inhibit CD4+ T-cell-proliferative responses to glycoprotein 120. AIDS Res. Hum. Retroviruses 16(9), 893-905 (2000).
    • (2000) AIDS Res. Hum. Retroviruses , vol.16 , Issue.9 , pp. 893-905
    • Hioe, C.E.1
  • 64
    • 0034764057 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus Type 1 gp120 presentation to CD4 T-cells by antibodies specific for the CD4 binding domain of gp120
    • Hioe CE et al. Inhibition of human immunodeficiency virus Type 1 gp120 presentation to CD4 T-cells by antibodies specific for the CD4 binding domain of gp120. J. Virol. 75(22), 10950-10957 (2001).
    • (2001) J. Virol. , vol.75 , Issue.22 , pp. 10950-10957
    • Hioe, C.E.1
  • 65
    • 3142741003 scopus 로고    scopus 로고
    • Human immunodeficiency virus Type 1 evades T-helper responses by exploiting antibodies that suppress antigen processing
    • Chien PC Jr et al. Human immunodeficiency virus Type 1 evades T-helper responses by exploiting antibodies that suppress antigen processing. J. Virol. 78(14), 7645-7652 (2004).
    • (2004) J. Virol. , vol.78 , Issue.14 , pp. 7645-7652
    • Chien Jr., P.C.1
  • 66
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry co-factor: Functional cDNA cloning of a seven-transmembrane, G-protein coupled receptor
    • Feng Y et al. HIV-1 entry co-factor: functional cDNA cloning of a seven-transmembrane, G-protein coupled receptor. Science 272(5263), 872-877 (1996).
    • (1996) Science , vol.272 , Issue.5263 , pp. 872-877
    • Feng, Y.1
  • 67
    • 0030878996 scopus 로고    scopus 로고
    • Determinants of HIV-1 coreceptor function on CC chemokine receptor 3. Importance of both extracellular and transmembrane/cytoplasmic regions
    • Alkhatib G et al. Determinants of HIV-1 coreceptor function on CC chemokine receptor 3. Importance of both extracellular and transmembrane/ cytoplasmic regions. J. Biol. Chem. 272(33), 20420-20426 (1997).
    • (1997) J. Biol. Chem. , vol.272 , Issue.33 , pp. 20420-20426
    • Alkhatib, G.1
  • 68
    • 15844419153 scopus 로고    scopus 로고
    • Identification of a major coreceptor for primary isolates of HIV-1
    • Deng H et al. Identification of a major coreceptor for primary isolates of HIV-1. Nature 381(6584), 661-666 (1996).
    • (1996) Nature , vol.381 , Issue.6584 , pp. 661-666
    • Deng, H.1
  • 69
    • 0036436313 scopus 로고    scopus 로고
    • Characterization of CD4-induced epitopes on the HIVType 1 gp120 envelope glycoprotein recognized by neutralizing human monoclonal antibodies
    • Xiang SH et al. Characterization of CD4-induced epitopes on the HIVType 1 gp120 envelope glycoprotein recognized by neutralizing human monoclonal antibodies. AIDS Res. Hum. Retroviruses 18(16), 1207-1217 (2002).
    • (2002) AIDS Res. Hum. Retroviruses , vol.18 , Issue.16 , pp. 1207-1217
    • Xiang, S.H.1
  • 70
    • 0037076265 scopus 로고    scopus 로고
    • Broadly cross-reactive HTV-1-neutralizing human monoclonal Fab selected for binding to gp120-CD4-CCR5 complexes
    • Moulard M et al. Broadly cross-reactive HTV-1-neutralizing human monoclonal Fab selected for binding to gp120-CD4-CCR5 complexes. Proc. Natl Acad. Sci. USA 99(10), 6913-6918 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.10 , pp. 6913-6918
    • Moulard, M.1
  • 71
    • 0037372301 scopus 로고    scopus 로고
    • Neutralization of human immunodeficiency virus Type 1 by sCD4-17b, a single-chain chimeric protein, based on sequential interaction of gp120 with CD4 and coreceptor
    • Dey B, Del Castillo CS, Berger EA. Neutralization of human immunodeficiency virus Type 1 by sCD4-17b, a single-chain chimeric protein, based on sequential interaction of gp120 with CD4 and coreceptor. J. Virol. 77(5), 2859-2865 (2003).
    • (2003) J. Virol. , vol.77 , Issue.5 , pp. 2859-2865
    • Dey, B.1    Del Castillo, C.S.2    Berger, E.A.3
  • 72
    • 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 et al. CD4-Induced conformational changes in the human immunodeficiency virus Type 1 gp120 glycoprotein: consequences for virus entry and neutralization. J. Virol. 72(6), 4694-4703 (1998).
    • (1998) J. Virol. , vol.72 , Issue.6 , pp. 4694-4703
    • Sullivan, N.1
  • 74
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the Type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard CX et al. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the Type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J. Biol. Chem. 265(18), 10373-10382 (1990).
    • (1990) J. Biol. Chem. , vol.265 , Issue.18 , pp. 10373-10382
    • Leonard, C.X.1
  • 75
    • 0025164009 scopus 로고
    • Priming of CD4+ T-cells specific for conserved regions of human immunodeficiency virus glycoprotein gp120 in humans immunized with a recombinant envelope protein
    • Abrignani S et al. Priming of CD4+ T-cells specific for conserved regions of human immunodeficiency virus glycoprotein gp120 in humans immunized with a recombinant envelope protein. Proc. Natl Acad. Sci. USA 87(16), 6136-6140 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , Issue.16 , pp. 6136-6140
    • Abrignani, S.1
  • 76
    • 0025042354 scopus 로고
    • Importance of hypervariable regions of HIV-1 gp120 in the generation of virus neutralizing antibodies
    • Haigwood NL et al. Importance of hypervariable regions of HIV-1 gp120 in the generation of virus neutralizing antibodies. AIDS Res. Hum. Retroviruses 6(7), 855-869 (1990).
    • (1990) AIDS Res. Hum. Retroviruses , vol.6 , Issue.7 , pp. 855-869
    • Haigwood, N.L.1
  • 77
    • 0032543555 scopus 로고    scopus 로고
    • The antigenic structure of the HIV gp120 envelope glycoprotein
    • Wyatt R et al. The antigenic structure of the HIV gp120 envelope glycoprotein. Nature 393(6686), 705-711 (1998).
    • (1998) Nature , vol.393 , Issue.6686 , pp. 705-711
    • Wyatt, R.1
  • 78
    • 0036637385 scopus 로고    scopus 로고
    • The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus Type 1 glycoprotein gp120
    • Sanders RW et al. The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus Type 1 glycoprotein gp120. J. Virol. 76(14), 7293-7305 (2002).
    • (2002) J. Virol. , vol.76 , Issue.14 , pp. 7293-7305
    • Sanders, R.W.1
  • 79
    • 0036170703 scopus 로고    scopus 로고
    • Regional clustering of shared neutralization determinants on primary isolates of clade C human immunodeficiency virus Type 1 from South Africa
    • Bures R et al. Regional clustering of shared neutralization determinants on primary isolates of clade C human immunodeficiency virus Type 1 from South Africa. J. Virol. 76(5), 2233-2244 (2002).
    • (2002) J. Virol. , vol.76 , Issue.5 , pp. 2233-2244
    • Bures, R.1
  • 80
    • 12444291017 scopus 로고    scopus 로고
    • Antibody domain exchange is an immunological solution to carbohydrate cluster recognition
    • Calarese DA et al. Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 300(5628), 2065-2071 (2003).
    • (2003) Science , vol.300 , Issue.5628 , pp. 2065-2071
    • Calarese, D.A.1
  • 81
    • 0036547263 scopus 로고    scopus 로고
    • New hope for an AIDS vaccine
    • Robinson HL. New hope for an AIDS vaccine. Nature Rev. Immunol. 2(4), 239-250 (2002).
    • (2002) Nature Rev. Immunol. , vol.2 , Issue.4 , pp. 239-250
    • Robinson, H.L.1
  • 82
    • 0030812563 scopus 로고    scopus 로고
    • Replication and neutralization of human immunodeficiency virus Type 1 lacking the V1 and V2 variable loops of the gp120 envelope glycoprotein
    • Cao J et al. Replication and neutralization of human immunodeficiency virus Type 1 lacking the V1 and V2 variable loops of the gp120 envelope glycoprotein. J. Virol. 71(12), 9808-9812 (1997).
    • (1997) J. Virol. , vol.71 , Issue.12 , pp. 9808-9812
    • Cao, J.1
  • 83
    • 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. 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(10), 7840-7845 (1998).
    • (1998) J. Virol. , vol.72 , Issue.10 , pp. 7840-7845
    • Stamatatos, L.1    Cheng-Mayer, C.2
  • 84
    • 0034003173 scopus 로고    scopus 로고
    • The human immunodeficiency virus Type 1 gp120 V2 domain mediates gp41-independent intersubunit contacts
    • Center RJ et al. The human immunodeficiency virus Type 1 gp120 V2 domain mediates gp41-independent intersubunit contacts. J. Virol. 74(10), 4448-4455 (2000).
    • (2000) J. Virol. , vol.74 , Issue.10 , pp. 4448-4455
    • Center, R.J.1
  • 85
    • 0032546952 scopus 로고    scopus 로고
    • A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding
    • Rizzuto CD et al. A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding. Science 280(5371), 1949-1953 (1998).
    • (1998) Science , vol.280 , Issue.5371 , pp. 1949-1953
    • Rizzuto, C.D.1
  • 86
    • 0029119783 scopus 로고
    • Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus Type 1 gp120 epitopes induced by receptor binding
    • Wyatt R et al. Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus Type 1 gp120 epitopes induced by receptor binding. J. Virol. 69(9), 5723-5733 (1995).
    • (1995) J. Virol. , vol.69 , Issue.9 , pp. 5723-5733
    • Wyatt, R.1
  • 87
    • 0027194743 scopus 로고
    • Functional and immunologic characterization of human immunodeficiency virus Type 1 envelope glycoproteins containing deletions of the major variable regions
    • Wyatt R et al. Functional and immunologic characterization of human immunodeficiency virus Type 1 envelope glycoproteins containing deletions of the major variable regions. J. Virol. 67(8), 4557-4565 (1993).
    • (1993) J. Virol. , vol.67 , Issue.8 , pp. 4557-4565
    • Wyatt, R.1
  • 88
    • 12144289425 scopus 로고    scopus 로고
    • Envelope-constrained neutralization-sensitive HIV-1 after heterosexual transmission
    • Derdeyn CA et al. Envelope-constrained neutralization-sensitive HIV-1 after heterosexual transmission. Science 303(5666), 2019-2022 (2004).
    • (2004) Science , vol.303 , Issue.5666 , pp. 2019-2022
    • Derdeyn, C.A.1
  • 89
    • 0037321708 scopus 로고    scopus 로고
    • Changes in the immunogenic properties of soluble gp140 human immunodeficiency virus envelope constructs upon partial deletion of the second hypervariable region
    • Srivastava IK et al. Changes in the immunogenic properties of soluble gp140 human immunodeficiency virus envelope constructs upon partial deletion of the second hypervariable region. J. Virol. 77(4), 2310-2320 (2003).
    • (2003) J. Virol. , vol.77 , Issue.4 , pp. 2310-2320
    • Srivastava, I.K.1
  • 90
    • 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. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393(6686), 648-659 (1998).
    • (1998) Nature , vol.393 , Issue.6686 , pp. 648-659
    • Kwong, P.D.1
  • 91
    • 0033919404 scopus 로고    scopus 로고
    • Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus
    • Kwong PD et al. Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus. J. Virol. 74(4), 1961-1972 (2000).
    • (2000) J. Virol. , vol.74 , Issue.4 , pp. 1961-1972
    • Kwong, P.D.1
  • 92
    • 1242351232 scopus 로고    scopus 로고
    • Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D
    • Stanfield RL et al. Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D. Structure (Camb.) 12(2), 193-204 (2004).
    • (2004) Structure (Camb.) , vol.12 , Issue.2 , pp. 193-204
    • Stanfield, R.L.1
  • 93
    • 0036333648 scopus 로고    scopus 로고
    • The crown and stem of the V3 loop play distinct roles in human immunodeficiency virus Type 1 envelope glycoprotein interactions with the CCR5 coreceptor
    • Cormier EG, Dragic T. The crown and stem of the V3 loop play distinct roles in human immunodeficiency virus Type 1 envelope glycoprotein interactions with the CCR5 coreceptor. J. Virol. 76(17), 8953-8957 (2002).
    • (2002) J. Virol. , vol.76 , Issue.17 , pp. 8953-8957
    • Cormier, E.G.1    Dragic, T.2
  • 94
    • 0037333420 scopus 로고    scopus 로고
    • Effect of amino acid substitution of the V3 and bridging sheet residues in human immunodeficiency virus Type 1 subtype C gp120 on CCR5 utilization
    • Suphaphiphat P et al. Effect of amino acid substitution of the V3 and bridging sheet residues in human immunodeficiency virus Type 1 subtype C gp120 on CCR5 utilization. J. Virol. 77(6), 3832-3837 (2003).
    • (2003) J. Virol. , vol.77 , Issue.6 , pp. 3832-3837
    • Suphaphiphat, P.1
  • 95
    • 0037317611 scopus 로고    scopus 로고
    • Alternative conformations of HIV-1 V3 loops mimic beta hairpins in chemokines, suggesting a mechanism for coreceptor selectivity
    • Sharon M et al. Alternative conformations of HIV-1 V3 loops mimic beta hairpins in chemokines, suggesting a mechanism for coreceptor selectivity. Structure (Camb.) 11(2), 225-236 (2003).
    • (2003) Structure (Camb.) , vol.11 , Issue.2 , pp. 225-236
    • Sharon, M.1
  • 96
    • 0035047159 scopus 로고    scopus 로고
    • Replacement of the V3 region of gp120 with SDF-1 preserves the infectivity of T-cell line-tropic human immunodeficiency virus Type 1
    • Yonezawa A et al. Replacement of the V3 region of gp120 with SDF-1 preserves the infectivity of T-cell line-tropic human immunodeficiency virus Type 1. J. Virol. 75(9), 4258-4267 (2001).
    • (2001) J. Virol. , vol.75 , Issue.9 , pp. 4258-4267
    • Yonezawa, A.1
  • 97
    • 0043080631 scopus 로고
    • Human immunodeficiency virus Type 1 neutralization epitope with conserved architecture elicits early type-specific antibodies in experimentally infected chimpanzees
    • Goudsmit J et al. Human immunodeficiency virus Type 1 neutralization epitope with conserved architecture elicits early type-specific antibodies in experimentally infected chimpanzees. Proc. Natl Acad. Sci. USA 85(12), 4478-4482 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , Issue.12 , pp. 4478-4482
    • Goudsmit, J.1
  • 98
    • 0031573212 scopus 로고    scopus 로고
    • Human monoclonal antibodies to the V3 loop of HIV-1 with intra- and interclade cross-reactivity
    • Gorny MK et al. Human monoclonal antibodies to the V3 loop of HIV-1 with intra- and interclade cross-reactivity. J. Immunol. 159(10), 5114-5122 (1997).
    • (1997) J. Immunol. , vol.159 , Issue.10 , pp. 5114-5122
    • Gorny, M.K.1
  • 99
    • 0027311936 scopus 로고
    • Repertoire of neutralizing human monoclonal antibodies specific for the V3 domain of HIV-1 gp120
    • Gorny MK et al. Repertoire of neutralizing human monoclonal antibodies specific for the V3 domain of HIV-1 gp120. J. Immunol. 150(2), 635-643 (1993).
    • (1993) J. Immunol. , vol.150 , Issue.2 , pp. 635-643
    • Gorny, M.K.1
  • 100
    • 0028116653 scopus 로고
    • Neutralization of primary human immunodeficiency virus Type 1 isolates by the broadly reactive antiV3 monoclonal antibody, 447-52D
    • Conley AJ et al. Neutralization of primary human immunodeficiency virus Type 1 isolates by the broadly reactive antiV3 monoclonal antibody, 447-52D. J. Virol. 68(11), 6994-7000 (1994).
    • (1994) J. Virol. , vol.68 , Issue.11 , pp. 6994-7000
    • Conley, A.J.1
  • 101
    • 0035701793 scopus 로고    scopus 로고
    • V3-specific polyclonal antibodies affinity purified from sera of infected humans effectively neutralize primary isolates of human immunodeficiency virus Type 1
    • Krachmarov CP et al. V3-specific polyclonal antibodies affinity purified from sera of infected humans effectively neutralize primary isolates of human immunodeficiency virus Type 1. AIDS Res. Hum. Petroviruses 17(18), 1737-1748 (2001).
    • (2001) AIDS Res. Hum. Petroviruses , vol.17 , Issue.18 , pp. 1737-1748
    • Krachmarov, C.P.1
  • 102
    • 0037213278 scopus 로고    scopus 로고
    • Heterogeneity of envelope molecules expressed on primary human immunodeficiency virus Type 1 particles as probed by the binding of neutralizing and nonneutralizing antibodies
    • Poignard P et al. Heterogeneity of envelope molecules expressed on primary human immunodeficiency virus Type 1 particles as probed by the binding of neutralizing and nonneutralizing antibodies. J. Virol. 77(1), 353-365 (2003).
    • (2003) J. Virol. , vol.77 , Issue.1 , pp. 353-365
    • Poignard, P.1
  • 103
    • 0036720793 scopus 로고    scopus 로고
    • Human monoclonal antibodies specific for conformation-sensitive epitopes of V3 neutralize human immunodeficiency virus Type 1 primary isolates from various clades
    • Gorny MK et al. Human monoclonal antibodies specific for conformation-sensitive epitopes of V3 neutralize human immunodeficiency virus Type 1 primary isolates from various clades. J. Virol. 76(18), 9035-9045 (2002).
    • (2002) J. Virol. , vol.76 , Issue.18 , pp. 9035-9045
    • Gorny, M.K.1
  • 104
    • 0025868277 scopus 로고
    • Molecular characterization of five human antihuman immunodeficiency virus Type 1 antibody heavy chains reveals extensive somatic mutation typical of an antigen-driven immune response
    • Andris JS et al. Molecular characterization of five human antihuman immunodeficiency virus Type 1 antibody heavy chains reveals extensive somatic mutation typical of an antigen-driven immune response. Proc. Natl Acad. Sci. USA 88(17), 7783-7787 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , Issue.17 , pp. 7783-7787
    • Andris, J.S.1
  • 105
    • 0042855800 scopus 로고    scopus 로고
    • Tyrosine sulfation of human antibodies contributes to recognition of the CCR5 binding region of HIV-1 gp120
    • Choe H et al. Tyrosine sulfation of human antibodies contributes to recognition of the CCR5 binding region of HIV-1 gp120. Cell 114(2), 161-170 (2003).
    • (2003) Cell , vol.114 , Issue.2 , pp. 161-170
    • Choe, H.1
  • 106
    • 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 CE et al. Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus Type 1 for the neutralizing monoclonal antibody 2F5. J. Virol. 75(22), 10906-10911 (2001).
    • (2001) J. Virol. , vol.75 , Issue.22 , pp. 10906-10911
    • Parker, C.E.1
  • 107
    • 0034984611 scopus 로고    scopus 로고
    • Identification and characterization of a peptide that specifically binds the human, broadly neutralizing antihuman immunodeficiency virus Type 1 antibody b12
    • Zwick MB et al. Identification and characterization of a peptide that specifically binds the human, broadly neutralizing antihuman immunodeficiency virus Type 1 antibody b12. J. Virol. 75(14), 6692-6699 (2001).
    • (2001) J. Virol. , vol.75 , Issue.14 , pp. 6692-6699
    • Zwick, M.B.1
  • 108
    • 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. Antigenicity and immunogenicity of the HIV-1 gp41 epitope ELDKWA inserted into permissive sites of the MalE protein. Vaccine 19(7-8), 684-693 (2000).
    • (2000) Vaccine , vol.19 , Issue.7-8 , pp. 684-693
    • Coeffier, E.1
  • 109
    • 0034759882 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus Type 1 glycoprotein gp41
    • Zwick MB et al. Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus Type 1 glycoprotein gp41. J. Virol. 75(22), 10892-10905 (2001).
    • (2001) J. Virol. , vol.75 , Issue.22 , pp. 10892-10905
    • Zwick, M.B.1
  • 110
    • 0028801450 scopus 로고
    • Epitope exposure on functional, oligomeric HIV-1 gp41 molecules
    • Sattentau QJ, Zolla-Pazner S, Poignard P. Epitope exposure on functional, oligomeric HIV-1 gp41 molecules. Virology 206(1), 713-717 (1995).
    • (1995) Virology , vol.206 , Issue.1 , pp. 713-717
    • Sattentau, Q.J.1    Zolla-Pazner, S.2    Poignard, P.3
  • 111
    • 0029039317 scopus 로고
    • Serotyping of primary human immunodeficiency virus Type 1 isolates from diverse geographic locations by flow cytometry
    • Zolla-Pazner S et al. Serotyping of primary human immunodeficiency virus Type 1 isolates from diverse geographic locations by flow cytometry. J. Virol. 69(6), 3807-3815 (1995).
    • (1995) J. Virol. , vol.69 , Issue.6 , pp. 3807-3815
    • Zolla-Pazner, S.1
  • 112
    • 0033942757 scopus 로고    scopus 로고
    • Conserved and exposed epitopes on intact, native, primary human immunodeficiency virus Type 1 virions of group M
    • Nyambi PN et al. Conserved and exposed epitopes on intact, native, primary human immunodeficiency virus Type 1 virions of group M J. Virol. 74(15), 7096-7107 (2000).
    • (2000) J. Virol. , vol.74 , Issue.15 , pp. 7096-7107
    • Nyambi, P.N.1
  • 113
    • 0030035109 scopus 로고    scopus 로고
    • A human monoclonal antibody to HIV-1 gp41 with neutralising activity against diverse laboratory isolates
    • Cotropia J et al. A human monoclonal antibody to HIV-1 gp41 with neutralising activity against diverse laboratory isolates. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 12(3), 221-232 (1996).
    • (1996) J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. , vol.12 , Issue.3 , pp. 221-232
    • Cotropia, J.1
  • 114
    • 9144242884 scopus 로고    scopus 로고
    • Potent cross-group neutralization of primary human immunodeficiency virus isolates with monoclonal antibodies-implications for acquired immunodeficiency syndrome vaccine
    • Ferrantelli F et al. Potent cross-group neutralization of primary human immunodeficiency virus isolates with monoclonal antibodies-implications for acquired immunodeficiency syndrome vaccine. J. Infect. Dis. 189(1), 71-74 (2004).
    • (2004) J. Infect. Dis. , vol.189 , Issue.1 , pp. 71-74
    • Ferrantelli, F.1
  • 115
    • 0026557112 scopus 로고
    • Prevention of HIV-1 infection in chimpanzees by gp120 V3 domain-specific monoclonal antibody
    • Emini EA et al. Prevention of HIV-1 infection in chimpanzees by gp120 V3 domain-specific monoclonal antibody. Nature 355(6362), 728-730 (1992).
    • (1992) Nature , vol.355 , Issue.6362 , pp. 728-730
    • Emini, E.A.1
  • 116
    • 9544239346 scopus 로고    scopus 로고
    • The consequence of passive administration of an antihuman immunodeficiency virus Type 1 neutralizing monoclonal antibody before challenge of chimpanzees with a primary virus isolate
    • Conley AJ et al. The consequence of passive administration of an antihuman immunodeficiency virus Type 1 neutralizing monoclonal antibody before challenge of chimpanzees with a primary virus isolate. J. Virol. 70(10), 6751-6758 (1996).
    • (1996) J. Virol. , vol.70 , Issue.10 , pp. 6751-6758
    • Conley, A.J.1
  • 117
    • 0023734130 scopus 로고
    • Transfer of a functional human immune system to mice with severe combined immunodeficiency
    • Mosier DE et al. Transfer of a functional human immune system to mice with severe combined immunodeficiency. Nature 335(6187), 256-259 (1988).
    • (1988) Nature , vol.335 , Issue.6187 , pp. 256-259
    • Mosier, D.E.1
  • 118
    • 0025907920 scopus 로고
    • Human immunodeficiency virus infection of human-PBL-SCID mice
    • Mosier DE et al. Human immunodeficiency virus infection of human-PBL-SCID mice. Science 251(4995), 791-794 (1991).
    • (1991) Science , vol.251 , Issue.4995 , pp. 791-794
    • Mosier, D.E.1
  • 119
    • 0027537122 scopus 로고
    • hu-PBL-SCID mice can be protected from HIV-1 infection bypassive transfer of monoclonal antibody to the principal neutralizing determinant of envelope gp120
    • Safrit JT et al. hu-PBL-SCID mice can be protected from HIV-1 infection bypassive transfer of monoclonal antibody to the principal neutralizing determinant of envelope gp120. AIDS 7(1), 15-21 (1993).
    • (1993) AIDS , vol.7 , Issue.1 , pp. 15-21
    • Safrit, J.T.1
  • 120
    • 0028950509 scopus 로고
    • Pre- and postexposure protection against human immunodeficiency virus Type 1 infection mediated by a monoclonal antibody
    • Gauduin MC et al. Pre- and postexposure protection against human immunodeficiency virus Type 1 infection mediated by a monoclonal antibody. J. Infect. Dis. 171(5), 1203-1209 (1995).
    • (1995) J. Infect. Dis. , vol.171 , Issue.5 , pp. 1203-1209
    • Gauduin, M.C.1
  • 121
    • 0029058337 scopus 로고
    • Protection against HIV-1 infection in hu-PBL-SCID mice bypassive immunization with a neutralizing human monoclonal antibody against the gp120 CD4-binding site
    • Parren PW et al. Protection against HIV-1 infection in hu-PBL-SCID mice bypassive immunization with a neutralizing human monoclonal antibody against the gp120 CD4-binding site. AIDS 9(6), F1-F6 (1995).
    • (1995) AIDS , vol.9 , Issue.6
    • Parren, P.W.1
  • 122
    • 0030805872 scopus 로고    scopus 로고
    • Erratum to 'Relevance of the antibody response against human immunodeficiency virus Type 1 envelope to vaccine design'
    • Parren PW et al. Erratum to 'Relevance of the antibody response against human immunodeficiency virus Type 1 envelope to vaccine design'. Immunol. Lett. 58(2), 125-132 (1997).
    • (1997) Immunol. Lett. , vol.58 , Issue.2 , pp. 125-132
    • Parren, P.W.1
  • 123
    • 0030805872 scopus 로고    scopus 로고
    • Erratum to 'Relevance of the antibody response against human immunodeficiency virus Type 1 envelope to vaccine design'
    • Parren PW et al. Erratum to 'Relevance of the antibody response against human immunodeficiency virus Type 1 envelope to vaccine design'. Immunol. Lett. 58(2), 125-132 (1997).
    • (1997) Immunol. Lett. , vol.58 , Issue.2 , pp. 125-132
    • Parren, P.W.1
  • 124
    • 0028971297 scopus 로고
    • Distinct rate and patterns of human CD4+ T-cell depletion in hu-PBL-SCID mice infected with different isolates of the human immunodeficiency virus
    • Mosier DE. Distinct rate and patterns of human CD4+ T-cell depletion in hu-PBL-SCID mice infected with different isolates of the human immunodeficiency virus. J. Clin. Immunol. 15(6 Suppl.), 1305-1335 (1995).
    • (1995) J. Clin. Immunol. , vol.15 , Issue.6 SUPPL. , pp. 1305-1335
    • Mosier, D.E.1
  • 125
    • 0032947286 scopus 로고    scopus 로고
    • Protection of Macaques against pathogenic simian/human immunodeficiency virus 89.6PD bypassive transfer of neutralizing antibodies
    • Mascola JR et al. Protection of Macaques against pathogenic simian/human immunodeficiency virus 89.6PD bypassive transfer of neutralizing antibodies. J. Virol. 73(5), 4009-4018 (1999).
    • (1999) J. Virol. , vol.73 , Issue.5 , pp. 4009-4018
    • Mascola, J.R.1
  • 126
    • 0033951746 scopus 로고    scopus 로고
    • Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus bypassive infusion of neutralizing antibodies
    • Mascola JR et al. Protection of macaques against vaginal transmission of a pathogenic HIV-1/SIV chimeric virus bypassive infusion of neutralizing antibodies. Nature Med. 6(2), 207-210 (2000).
    • (2000) Nature Med. , vol.6 , Issue.2 , pp. 207-210
    • Mascola, J.R.1
  • 127
    • 0345166103 scopus 로고    scopus 로고
    • Transfer of neutralizing IgG to macaques 6 h but not 24 h after SHIV infection confers sterilizing protection: Implications for HIV-1 vaccine development
    • Nishimura Y et al. Transfer of neutralizing IgG to macaques 6 h but not 24 h after SHIV infection confers sterilizing protection: implications for HIV-1 vaccine development. Proc. Natl Acad. Sci. USA 100(25), 15131-15136 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , Issue.25 , pp. 15131-15136
    • Nishimura, Y.1
  • 128
    • 0036307928 scopus 로고    scopus 로고
    • Postnatal pre-and postexposure passive immunization strategies: Protection of neonatal macaques against oral simian-human immunodeficiency virus challenge
    • Hofmann-Lehmann R et al. Postnatal pre-and postexposure passive immunization strategies: protection of neonatal macaques against oral simian-human immunodeficiency virus challenge. J. Med. Primatol. 31(3), 109-119 (2002).
    • (2002) J. Med. Primatol. , vol.31 , Issue.3 , pp. 109-119
    • Hofmann-Lehmann, R.1
  • 129
    • 9144262305 scopus 로고    scopus 로고
    • Immunoprophylaxis to prevent mother-to-child transmission of HIV-1
    • Safrit JT et al. Immunoprophylaxis to prevent mother-to-child transmission of HIV-1. J. Acquir. Immune Defic. Syndr. 35(2), 169-177 (2004).
    • (2004) J. Acquir. Immune Defic. Syndr. , vol.35 , Issue.2 , pp. 169-177
    • Safrit, J.T.1
  • 130
    • 17944380337 scopus 로고    scopus 로고
    • Protection of neonatal macaques against experimental SHIV infection by human neutralizing monoclonal antibodies
    • Ruprecht RM et al. Protection of neonatal macaques against experimental SHIV infection by human neutralizing monoclonal antibodies. Transfus. Clin. Biol. 8(4), 350-358 (2001).
    • (2001) Transfus. Clin. Biol. , vol.8 , Issue.4 , pp. 350-358
    • Ruprecht, R.M.1
  • 131
    • 0037436188 scopus 로고    scopus 로고
    • Post-exposure prophylaxis with human monoclonal antibodies prevented SHIV89.6P infection or disease in neonatal macaques
    • Ferrantelli F et al. Post-exposure prophylaxis with human monoclonal antibodies prevented SHIV89.6P infection or disease in neonatal macaques. AIDS 17(3), 301-309 (2003).
    • (2003) AIDS , vol.17 , Issue.3 , pp. 301-309
    • Ferrantelli, F.1
  • 132
    • 0037462713 scopus 로고    scopus 로고
    • Candidate HIV/AIDS vaccines: Lessons learned from the World's first Phase III efficacy trials
    • Francis DP et al. Candidate HIV/AIDS vaccines: lessons learned from the World's first Phase III efficacy trials. AIDS 17(2), 147-156 (2003).
    • (2003) AIDS , vol.17 , Issue.2 , pp. 147-156
    • Francis, D.P.1
  • 133
    • 0032080445 scopus 로고    scopus 로고
    • Interaction of polyclonal and monoclonal antiglycoprotein 120 antibodies with oligomeric glycoprotein 120-glycoprotein 41 complexes of a primary HIV Type 1 isolate relationship to neutralization
    • Fouts TR et al. Interaction of polyclonal and monoclonal antiglycoprotein 120 antibodies with oligomeric glycoprotein 120-glycoprotein 41 complexes of a primary HIV Type 1 isolate relationship to neutralization. AIDS Res. Hum. Retroviruses 14, 591-597 (1997).
    • (1997) AIDS Res. Hum. Retroviruses , vol.14 , pp. 591-597
    • Fouts, T.R.1
  • 134
    • 0028999803 scopus 로고
    • Human immunodeficiency virus Type 1 neutralization is determined by epitope exposure on the gp120 oligomer
    • Sattentau QJ, Moore JP. Human immunodeficiency virus Type 1 neutralization is determined by epitope exposure on the gp120 oligomer. J. Exp. Med. 182(1), 185-196 (1995).
    • (1995) J. Exp. Med. , vol.182 , Issue.1 , pp. 185-196
    • Sattentau, Q.J.1    Moore, J.P.2
  • 135
    • 0028028425 scopus 로고
    • Antigenic implications of human immunodeficiency virus Type 1 envelope quaternary structure: Oligomer-specific and -sensitive monoclonal antibodies
    • Broder CC et al. Antigenic implications of human immunodeficiency virus Type 1 envelope quaternary structure: oligomer-specific and -sensitive monoclonal antibodies. Proc. Natl Acad. Sci. USA 91(24), 11699-11703 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , Issue.24 , pp. 11699-11703
    • Broder, C.C.1
  • 136
    • 0028355456 scopus 로고
    • Native oligomeric human immunodeficiency virus Type 1 envelope glycoprotein elicits diverse monoclonal antibody reactivities
    • Earl PL et al. Native oligomeric human immunodeficiency virus Type 1 envelope glycoprotein elicits diverse monoclonal antibody reactivities. J. Virol. 68(5), 3015-3026 (1994).
    • (1994) J. Virol. , vol.68 , Issue.5 , pp. 3015-3026
    • Earl, P.L.1
  • 137
    • 0026068529 scopus 로고
    • Biological and immunological properties of human immunodeficiency virus Type 1 envelope glycoprotein: Analysis of proteins with truncations and deletions expressed by recombinant vaccinia viruses
    • Earl PL, Koenig S, Moss B. Biological and immunological properties of human immunodeficiency virus Type 1 envelope glycoprotein: analysis of proteins with truncations and deletions expressed by recombinant vaccinia viruses. J. Virol. 65(1), 31-41 (1991).
    • (1991) J. Virol. , vol.65 , Issue.1 , pp. 31-41
    • Earl, P.L.1    Koenig, S.2    Moss, B.3
  • 138
    • 0035168058 scopus 로고    scopus 로고
    • Immunogenicity and protective efficacy of oligomeric human immunodeficiency virus Type 1 gp140
    • Earl PL et al. Immunogenicity and protective efficacy of oligomeric human immunodeficiency virus Type 1 gp140. J. Virol. 75(2), 645-653 (2001).
    • (2001) J. Virol. , vol.75 , Issue.2 , pp. 645-653
    • Earl, P.L.1
  • 139
    • 0036184740 scopus 로고    scopus 로고
    • Purification and characterization of oligomeric envelope glycoprotein from a primary R5 subtype B human immunodeficiency virus
    • Srivastava IK et al. Purification and characterization of oligomeric envelope glycoprotein from a primary R5 subtype B human immunodeficiency virus. J. Virol. 76(6), 2835-2847 (2002).
    • (2002) J. Virol. , vol.76 , Issue.6 , pp. 2835-2847
    • Srivastava, I.K.1
  • 140
    • 0141788494 scopus 로고    scopus 로고
    • Purification, characterization, and immunogenicity of a soluble trimeric envelope protein containing a partial deletion of the V2 loop derived from SF162, an R5-tropic human immunodeficiency virus Type 1 isolate
    • Srivastava IK et al. Purification, characterization, and immunogenicity of a soluble trimeric envelope protein containing a partial deletion of the V2 loop derived from SF162, an R5-tropic human immunodeficiency virus Type 1 isolate. J. Virol. 77(20), 11244-11259 (2003).
    • (2003) J. Virol. , vol.77 , Issue.20 , pp. 11244-11259
    • Srivastava, I.K.1
  • 141
    • 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. 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(2), 627-643 (2000).
    • (2000) J. Virol. , vol.74 , Issue.2 , pp. 627-643
    • Binley, J.M.1
  • 142
    • 0031846234 scopus 로고    scopus 로고
    • Stabilization of human immunodeficiency virus Type 1 envelope glycoprotein trimers by disulfide bonds introduced into the gp41 glycoprotein ectodomain
    • Faizan M et al. Stabilization of human immunodeficiency virus Type 1 envelope glycoprotein trimers by disulfide bonds introduced into the gp41 glycoprotein ectodomain. J. Virol. 72(9), 7620-7625 (1998).
    • (1998) J. Virol. , vol.72 , Issue.9 , pp. 7620-7625
    • Faizan, M.1
  • 143
    • 0034063445 scopus 로고    scopus 로고
    • Variable-loop-deleted variants of the human immunodeficiency virus Type 1 envelope glycoprotein can be stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits
    • Sanders KW et al. Variable-loop-deleted variants of the human immunodeficiency virus Type 1 envelope glycoprotein can be stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits. J. Virol. 74(11), 5091-5100 (2000).
    • (2000) J. Virol. , vol.74 , Issue.11 , pp. 5091-5100
    • Sanders, K.W.1
  • 144
    • 0036315133 scopus 로고    scopus 로고
    • Oligomeric and conformational properties of a proteolytically mature, disulfide-stabilized human immunodeficiency virus Type 1 gp140 envelope glycoprotein
    • Schulke N et al. Oligomeric and conformational properties of a proteolytically mature, disulfide-stabilized human immunodeficiency virus Type 1 gp140 envelope glycoprotein. J. Virol. 76(15), 7760-7776 (2002).
    • (2002) J. Virol. , vol.76 , Issue.15 , pp. 7760-7776
    • Schulke, N.1
  • 145
    • 0036333661 scopus 로고    scopus 로고
    • Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus Type 1
    • Sanders RW et al. Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus Type 1. J. Virol. 76(17), 8875-8889 (2002).
    • (2002) J. Virol. , vol.76 , Issue.17 , pp. 8875-8889
    • Sanders, R.W.1
  • 146
    • 0034087050 scopus 로고    scopus 로고
    • Characterization of stable, soluble trimers containing complete ectodomains of human immunodeficiency virus Type 1 envelope glycoproteins
    • Yang X et al. Characterization of stable, soluble trimers containing complete ectodomains of human immunodeficiency virus Type 1 envelope glycoproteins. J. Virol. 74(12), 5716-5725 (2000).
    • (2000) J. Virol. , vol.74 , Issue.12 , pp. 5716-5725
    • Yang, X.1
  • 147
    • 0036231093 scopus 로고    scopus 로고
    • Highly stable trimers formed by human immunodeficiency virus Type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin
    • Yang X et al. Highly stable trimers formed by human immunodeficiency virus Type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin. J. Virol. 76(9), 4634-4642 (2002).
    • (2002) J. Virol. , vol.76 , Issue.9 , pp. 4634-4642
    • Yang, X.1
  • 148
    • 0025095635 scopus 로고
    • Oligomeric structure of the human immunodeficiency virus Type 1 envelope glycoprotein
    • Earl PL, Doms RW, Moss B. Oligomeric structure of the human immunodeficiency virus Type 1 envelope glycoprotein. Proc. Natl Acad. Sci. USA 87(2), 648-652 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , Issue.2 , pp. 648-652
    • Earl, P.L.1    Doms, R.W.2    Moss, B.3
  • 149
    • 0027183021 scopus 로고
    • Mutational analysis of the assembly domain of the HIV-1 envelope glycoprotein
    • Earl PL, Moss B. Mutational analysis of the assembly domain of the HIV-1 envelope glycoprotein. AIDS Ses. Hum. Retroviruses 9(7), 589-594 (1993).
    • (1993) AIDS Ses. Hum. Retroviruses , vol.9 , Issue.7 , pp. 589-594
    • Earl, P.L.1    Moss, B.2
  • 150
    • 0034712950 scopus 로고    scopus 로고
    • Passive infusion of immune serum into simian immunodeficiency virus-infected rhesus macaques undergoing a rapid disease course has minimal effect on plasma viremia
    • Binley JM et al. Passive infusion of immune serum into simian immunodeficiency virus-infected rhesus macaques undergoing a rapid disease course has minimal effect on plasma viremia. Virology 270(1), 237-249 (2000).
    • (2000) Virology , vol.270 , Issue.1 , pp. 237-249
    • Binley, J.M.1
  • 151
    • 0030975067 scopus 로고    scopus 로고
    • Antibodies with specificity to native gp120 and neutralization activity against primary human immunodeficiency virus Type 1 isolates elicited by immunization with oligomeric gp160
    • VanCott TC et al. Antibodies with specificity to native gp120 and neutralization activity against primary human immunodeficiency virus Type 1 isolates elicited by immunization with oligomeric gp160. J. Virol. 71, 4319-4330 (1997).
    • (1997) J. Virol. , vol.71 , pp. 4319-4330
    • VanCott, T.C.1
  • 152
    • 0035155850 scopus 로고    scopus 로고
    • Improved elicitation of neutralizing antibodies against primary human immunodeficiency viruses by soluble stabilized envelope glycoprotein trimers
    • Yang X, Wyatt R, Sodroski J. Improved elicitation of neutralizing antibodies against primary human immunodeficiency viruses by soluble stabilized envelope glycoprotein trimers. J. Virol. 75(3), 1165-1171 (2001).
    • (2001) J. Virol. , vol.75 , Issue.3 , pp. 1165-1171
    • Yang, X.1    Wyatt, R.2    Sodroski, J.3
  • 153
    • 0035000679 scopus 로고    scopus 로고
    • The ability of an oligomeric human immunodeficiency virus Type 1 (HIV-1) envelope antigen to elicit neutralizing antibodies against primary HIV-1 isolates is improved following partial deletion of the second hypervariable region
    • Barnett SW et al. The ability of an oligomeric human immunodeficiency virus Type 1 (HIV-1) envelope antigen to elicit neutralizing antibodies against primary HIV-1 isolates is improved following partial deletion of the second hypervariable region. J. Virol. 75(12), 5526-5540 (2001).
    • (2001) J. Virol. , vol.75 , Issue.12 , pp. 5526-5540
    • Barnett, S.W.1
  • 154
    • 0035148591 scopus 로고    scopus 로고
    • DNA vaccination with the human immunodeficiency virus Type 1 SF162DeltaV2 envelope elicits immune responses that offer partial protection from simian/human immunodeficiency virus infection to CD8(+) T-cell-depleted rhesus macaques
    • Cherpelis S et al. DNA vaccination with the human immunodeficiency virus Type 1 SF162DeltaV2 envelope elicits immune responses that offer partial protection from simian/human immunodeficiency virus infection to CD8(+) T-cell-depleted rhesus macaques. J. Virol. 75(3), 1547-1550 (2001).
    • (2001) J. Virol. , vol.75 , Issue.3 , pp. 1547-1550
    • Cherpelis, S.1
  • 155
    • 0035500872 scopus 로고    scopus 로고
    • DNA-immunization with a V2 deleted HIV-1 envelope elicits protective antibodies in macaques
    • Cherpelis S et al. DNA-immunization with a V2 deleted HIV-1 envelope elicits protective antibodies in macaques. Immunol. Lett. 79(1-2), 47-55 (2001).
    • (2001) Immunol. Lett. , vol.79 , Issue.1-2 , pp. 47-55
    • Cherpelis, S.1
  • 156
    • 10744224172 scopus 로고    scopus 로고
    • Priming B-cell-mediated antiHIV envelope responses by vaccination allows for the long-term control of infection in macaques exposed to a R5-tropic SHIV
    • Buckner C et al. Priming B-cell-mediated antiHIV envelope responses by vaccination allows for the long-term control of infection in macaques exposed to a R5-tropic SHIV Virology 320(1), 167-180 (2004).
    • (2004) Virology , vol.320 , Issue.1 , pp. 167-180
    • Buckner, C.1
  • 157
    • 0027247549 scopus 로고
    • Conformational perturbation of the envelope glycoprotein gp120 of human immunodeficiency virus type 1 by soluble CD4 and the lectin succinyl Con A
    • Pal R et al. Conformational perturbation of the envelope glycoprotein gp120 of human immunodeficiency virus type 1 by soluble CD4 and the lectin succinyl Con A. Virology 194(2), 833-837 (1993).
    • (1993) Virology , vol.194 , Issue.2 , pp. 833-837
    • Pal, R.1
  • 158
    • 0027324106 scopus 로고
    • HIV binding to its receptor creates specific epitopes for the CD4/gp120 complex
    • Gershoni JM et al. HIV binding to its receptor creates specific epitopes for the CD4/gp120 complex. FASEB J. 7(12), 1185-1187 (1993).
    • (1993) FASEB J. , vol.7 , Issue.12 , pp. 1185-1187
    • Gershoni, J.M.1
  • 159
    • 0029123163 scopus 로고
    • Monoclonal antibodies raised against covalentry crosslinked complexes of human immunodeficiency virus Type 1 gp120 and CD4 receptor identify a novel complex-dependent epitope on gp 120
    • DeVico AL et al. Monoclonal antibodies raised against covalentry crosslinked complexes of human immunodeficiency virus Type 1 gp120 and CD4 receptor identify a novel complex-dependent epitope on gp 120. Virology 211(2), 583-588 (1995).
    • (1995) Virology , vol.211 , Issue.2 , pp. 583-588
    • DeVico, A.L.1
  • 161
    • 0025016461 scopus 로고
    • Antibody raised against soluble CD4-rgp 20 complex recognizes the CD4 moiety and blocks membrane fusion without inhibiting CD4-gp120 binding
    • Celada F et al. Antibody raised against soluble CD4-rgp 20 complex recognizes the CD4 moiety and blocks membrane fusion without inhibiting CD4-gp120 binding. J. Exp. Med. 172, 1143-1150 (1990).
    • (1990) J. Exp. Med. , vol.172 , pp. 1143-1150
    • Celada, F.1
  • 162
    • 0026211179 scopus 로고
    • CD4: Its structure, role in immune function and AIDS pathogenesis, and potential as a pharmacological target
    • Sweet RW, Truneh A, Hendrickson WA. CD4: its structure, role in immune function and AIDS pathogenesis, and potential as a pharmacological target. Curr. Opin. Biotechnol. 2(4), 622-633 (1991).
    • (1991) Curr. Opin. Biotechnol. , vol.2 , Issue.4 , pp. 622-633
    • Sweet, R.W.1    Truneh, A.2    Hendrickson, W.A.3
  • 163
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T, Wells JA. A hot spot of binding energy in a hormone-receptor interface. Science 267(5196), 383-386 (1995).
    • (1995) Science , vol.267 , Issue.5196 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 164
    • 0030753982 scopus 로고    scopus 로고
    • Engineering novel proteins by transfer of active sites to natural scaffolds
    • Vita C. Engineering novel proteins by transfer of active sites to natural scaffolds. Curr. Opin. Biotechnol. 8(4), 429-434 (1997).
    • (1997) Curr. Opin. Biotechnol. , vol.8 , Issue.4 , pp. 429-434
    • Vita, C.1
  • 165
    • 0031904693 scopus 로고    scopus 로고
    • Novel miniproteins engineered by the transfer of active sites to small natural scaffolds
    • Vita C et al. Novel miniproteins engineered by the transfer of active sites to small natural scaffolds. Biopolymers 47(1), 93-100 (1998).
    • (1998) Biopolymers , vol.47 , Issue.1 , pp. 93-100
    • Vita, C.1
  • 166
    • 13044292627 scopus 로고    scopus 로고
    • Rational engineering of a miniprotein that reproduces the core of the CD4 site interacting with HIV-1 envelope glycoprotein
    • Vita C et al. Rational engineering of a miniprotein that reproduces the core of the CD4 site interacting with HIV-1 envelope glycoprotein. Proc. Natl Acad. Sci. USA 96(23), 13091-13096 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , Issue.23 , pp. 13091-13096
    • Vita, C.1
  • 167
    • 12244281787 scopus 로고    scopus 로고
    • Rational design of a CD4 mimic that inhibits HIV-1 entry and exposes cryptic neutralization epitopes
    • Martin L et al. Rational design of a CD4 mimic that inhibits HIV-1 entry and exposes cryptic neutralization epitopes. Nature Biotechnol. 21(1), 71-76 (2003).
    • (2003) Nature Biotechnol. , vol.21 , Issue.1 , pp. 71-76
    • Martin, L.1
  • 168
    • 0037015043 scopus 로고    scopus 로고
    • Crosslinked HIV-1 envelope-CD4 receptor complexes elicit broadly cross-reactive neutralizing antibodies in rhesus macaques
    • Fouts T et al. Crosslinked HIV-1 envelope-CD4 receptor complexes elicit broadly cross-reactive neutralizing antibodies in rhesus macaques. Proc. Natl Acad. Sci. USA 99(18), 11842-11847 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.18 , pp. 11842-11847
    • Fouts, T.1
  • 169
    • 0037213247 scopus 로고    scopus 로고
    • Fine mapping of the interaction of neutralizing and nonneutralizing monoclonal antibodies with the CD4 binding site of human immunodeficiency virus Type 1 gp120
    • Pantophlet R et al. Fine mapping of the interaction of neutralizing and nonneutralizing monoclonal antibodies with the CD4 binding site of human immunodeficiency virus Type 1 gp120. J. Virol. 77(1), 642-658 (2003).
    • (2003) J. Virol. , vol.77 , Issue.1 , pp. 642-658
    • Pantophlet, R.1
  • 170
    • 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, Wilson IA, Burton DR. Hyperglycosylated mutants of human immunodeficiency virus (HIV) Type 1 monomeric gp120 as novel antigens for HIV vaccine design. J. Virol. 77(10), 5889-5901 (2003).
    • (2003) J. Virol. , vol.77 , Issue.10 , pp. 5889-5901
    • Pantophlet, R.1    Wilson, I.A.2    Burton, D.R.3
  • 171
    • 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. 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).
    • (1998) J. Virol. , vol.72 , pp. 7840-7845
    • Stamatatos, L.1    Cheng-Mayer, C.2
  • 172
    • 0034235058 scopus 로고    scopus 로고
    • Generation and structural analysis of soluble oligpmeric gp140 envelope proteins derived from neutralization-resistant and neutralization-susceptible primary HIV Type 1 isolates
    • Stamatatos L, Iim M, Cheng-Mayer C. Generation and structural analysis of soluble oligpmeric gp140 envelope proteins derived from neutralization- resistant and neutralization-susceptible primary HIV Type 1 isolates [In Process Citation]. AIDS Res. Hum. Retroviruses 16(10), 981-994 (2000).
    • (2000) AIDS Res. Hum. Retroviruses , vol.16 , Issue.10 , pp. 981-994
    • Stamatatos, L.1    Iim, M.2    Cheng-Mayer, C.3
  • 173
    • 4344563562 scopus 로고    scopus 로고
    • Immunogenicity of monovalent and polyvalent DNA prime/protein boost formulations encoding primary HIV-1 Env ntigens as tested in rabbits and non-human primate models
    • Whistler, British Columbia, Canada. Abstract 245
    • Lu S, Wang S, Mascola J et al. Immunogenicity of monovalent and polyvalent DNA prime/protein boost formulations encoding primary HIV-1 Env ntigens as tested in rabbits and non-human primate models. Keystone Symposium on HIV Vaccine Development: Progress and Prospects. Whistler, British Columbia, Canada. Abstract 245 (2004).
    • (2004) Keystone Symposium on HIV Vaccine Development: Progress and Prospects
    • Lu, S.1    Wang, S.2    Mascola, J.3
  • 174
    • 4344632030 scopus 로고    scopus 로고
    • Neutralizing antibodies elicited by immunization of monkeys with DNA plasmids and recombinant adenoviral vectors expressing HIV-1 proteins
    • Whistler, British Columbia, Canada. Abstract 306
    • Sambor A, Louder M, Welcher B et al. Neutralizing antibodies elicited by immunization of monkeys with DNA plasmids and recombinant adenoviral vectors expressing HIV-1 proteins. Keystone Symposium on HIV Vaccine Development: Progress and Prospects. Whistler, British Columbia, Canada. Abstract 306 (2004).
    • (2004) Keystone Symposium on HIV Vaccine Development: Progress and Prospects
    • Sambor, A.1    Louder, M.2    Welcher, B.3
  • 175
  • 176
    • 4344708408 scopus 로고    scopus 로고
    • In vitro and in vivo biological characteristics of subtype C consensus and ancesteral envelope immunogens
    • San Francisco, USA. Abstract 278
    • Li Y, Weaver EA, Decker JM et al. In vitro and in vivo biological characteristics of subtype C consensus and ancesteral envelope immunogens. 11th Conference on Retrovirus and Opportunitic Infections. San Francisco, USA. Abstract 278 (2004).
    • (2004) 11th Conference on Retrovirus and Opportunitic Infections
    • Li, Y.1    Weaver, E.A.2    Decker, J.M.3
  • 177
    • 0037189323 scopus 로고    scopus 로고
    • Diversity considerations in HIV-1 vaccine selection
    • Gaschen B et al. Diversity considerations in HIV-1 vaccine selection. Science 296(5577), 2354-2360 (2002).
    • (2002) Science , vol.296 , Issue.5577 , pp. 2354-2360
    • Gaschen, B.1
  • 179
    • 0031657986 scopus 로고    scopus 로고
    • Studies of the neutralizing activity and avidity of antihuman immunodeficiency virus Type 1 Env antibody elicited by DNA priming and protein boosting
    • Richmond JF et al. Studies of the neutralizing activity and avidity of antihuman immunodeficiency virus Type 1 Env antibody elicited by DNA priming and protein boosting. J. Virol. 72(11), p9092-100 (1998).
    • (1998) J. Virol. , vol.72 , Issue.11 , pp. 9092-9100
    • Richmond, J.F.1
  • 180
    • 0002678757 scopus 로고
    • Sur la toxine et surranatoxine diphtheriques
    • Ramon G. Sur la toxine et surranatoxine diphtheriques. Ann. Inst. Pasteur 38, 1 (1924).
    • (1924) Ann. Inst. Pasteur , vol.38 , pp. 1
    • Ramon, G.1
  • 181
    • 0029200883 scopus 로고
    • A compendium of vaccine adjuvants and excipients
    • MF Powell, MJ Newman (Eds), Plenum Press, New York
    • Vogel FR, Powell MF. A compendium of vaccine adjuvants and excipients. In: Vaccine Design: The Subunit and Adjuvant Approach. MF Powell, MJ Newman (Eds), Plenum Press, New York 141-228 (1995).
    • (1995) Vaccine Design: The Subunit and Adjuvant Approach , pp. 141-228
    • Vogel, F.R.1    Powell, M.F.2
  • 182
    • 0037056053 scopus 로고    scopus 로고
    • Synergistic adjuvant activity of immunostimulatory DNA and oil/water emulsions for immunization with HIV p55 gag antigen
    • O'Hagan DT et al. Synergistic adjuvant activity of immunostimulatory DNA and oil/water emulsions for immunization with HIV p55 gag antigen. Vaccine 20(27-28), 3389-3398 (2002).
    • (2002) Vaccine , vol.20 , Issue.27-28 , pp. 3389-3398
    • O'Hagan, D.T.1
  • 183
    • 0037654710 scopus 로고    scopus 로고
    • Microparticles as vaccine adjuvants and delivery systems
    • O'Hagan D, Singh M. Microparticles as vaccine adjuvants and delivery systems. Expert Rev. Vaccines 2(2), 269-283 (2003).
    • (2003) Expert Rev. Vaccines , vol.2 , Issue.2 , pp. 269-283
    • O'Hagan, D.1    Singh, M.2
  • 184
    • 0034770990 scopus 로고    scopus 로고
    • Cationic microparticles are an effective delivery system for immune stimulatory cpG DNA
    • Singh M et al. Cationic microparticles are an effective delivery system for immune stimulatory cpG DNA. Pharm. Res. 18(10), 1476-1479 (2001).
    • (2001) Pharm. Res. , vol.18 , Issue.10 , pp. 1476-1479
    • Singh, M.1
  • 185
    • 0035838981 scopus 로고    scopus 로고
    • Regulation of T-cell immunity by dendritic cells
    • Lanzavecchia A, Sallusto F. Regulation of T-cell immunity by dendritic cells. Cell 106(3), 263-266 (2001).
    • (2001) Cell , vol.106 , Issue.3 , pp. 263-266
    • Lanzavecchia, A.1    Sallusto, F.2


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