메뉴 건너뛰기




Volumn 109, Issue 3, 2012, Pages 875-880

Enhanced HIV-1 neutralization by antibody heteroligation

Author keywords

Bispecific antibodies; Heterotypic binding; HIV gp160

Indexed keywords

GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 160; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; NEUTRALIZING ANTIBODY;

EID: 84856371864     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1120059109     Document Type: Article
Times cited : (52)

References (80)
  • 1
    • 77952311370 scopus 로고    scopus 로고
    • The role of antibodies in HIV vaccines
    • Mascola JR, Montefiori DC (2010) The role of antibodies in HIV vaccines. Annu Rev Immunol 28:413-444.
    • (2010) Annu Rev Immunol , vol.28 , pp. 413-444
    • Mascola, J.R.1    Montefiori, D.C.2
  • 2
    • 1542615646 scopus 로고    scopus 로고
    • Identifying epitopes of HIV-1 that induce protective antibodies
    • Zolla-Pazner S (2004) Identifying epitopes of HIV-1 that induce protective antibodies. Nat Rev Immunol 4:199-210.
    • (2004) Nat Rev Immunol , vol.4 , pp. 199-210
    • Zolla-Pazner, S.1
  • 3
    • 33744904454 scopus 로고    scopus 로고
    • Neutralizing antibody responses against autologous and heterologous viruses in acute versus chronic human immunodeficiency virus (HIV) infection: Evidence for a constraint on the ability of HIV to completely evade neutralizing antibody responses
    • DOI 10.1128/JVI.00093-06
    • Deeks SG, et al. (2006) Neutralizing antibody responses against autologous and heterologous viruses in acute versus chronic human immunodeficiency virus (HIV) infection: Evidence for a constraint on the ability of HIV to completely evade neutralizing antibody responses. J Virol 80:6155-6164. (Pubitemid 43849193)
    • (2006) Journal of Virology , vol.80 , Issue.12 , pp. 6155-6164
    • Deeks, S.G.1    Schweighardt, B.2    Wrin, T.3    Galovich, J.4    Hoh, R.5    Sinclair, E.6    Hunt, P.7    McCune, J.M.8    Martin, J.N.9    Petropoulos, C.J.10    Hecht, F.M.11
  • 4
    • 58149487645 scopus 로고    scopus 로고
    • Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection
    • Sather DN, et al. (2009) Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection. J Virol 83:757-769.
    • (2009) J Virol , vol.83 , pp. 757-769
    • Sather, D.N.1
  • 5
    • 58149399396 scopus 로고    scopus 로고
    • Frequency and phenotype of human immunodeficiency virus envelope-specific B cells from patients with broadly cross-neutralizing antibodies
    • Doria-Rose NA, et al. (2009) Frequency and phenotype of human immunodeficiency virus envelope-specific B cells from patients with broadly cross-neutralizing antibodies. J Virol 83:188-199.
    • (2009) J Virol , vol.83 , pp. 188-199
    • Doria-Rose, N.A.1
  • 6
    • 56449131391 scopus 로고    scopus 로고
    • Profiling the specificity of neutralizing antibodies in a large panel of plasmas from patients chronically infected with human immunodeficiency virus type 1 subtypes B and C
    • Binley JM, et al. (2008) Profiling the specificity of neutralizing antibodies in a large panel of plasmas from patients chronically infected with human immunodeficiency virus type 1 subtypes B and C. J Virol 82:11651-11668.
    • (2008) J Virol , vol.82 , pp. 11651-11668
    • Binley, J.M.1
  • 8
    • 67650453747 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 elite neutralizers: Individuals with broad and potent neutralizing activity identified by using a high-throughput neutralization assay together with an analytical selection algorithm
    • Simek MD, et al. (2009) Human immunodeficiency virus type 1 elite neutralizers: Individuals with broad and potent neutralizing activity identified by using a high-throughput neutralization assay together with an analytical selection algorithm. J Virol 83:7337-7348.
    • (2009) J Virol , vol.83 , pp. 7337-7348
    • Simek, M.D.1
  • 9
    • 69249208675 scopus 로고    scopus 로고
    • Antibody specificities associated with neutralization breadth in plasma from human immunodeficiency virus type 1 subtype C-infected blood donors
    • Gray ES, et al. (2009) Antibody specificities associated with neutralization breadth in plasma from human immunodeficiency virus type 1 subtype C-infected blood donors. J Virol 83:8925-8937.
    • (2009) J Virol , vol.83 , pp. 8925-8937
    • Gray, E.S.1
  • 10
    • 77649318846 scopus 로고    scopus 로고
    • Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals
    • Corti D, et al. (2010) Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals. PLoS ONE 5:e8805.
    • (2010) PLoS ONE , vol.5
    • Corti, D.1
  • 13
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Protocol G Principal Investigators
    • Walker LM, et al.; Protocol G Principal Investigators (2009) Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326:285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1
  • 14
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu X, et al. (2010) Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 329:856-861.
    • (2010) Science , vol.329 , pp. 856-861
    • Wu, X.1
  • 15
    • 80052938385 scopus 로고    scopus 로고
    • Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors
    • Bonsignori M, et al. (2011) Analysis of a clonal lineage of HIV-1 envelope V2/V3 conformational epitope-specific broadly neutralizing antibodies and their inferred unmutated common ancestors. J Virol 85:9998-10009.
    • (2011) J Virol , vol.85 , pp. 9998-10009
    • Bonsignori, M.1
  • 16
    • 80052925616 scopus 로고    scopus 로고
    • Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding
    • Scheid JF, et al. (2011) Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 333:1633-1637.
    • (2011) Science , vol.333 , pp. 1633-1637
    • Scheid, J.F.1
  • 17
    • 80052942203 scopus 로고    scopus 로고
    • Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    • NISC Comparative Sequencing Program
    • Wu X, et al.; NISC Comparative Sequencing Program (2011) Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 333: 1593-1602.
    • (2011) Science , vol.333 , pp. 1593-1602
    • Wu, X.1
  • 18
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Protocol G Principal Investigators
    • Walker LM, et al.; Protocol G Principal Investigators (2011) Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 477:466-470.
    • (2011) Nature , vol.477 , pp. 466-470
    • Walker, L.M.1
  • 25
    • 68349160853 scopus 로고    scopus 로고
    • Effective, low-titer antibody protection against low-dose repeated mucosal SHIV challenge in macaques
    • Hessell AJ, et al. (2009) Effective, low-titer antibody protection against low-dose repeated mucosal SHIV challenge in macaques. Nat Med 15:951-954.
    • (2009) Nat Med , vol.15 , pp. 951-954
    • Hessell, A.J.1
  • 26
    • 0034864776 scopus 로고    scopus 로고
    • Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro
    • DOI 10.1128/JVI.75.17.8340-8347.2001
    • Parren PW, et al. (2001) Antibody protects macaques against vaginal challenge with a pathogenic R5 simian/human immunodeficiency virus at serum levels giving complete neutralization in vitro. J Virol 75:8340-8347. (Pubitemid 32743706)
    • (2001) Journal of Virology , vol.75 , Issue.17 , pp. 8340-8347
    • Parren, P.W.H.I.1    Marx, P.A.2    Hessell, A.J.3    Luckay, A.4    Harouse, J.5    Cheng-Mayer, C.6    Moore, J.P.7    Burton, D.R.8
  • 28
    • 67249131966 scopus 로고    scopus 로고
    • Broadly neutralizing human anti-HIV antibody 2G12 is effective in protection against mucosal SHIV challenge even at low serum neutralizing titers
    • Hessell AJ, et al. (2009) Broadly neutralizing human anti-HIV antibody 2G12 is effective in protection against mucosal SHIV challenge even at low serum neutralizing titers. PLoS Pathog 5:e1000433.
    • (2009) PLoS Pathog , vol.5
    • Hessell, A.J.1
  • 29
    • 73949154006 scopus 로고    scopus 로고
    • Broadly neutralizing monoclonal antibodies 2F5 and 4E10 directed against the human immunodeficiency virus type 1 gp41 membrane-proximal external region protect against mucosal challenge by simian-human immunodeficiency virus SHIVBa-L
    • Hessell AJ, et al. (2010) Broadly neutralizing monoclonal antibodies 2F5 and 4E10 directed against the human immunodeficiency virus type 1 gp41 membrane-proximal external region protect against mucosal challenge by simian-human immunodeficiency virus SHIVBa-L. J Virol 84:1302-1313.
    • (2010) J Virol , vol.84 , pp. 1302-1313
    • Hessell, A.J.1
  • 31
    • 77957820631 scopus 로고    scopus 로고
    • Passive neutralizing antibody controls SHIV viremia and enhances B cell responses in infant macaques
    • Ng CT, et al. (2010) Passive neutralizing antibody controls SHIV viremia and enhances B cell responses in infant macaques. Nat Med 16:1117-1119.
    • (2010) Nat Med , vol.16 , pp. 1117-1119
    • Ng, C.T.1
  • 32
    • 34548474844 scopus 로고    scopus 로고
    • HIV/AIDS: Allied responses
    • Mascola JR (2007) HIV/AIDS: Allied responses. Nature 449:29-30.
    • (2007) Nature , vol.449 , pp. 29-30
    • Mascola, J.R.1
  • 33
    • 38349081511 scopus 로고    scopus 로고
    • The challenges of eliciting neutralizing antibodies to HIV-1 and to influenza virus
    • Karlsson Hedestam GB, et al. (2008) The challenges of eliciting neutralizing antibodies to HIV-1 and to influenza virus. Nat Rev Microbiol 6:143-155.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 143-155
    • Karlsson Hedestam, G.B.1
  • 34
    • 69549114407 scopus 로고    scopus 로고
    • Neutralizing antibodies against HIV-1: Can we elicit them with vaccines and how much do we need?
    • Montefiori DC, Mascola JR (2009) Neutralizing antibodies against HIV-1: Can we elicit them with vaccines and how much do we need? Curr Opin HIV AIDS 4:347-351
    • (2009) Curr Opin HIV AIDS , vol.4 , pp. 347-351
    • Montefiori, D.C.1    Mascola, J.R.2
  • 37
    • 0025267919 scopus 로고
    • Rapid development of isolate-specific neutralizing antibodies after primary HIV-1 infection and consequent emergence of virus variants which resist neutralization by autologous sera
    • Albert J, et al. (1990) Rapid development of isolate-specific neutralizing antibodies after primary HIV-1 infection and consequent emergence of virus variants which resist neutralization by autologous sera. AIDS 4:107-112. (Pubitemid 20108767)
    • (1990) AIDS , vol.4 , Issue.2 , pp. 107-112
    • Albert, J.1    Abrahamsson, B.2    Nagy, K.3    Aurelius, E.4    Gaines, H.5    Nystrom, G.6    Fenyo, E.M.7
  • 38
    • 0026544650 scopus 로고
    • Autologous HIV-1 neutralizing antibodies: Emergence of neutralization-resistant escape virus and subsequent development of escape virus neutralizing antibodies
    • Arendrup M, et al. (1992) Autologous HIV-1 neutralizing antibodies: Emergence of neutralization-resistant escape virus and subsequent development of escape virus neutralizing antibodies. J Acquir Immune Defic Syndr 5:303-307.
    • (1992) J Acquir Immune Defic Syndr , vol.5 , pp. 303-307
    • Arendrup, M.1
  • 39
    • 49149118421 scopus 로고    scopus 로고
    • Autologous neutralizing humoral immunity and evolution of the viral envelope in the course of subtype B human immunodeficiency virus type 1 infection
    • Bunnik EM, Pisas L, van Nuenen AC, Schuitemaker H (2008) Autologous neutralizing humoral immunity and evolution of the viral envelope in the course of subtype B human immunodeficiency virus type 1 infection. J Virol 82:7932-7941.
    • (2008) J Virol , vol.82 , pp. 7932-7941
    • Bunnik, E.M.1    Pisas, L.2    Van Nuenen, A.C.3    Schuitemaker, H.4
  • 40
    • 70349686331 scopus 로고    scopus 로고
    • Limited neutralizing antibody specificities drive neutralization escape in early HIV-1 subtype C infection
    • CAPRISA 002 Study; NIAID Center for HIV/AIDS Vaccine Immunology (CHAVI)
    • Moore PL, et al.; CAPRISA 002 Study; NIAID Center for HIV/AIDS Vaccine Immunology (CHAVI) (2009) Limited neutralizing antibody specificities drive neutralization escape in early HIV-1 subtype C infection. PLoS Pathog 5:e1000598.
    • (2009) PLoS Pathog , vol.5
    • Moore, P.L.1
  • 41
    • 70349695689 scopus 로고    scopus 로고
    • Escape from autologous neutralizing antibodies in acute/early subtype C HIV-1 infection requires multiple pathways
    • Rong R, et al. (2009) Escape from autologous neutralizing antibodies in acute/early subtype C HIV-1 infection requires multiple pathways. PLoS Pathog 5:e1000594.
    • (2009) PLoS Pathog , vol.5
    • Rong, R.1
  • 42
    • 77952001983 scopus 로고    scopus 로고
    • Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization
    • Binley JM, et al. (2010) Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization. J Virol 84:5637-5655.
    • (2010) J Virol , vol.84 , pp. 5637-5655
    • Binley, J.M.1
  • 45
  • 47
    • 33144486096 scopus 로고    scopus 로고
    • Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1
    • Moore PL, et al. (2006) Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1. J Virol 80:2515-25-28.
    • (2006) J Virol , vol.80 , pp. 251525-251528
    • Moore, P.L.1
  • 48
    • 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
    • DOI 10.1128/JVI.77.1.353-365.2003
    • Poignard P, et al. (2003) 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 77:353-365. (Pubitemid 36004975)
    • (2003) Journal of Virology , vol.77 , Issue.1 , pp. 353-365
    • Poignard, P.1    Moulard, M.2    Golez, E.3    Vivona, V.4    Franti, M.5    Venturini, S.6    Wang, M.7    Parren, P.W.H.I.8    Burton, D.R.9
  • 49
    • 33745203490 scopus 로고    scopus 로고
    • Distribution and three-dimensional structure of AIDS virus envelope spikes
    • Zhu P, et al. (2006) Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 441:847-852.
    • (2006) Nature , vol.441 , pp. 847-852
    • Zhu, P.1
  • 50
    • 77954042425 scopus 로고    scopus 로고
    • Few and far between: How HIV may be evading antibody avidity
    • Klein JS, Bjorkman PJ (2010) Few and far between: how HIV may be evading antibody avidity. PLoS Pathog 6:e1000908.
    • (2010) PLoS Pathog , vol.6
    • Klein, J.S.1    Bjorkman, P.J.2
  • 51
    • 66149132686 scopus 로고    scopus 로고
    • Examination of the contributions of size and avidity to the neutralization mechanisms of the anti-HIV antibodies b12 and 4E10
    • Klein JS, et al. (2009) Examination of the contributions of size and avidity to the neutralization mechanisms of the anti-HIV antibodies b12 and 4E10. Proc Natl Acad Sci USA 106:7385-7390.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7385-7390
    • Klein, J.S.1
  • 52
    • 0028348564 scopus 로고
    • In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity
    • Barbas CF, 3rd, et al. (1994) In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity. Proc Natl Acad Sci USA 91:3809-3813.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3809-3813
    • Barbas III, C.F.1
  • 53
    • 0029653339 scopus 로고
    • Early high-affinity neutralizing anti-viral IgG responses without further overall improvements of affinity
    • Roost HP, et al. (1995) Early high-affinity neutralizing anti-viral IgG responses without further overall improvements of affinity. Proc Natl Acad Sci USA 92:1257-1261.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1257-1261
    • Roost, H.P.1
  • 55
    • 0034785732 scopus 로고    scopus 로고
    • Hemagglutinin 1-specific immunoglobulin G and Fab molecules mediate postattachment neutralization of influenza a virus by inhibition of an early fusion event
    • DOI 10.1128/JVI.75.21.10208-10218.2001
    • Edwards MJ, Dimmock NJ (2001) Hemagglutinin 1-specific immunoglobulin G and Fab molecules mediate postattachment neutralization of influenza A virus by inhibition of an early fusion event. J Virol 75:10208-10218. (Pubitemid 32948051)
    • (2001) Journal of Virology , vol.75 , Issue.21 , pp. 10208-10218
    • Edwards, M.J.1    Dimmock, N.J.2
  • 56
    • 0020619874 scopus 로고
    • Neutralization of poliovirus by a monoclonal antibody: Kinetics and stoichiometry
    • Icenogle J, et al. (1983) Neutralization of poliovirus by a monoclonal antibody: Kinetics and stoichiometry. Virology 127:412-425. (Pubitemid 13026450)
    • (1983) Virology , vol.127 , Issue.2 , pp. 412-425
    • Icenogle, J.1    Shiwen, H.2    Duke, G.3
  • 57
    • 0030732117 scopus 로고    scopus 로고
    • Variations in the neutralizing and haemagglutination-inhibiting activities of five influenza A virus-specific IgGs and their antibody fragments
    • Schofield DJ, Stephenson JR, Dimmock NJ (1997) Variations in the neutralizing and haemagglutination-inhibiting activities of five influenza A virus-specific IgGs and their antibody fragments. J Gen Virol 78:2431-2439. (Pubitemid 27469983)
    • (1997) Journal of General Virology , vol.78 , Issue.10 , pp. 2431-2439
    • Schofield, D.J.1    Stephenson, J.R.2    Dimmock, N.J.3
  • 59
    • 80052531336 scopus 로고    scopus 로고
    • Memory B cell antibodies to HIV-1 gp140 cloned from individuals infected with clade A and B viruses
    • Mouquet H, et al. (2011) Memory B cell antibodies to HIV-1 gp140 cloned from individuals infected with clade A and B viruses. PLoS ONE 6:e24078.
    • (2011) PLoS ONE , vol.6
    • Mouquet, H.1
  • 60
    • 63849131879 scopus 로고    scopus 로고
    • Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals
    • Scheid JF, et al. (2009) Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals. Nature 458:636-640.
    • (2009) Nature , vol.458 , pp. 636-640
    • Scheid, J.F.1
  • 62
    • 0029946383 scopus 로고    scopus 로고
    • 'Knobs-into-holes' engineering of antibody C(H)3 domains for heavy chain heterodimerization
    • Ridgway JB, Presta LG, Carter P (1996) 'Knobs-into-holes' engineering of antibody CH3 domains for heavy chain heterodimerization. Protein Eng 9:617-621. (Pubitemid 26241639)
    • (1996) Protein Engineering , vol.9 , Issue.7 , pp. 617-621
    • Ridgway, J.B.B.1    Presta, L.G.2    Carter, P.3
  • 63
    • 77951480441 scopus 로고    scopus 로고
    • Anti-gp41 antibodies cloned from HIV-infected patients with broadly neutralizing serologic activity
    • Pietzsch J, et al. (2010) Anti-gp41 antibodies cloned from HIV-infected patients with broadly neutralizing serologic activity. J Virol 84:5032-5042.
    • (2010) J Virol , vol.84 , pp. 5032-5042
    • Pietzsch, J.1
  • 65
    • 0026085170 scopus 로고
    • Characterization of a discontinuous human immunodeficiency virus type 1 gp120 epitope recognized by a broadly reactive neutralizing human monoclonal antibody
    • Thali M, et al. (1991) Characterization of a discontinuous human immunodeficiency virus type 1 gp120 epitope recognized by a broadly reactive neutralizing human monoclonal antibody. J Virol 65:6188-6193.
    • (1991) J Virol , vol.65 , pp. 6188-6193
    • Thali, M.1
  • 66
    • 0037379220 scopus 로고    scopus 로고
    • Characterization of human class-switched polymeric (immunoglobulin M [IgM] and IgA) anti-human immunodeficiency virus type 1 antibodies 2F5 and 2G12
    • DOI 10.1128/JVI.77.7.4095-4103.2003
    • Wolbank S, Kunert R, Stiegler G, Katinger H (2003) Characterization of human class-switched polymeric (immunoglobulin M [IgM] and IgA) anti-human immunodeficiency virus type 1 antibodies 2F5 and 2G12. J Virol 77:4095-4103. (Pubitemid 36350949)
    • (2003) Journal of Virology , vol.77 , Issue.7 , pp. 4095-4103
    • Wolbank, S.1    Kunert, R.2    Stiegler, G.3    Katinger, H.4
  • 67
    • 58149376504 scopus 로고    scopus 로고
    • Design and expression of a dimeric form of human immunodeficiency virus type 1 antibody 2G12 with increased neutralization potency
    • West AP, Jr., et al. (2009) Design and expression of a dimeric form of human immunodeficiency virus type 1 antibody 2G12 with increased neutralization potency. J Virol 83:98-104.
    • (2009) J Virol , vol.83 , pp. 98-104
    • West Jr., A.P.1
  • 68
    • 72849116535 scopus 로고    scopus 로고
    • Evaluation of CD4-CD4i antibody architectures yields potent, broadly cross-reactive anti-human immunodeficiency virus reagents
    • West AP, Jr., et al. (2010) Evaluation of CD4-CD4i antibody architectures yields potent, broadly cross-reactive anti-human immunodeficiency virus reagents. J Virol 84:261-269.
    • (2010) J Virol , vol.84 , pp. 261-269
    • West Jr., A.P.1
  • 69
    • 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
    • DOI 10.1128/JVI.77.5.2859-2865.2003
    • Dey B, Del Castillo CS, Berger EA (2003) 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 77:2859-2865. (Pubitemid 36228069)
    • (2003) Journal of Virology , vol.77 , Issue.5 , pp. 2859-2865
    • Dey, B.1    Del, C.C.S.2    Berger, E.A.3
  • 70
    • 77953786430 scopus 로고    scopus 로고
    • Neutralization efficiency is greatly enhanced by bivalent binding of an antibody to epitopes in the V4 region and the membrane-proximal external region within one trimer of human immunodeficiency virus type 1 glycoproteins
    • Wang P, Yang X (2010) Neutralization efficiency is greatly enhanced by bivalent binding of an antibody to epitopes in the V4 region and the membrane-proximal external region within one trimer of human immunodeficiency virus type 1 glycoproteins. J Virol 84:7114-7123.
    • (2010) J Virol , vol.84 , pp. 7114-7123
    • Wang, P.1    Yang, X.2
  • 71
    • 33947635198 scopus 로고    scopus 로고
    • The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes
    • Alam SM, et al. (2007) The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes. J Immunol 178:4424-4435. (Pubitemid 46492394)
    • (2007) Journal of Immunology , vol.178 , Issue.7 , pp. 4424-4435
    • Alam, S.M.1    McAdams, M.2    Boren, D.3    Rak, M.4    Scearce, R.M.5    Gao, F.6    Camacho, Z.T.7    Gewirth, D.8    Kelsoe, G.9    Chen, P.10    Haynes, B.F.11
  • 72
    • 73949133588 scopus 로고    scopus 로고
    • Role of HIV membrane in neutralization by two broadly neutralizing antibodies
    • Alam SM, et al. (2009) Role of HIV membrane in neutralization by two broadly neutralizing antibodies. Proc Natl Acad Sci USA 106:20234-20239.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20234-20239
    • Alam, S.M.1
  • 73
    • 85043488048 scopus 로고    scopus 로고
    • Interactions of HIV-1 antibodies 2F5 and 4E10 with a gp41 epitope prebound to host and viral membrane model systems
    • Veiga AS, Pattenden LK, Fletcher JM, Castanho MA, Aguilar MI (2009) Interactions of HIV-1 antibodies 2F5 and 4E10 with a gp41 epitope prebound to host and viral membrane model systems. ChemBioChem 10:1032-1044.
    • (2009) ChemBioChem , vol.10 , pp. 1032-1044
    • Veiga, A.S.1    Pattenden, L.K.2    Fletcher, J.M.3    Castanho, M.A.4    Aguilar, M.I.5
  • 74
    • 76549125090 scopus 로고    scopus 로고
    • Aromatic residues at the edge of the antibody combining site facilitate viral glycoprotein recognition through membrane interactions
    • Scherer EM, Leaman DP, Zwick MB, McMichael AJ, Burton DR (2010) Aromatic residues at the edge of the antibody combining site facilitate viral glycoprotein recognition through membrane interactions. Proc Natl Acad Sci USA 107:1529-1534.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 1529-1534
    • Scherer, E.M.1    Leaman, D.P.2    Zwick, M.B.3    McMichael, A.J.4    Burton, D.R.5
  • 75
    • 77950803157 scopus 로고    scopus 로고
    • Ablation of the complementarity-determining region H3 apex of the anti-HIV-1 broadly neutralizing antibody 2F5 abrogates neutralizing capacity without affecting core epitope binding
    • Julien JP, et al. (2010) Ablation of the complementarity-determining region H3 apex of the anti-HIV-1 broadly neutralizing antibody 2F5 abrogates neutralizing capacity without affecting core epitope binding. J Virol 84:4136-4147.
    • (2010) J Virol , vol.84 , pp. 4136-4147
    • Julien, J.P.1
  • 76
    • 77649132440 scopus 로고    scopus 로고
    • Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region
    • Ofek G, et al. (2010) Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region. J Virol 84:2955-2962.
    • (2010) J Virol , vol.84 , pp. 2955-2962
    • Ofek, G.1
  • 77
    • 77951939875 scopus 로고    scopus 로고
    • Structure of a clade C HIV-1 gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity
    • Diskin R, Marcovecchio PM, Bjorkman PJ (2010) Structure of a clade C HIV-1 gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity. Nat Struct Mol Biol 17:608-613.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 608-613
    • Diskin, R.1    Marcovecchio, P.M.2    Bjorkman, P.J.3
  • 78
    • 77957355961 scopus 로고    scopus 로고
    • Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation
    • Mouquet H, et al. (2010) Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation. Nature 467:591-595.
    • (2010) Nature , vol.467 , pp. 591-595
    • Mouquet, H.1
  • 79
    • 36849031722 scopus 로고    scopus 로고
    • Efficient generation of monoclonal antibodies from single human B cells by single cell RT-PCR and expression vector cloning
    • DOI 10.1016/j.jim.2007.09.017, PII S0022175907003122
    • Tiller T, et al. (2008) Efficient generation of monoclonal antibodies from single human B cells by single cell RT-PCR and expression vector cloning. J Immunol Methods 329:112-124. (Pubitemid 350235462)
    • (2008) Journal of Immunological Methods , vol.329 , Issue.1-2 , pp. 112-124
    • Tiller, T.1    Meffre, E.2    Yurasov, S.3    Tsuiji, M.4    Nussenzweig, M.C.5    Wardemann, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.