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Volumn 250, Issue 1, 2012, Pages 180-198

Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA

Author keywords

Env; Hemagglutinin antibody; HIV 1; Influenza; Structure

Indexed keywords

EPITOPE; GLYCAN; GLYCOPROTEIN GP 120; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; INFLUENZA VACCINE; INFLUENZA VIRUS HEMAGGLUTININ; INFLUENZA VIRUS HEMAGGLUTININ ANTIBODY; MUTANT PROTEIN; NEUTRALIZING ANTIBODY; PROTEIN ANTIBODY; UNCLASSIFIED DRUG; VIRUS ANTIBODY; VIRUS ENVELOPE PROTEIN; VIRUS ENVELOPE PROTEIN ANTIBODY;

EID: 84867427047     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/imr.12005     Document Type: Article
Times cited : (81)

References (199)
  • 1
    • 0035857959 scopus 로고    scopus 로고
    • Probability of HIV-1 transmission per coital act in monogamous, heterosexual, HIV-1-discordant couples in Rakai, Uganda
    • Gray RH, et al. Probability of HIV-1 transmission per coital act in monogamous, heterosexual, HIV-1-discordant couples in Rakai, Uganda. Lancet 2001;357:1149-1153.
    • (2001) Lancet , vol.357 , pp. 1149-1153
    • Gray, R.H.1
  • 3
    • 0023099283 scopus 로고
    • Fine structure of human immunodeficiency virus (HIV) and immunolocalization of structural proteins
    • Gelderblom HR, Hausmann EH, Ozel M, Pauli G, Koch MA. Fine structure of human immunodeficiency virus (HIV) and immunolocalization of structural proteins. Virology 1987;156:171-176.
    • (1987) Virology , vol.156 , pp. 171-176
    • Gelderblom, H.R.1    Hausmann, E.H.2    Ozel, M.3    Pauli, G.4    Koch, M.A.5
  • 4
    • 0347364638 scopus 로고    scopus 로고
    • Electron tomography analysis of envelope glycoprotein trimers on HIV and simian immunodeficiency virus virions
    • Zhu P, et al. Electron tomography analysis of envelope glycoprotein trimers on HIV and simian immunodeficiency virus virions. Proc Natl Acad Sci USA 2003;100:15812-15817.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15812-15817
    • Zhu, P.1
  • 5
    • 33745203490 scopus 로고    scopus 로고
    • Distribution and three-dimensional structure of AIDS virus envelope spikes
    • Zhu P, et al. Distribution and three-dimensional structure of AIDS virus envelope spikes. Nature 2006;441:847-852.
    • (2006) Nature , vol.441 , pp. 847-852
    • Zhu, P.1
  • 6
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, Kim PS. Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997;89:263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 7
    • 57149107577 scopus 로고    scopus 로고
    • Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs
    • Zhu P, Winkler H, Chertova E, Taylor KA, Roux KH. Cryoelectron tomography of HIV-1 envelope spikes: further evidence for tripod-like legs. PLoS Pathog 2008;4:e1000203.
    • (2008) PLoS Pathog , vol.4
    • Zhu, P.1    Winkler, H.2    Chertova, E.3    Taylor, K.A.4    Roux, K.H.5
  • 9
    • 78651241895 scopus 로고    scopus 로고
    • Molecular architectures of trimeric SIV and HIV-1 envelope glycoproteins on intact viruses: strain-dependent variation in quaternary structure
    • White TA, et al. Molecular architectures of trimeric SIV and HIV-1 envelope glycoproteins on intact viruses: strain-dependent variation in quaternary structure. PLoS Pathog 2010;6:e1001249.
    • (2010) PLoS Pathog , vol.6
    • White, T.A.1
  • 10
    • 78650426126 scopus 로고    scopus 로고
    • Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure
    • Wu SR, et al. Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure. Proc Natl Acad Sci USA 2010;107:18844-18849.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 18844-18849
    • Wu, S.R.1
  • 11
    • 81255213876 scopus 로고    scopus 로고
    • Three-dimensional structures of soluble CD4-bound states of trimeric simian immunodeficiency virus envelope glycoproteins determined by using cryo-electron tomography
    • White TA, et al. Three-dimensional structures of soluble CD4-bound states of trimeric simian immunodeficiency virus envelope glycoproteins determined by using cryo-electron tomography. J Virol 2011;85:12114-12123.
    • (2011) J Virol , vol.85 , pp. 12114-12123
    • White, T.A.1
  • 12
    • 79960974710 scopus 로고    scopus 로고
    • Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architectures
    • Harris A, et al. Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architectures. Proc Natl Acad Sci USA 2011;108:11440-11445.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 11440-11445
    • Harris, A.1
  • 13
    • 79955048174 scopus 로고    scopus 로고
    • Quaternary structures of HIV Env immunogen exhibit conformational vicissitudes and interface diminution elicited by ligand binding
    • Moscoso CG, et al. Quaternary structures of HIV Env immunogen exhibit conformational vicissitudes and interface diminution elicited by ligand binding. Proc Natl Acad Sci USA 2011;108:6091-6096.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 6091-6096
    • Moscoso, C.G.1
  • 14
    • 79952368717 scopus 로고    scopus 로고
    • Structural comparison of HIV-1 envelope spikes with and without the V1/V2 loop
    • Hu G, Liu J, Taylor KA, Roux KH. Structural comparison of HIV-1 envelope spikes with and without the V1/V2 loop. J Virol 2011;85:2741-2750.
    • (2011) J Virol , vol.85 , pp. 2741-2750
    • Hu, G.1    Liu, J.2    Taylor, K.A.3    Roux, K.H.4
  • 15
    • 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, Wyatt R, Robinson J, Sweet RW, Sodroski J, Hendrickson WA. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 1998;393:648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 16
    • 84859561617 scopus 로고    scopus 로고
    • Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops
    • Kwon YD, et al. Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops. Proc Natl Acad Sci USA 2012;109:5663-5668.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 5663-5668
    • Kwon, Y.D.1
  • 17
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    • McLellan JS, et al. Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 2011;480:336-343.
    • (2011) Nature , vol.480 , pp. 336-343
    • McLellan, J.S.1
  • 18
    • 84864603281 scopus 로고    scopus 로고
    • Structural mechanism of trimeric HIV-1 envelope glycoprotein activation
    • Tran EE, et al. Structural mechanism of trimeric HIV-1 envelope glycoprotein activation. PLoS Pathog 2012;8:e1002797.
    • (2012) PLoS Pathog , vol.8
    • Tran, E.E.1
  • 19
    • 0037769964 scopus 로고    scopus 로고
    • The HIV Env-mediated fusion reaction
    • Gallo SA, et al. The HIV Env-mediated fusion reaction. Biochim Biophys Acta 2003;1614:36-50.
    • (2003) Biochim Biophys Acta , vol.1614 , pp. 36-50
    • Gallo, S.A.1
  • 20
    • 3042794175 scopus 로고    scopus 로고
    • Recent advances in understanding the molecular mechanisms of HIV-1 entry and fusion: revisiting current targets and considering new options for therapeutic intervention
    • Markovic I, Clouse KA. Recent advances in understanding the molecular mechanisms of HIV-1 entry and fusion: revisiting current targets and considering new options for therapeutic intervention. Curr HIV Res 2004;2:223-234.
    • (2004) Curr HIV Res , vol.2 , pp. 223-234
    • Markovic, I.1    Clouse, K.A.2
  • 22
    • 0031729823 scopus 로고    scopus 로고
    • Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry
    • Kilby JM, et al. Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry. Nat Med 1998;4:1302-1307.
    • (1998) Nat Med , vol.4 , pp. 1302-1307
    • Kilby, J.M.1
  • 23
    • 0034701058 scopus 로고    scopus 로고
    • Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides
    • Shu W, Liu J, Ji H, Radigen L, Jiang S, Lu M. Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides. Biochemistry 2000;39:1634-1642.
    • (2000) Biochemistry , vol.39 , pp. 1634-1642
    • Shu, W.1    Liu, J.2    Ji, H.3    Radigen, L.4    Jiang, S.5    Lu, M.6
  • 25
    • 0343365487 scopus 로고    scopus 로고
    • Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion
    • Munoz-Barroso I, Salzwedel K, Hunter E, Blumenthal R. Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion. J Virol 1999;73:6089-6092.
    • (1999) J Virol , vol.73 , pp. 6089-6092
    • Munoz-Barroso, I.1    Salzwedel, K.2    Hunter, E.3    Blumenthal, R.4
  • 26
    • 0033941573 scopus 로고    scopus 로고
    • Cooperation of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1
    • Kuhmann SE, Platt EJ, Kozak SL, Kabat D. Cooperation of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1. J Virol 2000;74:7005-7015.
    • (2000) J Virol , vol.74 , pp. 7005-7015
    • Kuhmann, S.E.1    Platt, E.J.2    Kozak, S.L.3    Kabat, D.4
  • 28
    • 25144500649 scopus 로고    scopus 로고
    • Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1
    • Yang X, Kurteva S, Ren X, Lee S, Sodroski J. Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1. J Virol 2005;79:12132-12147.
    • (2005) J Virol , vol.79 , pp. 12132-12147
    • Yang, X.1    Kurteva, S.2    Ren, X.3    Lee, S.4    Sodroski, J.5
  • 29
    • 36048944421 scopus 로고    scopus 로고
    • Modeling how many envelope glycoprotein trimers per virion participate in human immunodeficiency virus infectivity and its neutralization by antibody
    • Klasse PJ. Modeling how many envelope glycoprotein trimers per virion participate in human immunodeficiency virus infectivity and its neutralization by antibody. Virology 2007;369:245-262.
    • (2007) Virology , vol.369 , pp. 245-262
    • Klasse, P.J.1
  • 30
    • 59749083598 scopus 로고    scopus 로고
    • Estimating the stoichiometry of human immunodeficiency virus entry
    • Magnus C, Rusert P, Bonhoeffer S, Trkola A, Regoes RR. Estimating the stoichiometry of human immunodeficiency virus entry. J Virol 2009;83:1523-1531.
    • (2009) J Virol , vol.83 , pp. 1523-1531
    • Magnus, C.1    Rusert, P.2    Bonhoeffer, S.3    Trkola, A.4    Regoes, R.R.5
  • 31
    • 84859123277 scopus 로고    scopus 로고
    • Analysis of the subunit stoichiometries in viral entry
    • Magnus C, Regoes RR. Analysis of the subunit stoichiometries in viral entry. PLoS ONE 2012;7:e33441.
    • (2012) PLoS ONE , vol.7
    • Magnus, C.1    Regoes, R.R.2
  • 32
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson IA, Skehel JJ, Wiley DC. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 1981;289:366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 33
    • 34250901022 scopus 로고    scopus 로고
    • Influenza virus pleiomorphy characterized by cryoelectron tomography
    • Harris A, et al. Influenza virus pleiomorphy characterized by cryoelectron tomography. Proc Natl Acad Sci USA 2006;103:19123-19127.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 19123-19127
    • Harris, A.1
  • 34
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin
    • Skehel JJ, Wiley DC. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 2000;69:531-569.
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 35
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis W, Brown JH, Cusack S, Paulson JC, Skehel JJ, Wiley DC. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 1988;333:426-431.
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 36
    • 0024466223 scopus 로고
    • Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: a 500-MHz proton nuclear magnetic resonance study
    • Sauter NK, et al. Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: a 500-MHz proton nuclear magnetic resonance study. Biochemistry 1989;28:8388-8396.
    • (1989) Biochemistry , vol.28 , pp. 8388-8396
    • Sauter, N.K.1
  • 37
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 1994;371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 38
    • 0019860749 scopus 로고
    • Sequence relationships among the hemagglutinin genes of 12 subtypes of influenza A virus
    • Air GM. Sequence relationships among the hemagglutinin genes of 12 subtypes of influenza A virus. Proc Natl Acad Sci USA 1981;78:7639-7643.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 7639-7643
    • Air, G.M.1
  • 39
    • 0026175939 scopus 로고
    • Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses
    • Nobusawa E, Aoyama T, Kato H, Suzuki Y, Tateno Y, Nakajima K. Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses. Virology 1991;182:475-485.
    • (1991) Virology , vol.182 , pp. 475-485
    • Nobusawa, E.1    Aoyama, T.2    Kato, H.3    Suzuki, Y.4    Tateno, Y.5    Nakajima, K.6
  • 40
    • 47049092748 scopus 로고    scopus 로고
    • The contents of the syringe
    • Salzberg S. The contents of the syringe. Nature 2008;454:160-161.
    • (2008) Nature , vol.454 , pp. 160-161
    • Salzberg, S.1
  • 41
    • 42149130934 scopus 로고    scopus 로고
    • Interim within-season estimate of the effectiveness of trivalent inactivated influenza vaccine-Marshfield, Wisconsin, 2007-08 influenza season
    • Centers for Disease Control and Prevention (CDC).
    • Centers for Disease Control and Prevention (CDC). Interim within-season estimate of the effectiveness of trivalent inactivated influenza vaccine-Marshfield, Wisconsin, 2007-08 influenza season. MMWR Morb Mortal Wkly Rep 2008;57:393-398.
    • (2008) MMWR Morb Mortal Wkly Rep , vol.57 , pp. 393-398
  • 42
    • 0022477122 scopus 로고
    • Measurement of the mutation rates of animal viruses: influenza A virus and poliovirus type 1
    • Parvin JD, Moscona A, Pan WT, Leider JM, Palese P. Measurement of the mutation rates of animal viruses: influenza A virus and poliovirus type 1. J Virol 1986;59:377-383.
    • (1986) J Virol , vol.59 , pp. 377-383
    • Parvin, J.D.1    Moscona, A.2    Pan, W.T.3    Leider, J.M.4    Palese, P.5
  • 43
    • 0034625771 scopus 로고    scopus 로고
    • Timing the ancestor of the HIV-1 pandemic strains
    • Korber B, et al. Timing the ancestor of the HIV-1 pandemic strains. Science 2000;288:1789-1796.
    • (2000) Science , vol.288 , pp. 1789-1796
    • Korber, B.1
  • 44
    • 0037189323 scopus 로고    scopus 로고
    • Diversity considerations in HIV-1 vaccine selection
    • Gaschen B, et al. Diversity considerations in HIV-1 vaccine selection. Science 2002;296:2354-2360.
    • (2002) Science , vol.296 , pp. 2354-2360
    • Gaschen, B.1
  • 47
    • 0028244285 scopus 로고
    • An N-glycan within the human immunodeficiency virus type 1 gp120 V3 loop affects virus neutralization
    • Back NK, et al. An N-glycan within the human immunodeficiency virus type 1 gp120 V3 loop affects virus neutralization. Virology 1994;199:431-438.
    • (1994) Virology , vol.199 , pp. 431-438
    • Back, N.K.1
  • 48
    • 0035131175 scopus 로고    scopus 로고
    • Increased neutralization sensitivity of CD4-independent human immunodeficiency virus variants
    • Kolchinsky P, Kiprilov E, Sodroski J. Increased neutralization sensitivity of CD4-independent human immunodeficiency virus variants. J Virol 2001;75:2041-2050.
    • (2001) J Virol , vol.75 , pp. 2041-2050
    • Kolchinsky, P.1    Kiprilov, E.2    Sodroski, J.3
  • 49
    • 1842562419 scopus 로고    scopus 로고
    • N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies
    • McCaffrey RA, Saunders C, Hensel M, Stamatatos L. N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies. J Virol 2004;78:3279-3295.
    • (2004) J Virol , vol.78 , pp. 3279-3295
    • McCaffrey, R.A.1    Saunders, C.2    Hensel, M.3    Stamatatos, L.4
  • 50
    • 9944225582 scopus 로고    scopus 로고
    • Modified HIV envelope proteins with enhanced binding to neutralizing monoclonal antibodies
    • Kang SM, et al. Modified HIV envelope proteins with enhanced binding to neutralizing monoclonal antibodies. Virology 2005;331:20-32.
    • (2005) Virology , vol.331 , pp. 20-32
    • Kang, S.M.1
  • 51
    • 37849026069 scopus 로고    scopus 로고
    • Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses
    • Li Y, et al. Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses. J Virol 2008;82:638-651.
    • (2008) J Virol , vol.82 , pp. 638-651
    • Li, Y.1
  • 52
    • 70849114731 scopus 로고    scopus 로고
    • Glycans on influenza hemagglutinin affect receptor binding and immune response
    • Wang CC, et al. Glycans on influenza hemagglutinin affect receptor binding and immune response. Proc Natl Acad Sci USA 2009;106:18137-18142.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 18137-18142
    • Wang, C.C.1
  • 53
    • 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. Role of complex carbohydrates in human immunodeficiency virus type 1 infection and resistance to antibody neutralization. J Virol 2010;84:5637-5655.
    • (2010) J Virol , vol.84 , pp. 5637-5655
    • Binley, J.M.1
  • 54
    • 79952713119 scopus 로고    scopus 로고
    • Glycan shielding of the influenza virus hemagglutinin contributes to immunopathology in mice
    • Wanzeck K, Boyd KL, McCullers JA. Glycan shielding of the influenza virus hemagglutinin contributes to immunopathology in mice. Am J Respir Crit Care Med 2011;183:767-773.
    • (2011) Am J Respir Crit Care Med , vol.183 , pp. 767-773
    • Wanzeck, K.1    Boyd, K.L.2    McCullers, J.A.3
  • 55
    • 0023811767 scopus 로고
    • Carbohydrates of human immunodeficiency virus. Structures of oligosaccharides linked to the envelope glycoprotein 120
    • Geyer H, Holschbach C, Hunsmann G, Schneider J. Carbohydrates of human immunodeficiency virus. Structures of oligosaccharides linked to the envelope glycoprotein 120. J Biol Chem 1988;263:11760-11767.
    • (1988) J Biol Chem , vol.263 , pp. 11760-11767
    • Geyer, H.1    Holschbach, C.2    Hunsmann, G.3    Schneider, J.4
  • 56
    • 0026451818 scopus 로고
    • An O-linked carbohydrate neutralization epitope of HIV-1 gp 120 is expressed by HIV-1 env gene recombinant vaccinia virus
    • Hansen JE, Clausen H, Hu SL, Nielsen JO, Olofsson S. An O-linked carbohydrate neutralization epitope of HIV-1 gp 120 is expressed by HIV-1 env gene recombinant vaccinia virus. Arch Virol 1992;126:11-20.
    • (1992) Arch Virol , vol.126 , pp. 11-20
    • Hansen, J.E.1    Clausen, H.2    Hu, S.L.3    Nielsen, J.O.4    Olofsson, S.5
  • 57
    • 0027957921 scopus 로고
    • Human immunodeficiency virus type 1 envelope glycoprotein is modified by O-linked oligosaccharides
    • Bernstein HB, Tucker SP, Hunter E, Schutzbach JS, Compans RW. Human immunodeficiency virus type 1 envelope glycoprotein is modified by O-linked oligosaccharides. J Virol 1994;68:463-468.
    • (1994) J Virol , vol.68 , pp. 463-468
    • Bernstein, H.B.1    Tucker, S.P.2    Hunter, E.3    Schutzbach, J.S.4    Compans, R.W.5
  • 58
    • 77956385205 scopus 로고    scopus 로고
    • Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens
    • Doores KJ, et al. Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens. Proc Natl Acad Sci USA 2010;107:13800-13805.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 13800-13805
    • Doores, K.J.1
  • 59
    • 44649136618 scopus 로고    scopus 로고
    • Genetically destined potentials for N-linked glycosylation of influenza virus hemagglutinin
    • Igarashi M, Ito K, Kida H, Takada A. Genetically destined potentials for N-linked glycosylation of influenza virus hemagglutinin. Virology 2008;376:323-329.
    • (2008) Virology , vol.376 , pp. 323-329
    • Igarashi, M.1    Ito, K.2    Kida, H.3    Takada, A.4
  • 60
    • 79251480393 scopus 로고    scopus 로고
    • Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain
    • Das SR, Puigbo P, Hensley SE, Hurt DE, Bennink JR, Yewdell JW. Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain. PLoS Pathog 2010;6:e1001211.
    • (2010) PLoS Pathog , vol.6
    • Das, S.R.1    Puigbo, P.2    Hensley, S.E.3    Hurt, D.E.4    Bennink, J.R.5    Yewdell, J.W.6
  • 61
    • 0019432165 scopus 로고
    • Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
    • Wiley DC, Wilson IA, Skehel JJ. Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature 1981;289:373-378.
    • (1981) Nature , vol.289 , pp. 373-378
    • Wiley, D.C.1    Wilson, I.A.2    Skehel, J.J.3
  • 62
    • 0020738619 scopus 로고
    • The structure and role of the carbohydrate moieties of influenza virus haemagglutinin
    • Wilson IA, Ladner RC, Skehel JJ, Wiley DC. The structure and role of the carbohydrate moieties of influenza virus haemagglutinin. Biochem Soc Trans 1983;11:145-147.
    • (1983) Biochem Soc Trans , vol.11 , pp. 145-147
    • Wilson, I.A.1    Ladner, R.C.2    Skehel, J.J.3    Wiley, D.C.4
  • 63
    • 77952969448 scopus 로고    scopus 로고
    • Cross-neutralization of 1918 and 2009 influenza viruses: role of glycans in viral evolution and vaccine design
    • Wei CJ, et al. Cross-neutralization of 1918 and 2009 influenza viruses: role of glycans in viral evolution and vaccine design. Sci Transl Med 2010;2:24ra21.
    • (2010) Sci Transl Med , vol.2
    • Wei, C.J.1
  • 64
    • 77951165843 scopus 로고    scopus 로고
    • Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus
    • Xu R, Ekiert DC, Krause JC, Hai R, Crowe JE, Jr., Wilson IA. Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus. Science 2010;328:357-360.
    • (2010) Science , vol.328 , pp. 357-360
    • Xu, R.1    Ekiert, D.C.2    Krause, J.C.3    Hai, R.4    Crowe Jr., J.E.5    Wilson, I.A.6
  • 65
    • 70349923632 scopus 로고    scopus 로고
    • Glycosylation site-specific analysis of clade C HIV-1 envelope proteins
    • Go EP, et al. Glycosylation site-specific analysis of clade C HIV-1 envelope proteins. J Proteome Res 2009;8:4231-4242.
    • (2009) J Proteome Res , vol.8 , pp. 4231-4242
    • Go, E.P.1
  • 66
    • 79961184231 scopus 로고    scopus 로고
    • Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry
    • Go EP, et al. Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry. J Virol 2011;85:8270-8284.
    • (2011) J Virol , vol.85 , pp. 8270-8284
    • Go, E.P.1
  • 67
    • 80051677678 scopus 로고    scopus 로고
    • The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade
    • Bonomelli C, et al. The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade. PLoS ONE 2011;6:e23521.
    • (2011) PLoS ONE , vol.6
    • Bonomelli, C.1
  • 68
    • 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 1998;393:705-711.
    • (1998) Nature , vol.393 , pp. 705-711
    • Wyatt, R.1
  • 69
    • 0036181249 scopus 로고    scopus 로고
    • Viral persistance: HIV's strategies of immune system evasion
    • Johnson WE, Desrosiers RC. Viral persistance: HIV's strategies of immune system evasion. Annu Rev Med 2002;53:499-518.
    • (2002) Annu Rev Med , vol.53 , pp. 499-518
    • Johnson, W.E.1    Desrosiers, R.C.2
  • 70
    • 0141521564 scopus 로고    scopus 로고
    • Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1
    • Labrijn AF, et al. Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1. J Virol 2003;77:10557-10565.
    • (2003) J Virol , vol.77 , pp. 10557-10565
    • Labrijn, A.F.1
  • 71
    • 27744597054 scopus 로고    scopus 로고
    • Structure of a V3-containing HIV-1 gp120 core
    • Huang CC, et al. Structure of a V3-containing HIV-1 gp120 core. Science 2005;310:1025-1028.
    • (2005) Science , vol.310 , pp. 1025-1028
    • Huang, C.C.1
  • 72
    • 33144486096 scopus 로고    scopus 로고
    • Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1
    • Moore PL, et al. Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1. J Virol 2006;80:2515-2528.
    • (2006) J Virol , vol.80 , pp. 2515-2528
    • Moore, P.L.1
  • 73
  • 74
    • 38849090714 scopus 로고    scopus 로고
    • The C3-V4 region is a major target of autologous neutralizing antibodies in human immunodeficiency virus type 1 subtype C infection
    • Moore PL, et al. The C3-V4 region is a major target of autologous neutralizing antibodies in human immunodeficiency virus type 1 subtype C infection. J Virol 2008;82:1860-1869.
    • (2008) J Virol , vol.82 , pp. 1860-1869
    • Moore, P.L.1
  • 75
    • 56649083541 scopus 로고    scopus 로고
    • Humoral immunity to HIV-1: neutralisation and antibody effector functions
    • Willey S, Aasa-Chapman MM. Humoral immunity to HIV-1: neutralisation and antibody effector functions. Trends Microbiol 2008;16:596-604.
    • (2008) Trends Microbiol , vol.16 , pp. 596-604
    • Willey, S.1    Aasa-Chapman, M.M.2
  • 76
    • 9544239346 scopus 로고    scopus 로고
    • The consequence of passive administration of an anti-human 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 anti-human immunodeficiency virus type 1 neutralizing monoclonal antibody before challenge of chimpanzees with a primary virus isolate. J Virol 1996;70:6751-6758.
    • (1996) J Virol , vol.70 , pp. 6751-6758
    • Conley, A.J.1
  • 77
    • 0037405488 scopus 로고    scopus 로고
    • Defining the protective antibody response for HIV-1
    • Mascola JR. Defining the protective antibody response for HIV-1. Curr Mol Med 2003;3:209-216.
    • (2003) Curr Mol Med , vol.3 , pp. 209-216
    • Mascola, J.R.1
  • 78
    • 68349160853 scopus 로고    scopus 로고
    • Effective, low-titer antibody protection against low-dose repeated mucosal SHIV challenge in macaques
    • Hessell AJ, et al. Effective, low-titer antibody protection against low-dose repeated mucosal SHIV challenge in macaques. Nat Med 2009;15:951-954.
    • (2009) Nat Med , vol.15 , pp. 951-954
    • Hessell, A.J.1
  • 79
    • 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. Broadly neutralizing human anti-HIV antibody 2G12 is effective in protection against mucosal SHIV challenge even at low serum neutralizing titers. PLoS Pathog 2009;5:e1000433.
    • (2009) PLoS Pathog , vol.5
    • Hessell, A.J.1
  • 80
    • 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. 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 2009;84:1302-1313.
    • (2009) J Virol , vol.84 , pp. 1302-1313
    • Hessell, A.J.1
  • 81
    • 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. Frequency and phenotype of human immunodeficiency virus envelope-specific B cells from patients with broadly cross-neutralizing antibodies. J Virol 2009;83:188-199.
    • (2009) J Virol , vol.83 , pp. 188-199
    • Doria-Rose, N.A.1
  • 82
    • 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. Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection. J Virol 2009;83:757-769.
    • (2009) J Virol , vol.83 , pp. 757-769
    • Sather, D.N.1
  • 83
    • 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. 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 2009;83:7337-7348.
    • (2009) J Virol , vol.83 , pp. 7337-7348
    • Simek, M.D.1
  • 84
    • 69149083668 scopus 로고    scopus 로고
    • Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine?
    • Stamatatos L, Morris L, Burton DR, Mascola JR. Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine? Nat Med 2009;15:866-870.
    • (2009) Nat Med , vol.15 , pp. 866-870
    • Stamatatos, L.1    Morris, L.2    Burton, D.R.3    Mascola, J.R.4
  • 85
    • 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 1992;89:9339-9343.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9339-9343
    • Barbas 3rd, C.F.1
  • 86
    • 0027223565 scopus 로고
    • Molecular profile of an antibody response to HIV-1 as probed by combinatorial libraries
    • Barbas CF, 3rd, et al. Molecular profile of an antibody response to HIV-1 as probed by combinatorial libraries. J Mol Biol 1993;230:812-823.
    • (1993) J Mol Biol , vol.230 , pp. 812-823
    • Barbas 3rd, C.F.1
  • 87
    • 0028155283 scopus 로고
    • Generation of human monoclonal antibodies against HIV-1 proteins; electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization
    • Buchacher A, et al. Generation of human monoclonal antibodies against HIV-1 proteins; electrofusion and Epstein-Barr virus transformation for peripheral blood lymphocyte immortalization. AIDS Res Hum Retroviruses 1994;10:359-369.
    • (1994) AIDS Res Hum Retroviruses , vol.10 , pp. 359-369
    • Buchacher, A.1
  • 88
    • 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 2003;300:2065-2071.
    • (2003) Science , vol.300 , pp. 2065-2071
    • Calarese, D.A.1
  • 89
    • 4544379899 scopus 로고    scopus 로고
    • Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope
    • Ofek G, et al. Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope. J Virol 2004;78:10724-10737.
    • (2004) J Virol , vol.78 , pp. 10724-10737
    • Ofek, G.1
  • 90
    • 13844255333 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41
    • Cardoso RM, et al. Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41. Immunity 2005;22:163-173.
    • (2005) Immunity , vol.22 , pp. 163-173
    • Cardoso, R.M.1
  • 91
    • 33847101745 scopus 로고    scopus 로고
    • Structural definition of a conserved neutralization epitope on HIV-1 gp120
    • Zhou T, et al. Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature 2007;445:732-737.
    • (2007) Nature , vol.445 , pp. 732-737
    • Zhou, T.1
  • 92
    • 54849416088 scopus 로고    scopus 로고
    • Structural details of HIV-1 recognition by the broadly neutralizing monoclonal antibody 2F5: epitope conformation, antigen-recognition loop mobility, and anion-binding site
    • Julien JP, Bryson S, Nieva JL, Pai EF. Structural details of HIV-1 recognition by the broadly neutralizing monoclonal antibody 2F5: epitope conformation, antigen-recognition loop mobility, and anion-binding site. J Mol Biol 2008;384:377-392.
    • (2008) J Mol Biol , vol.384 , pp. 377-392
    • Julien, J.P.1    Bryson, S.2    Nieva, J.L.3    Pai, E.F.4
  • 93
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, et al. Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 2009;326:285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1
  • 94
    • 80052942203 scopus 로고    scopus 로고
    • Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing
    • Wu X, et al. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing. Science 2011;333:1593-1602.
    • (2011) Science , vol.333 , pp. 1593-1602
    • Wu, X.1
  • 95
    • 80052925616 scopus 로고    scopus 로고
    • Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding
    • Scheid JF, et al. Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science 2011;333:1633-1637.
    • (2011) Science , vol.333 , pp. 1633-1637
    • Scheid, J.F.1
  • 96
    • 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. Memory B cell antibodies to HIV-1 gp140 cloned from individuals infected with clade A and B viruses. PLoS ONE 2011;6:e24078.
    • (2011) PLoS ONE , vol.6
    • Mouquet, H.1
  • 97
    • 80053132436 scopus 로고    scopus 로고
    • Broad neutralization coverage of HIV by multiple highly potent antibodies
    • Walker LM, et al. Broad neutralization coverage of HIV by multiple highly potent antibodies. Nature 2011;477:466-470.
    • (2011) Nature , vol.477 , pp. 466-470
    • Walker, L.M.1
  • 98
    • 72649097490 scopus 로고    scopus 로고
    • Mining the B cell repertoire for broadly neutralizing monoclonal antibodies to HIV-1
    • Kwong PD, Mascola JR, Nabel GJ. Mining the B cell repertoire for broadly neutralizing monoclonal antibodies to HIV-1. Cell Host Microbe 2009;6:292-294.
    • (2009) Cell Host Microbe , vol.6 , pp. 292-294
    • Kwong, P.D.1    Mascola, J.R.2    Nabel, G.J.3
  • 99
    • 80053146815 scopus 로고    scopus 로고
    • Vaccinology: precisely tuned antibodies nab HIV
    • Clapham PR, Lu S. Vaccinology: precisely tuned antibodies nab HIV. Nature 2011;477:416-417.
    • (2011) Nature , vol.477 , pp. 416-417
    • Clapham, P.R.1    Lu, S.2
  • 101
    • 84863774072 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses
    • Burton DR, Poignard P, Stanfield RL, Wilson IA. Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses. Science 2012;337:183-186.
    • (2012) Science , vol.337 , pp. 183-186
    • Burton, D.R.1    Poignard, P.2    Stanfield, R.L.3    Wilson, I.A.4
  • 102
    • 0024833055 scopus 로고
    • Generation of a large combinatorial library of the immunoglobulin repertoire in phage lambda
    • Huse WD, et al. Generation of a large combinatorial library of the immunoglobulin repertoire in phage lambda. Science 1989;246:1275-1281.
    • (1989) Science , vol.246 , pp. 1275-1281
    • Huse, W.D.1
  • 103
    • 0027471177 scopus 로고
    • A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains
    • Okuno Y, Isegawa Y, Sasao F, Ueda S. A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains. J Virol 1993;67:2552-2558.
    • (1993) J Virol , vol.67 , pp. 2552-2558
    • Okuno, Y.1    Isegawa, Y.2    Sasao, F.3    Ueda, S.4
  • 104
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou T, et al. Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 2010;329:811-817.
    • (2010) Science , vol.329 , pp. 811-817
    • Zhou, T.1
  • 105
    • 84870317596 scopus 로고    scopus 로고
    • Structure and design of broadly-neutralizing antibodies against HIV
    • doi:10.1007/s10059-012-0104-4.
    • Ryu SE, Hendrickson WA. Structure and design of broadly-neutralizing antibodies against HIV. Mol Cells 2012;doi:10.1007/s10059-012-0104-4.
    • (2012) Mol Cells
    • Ryu, S.E.1    Hendrickson, W.A.2
  • 106
    • 70450182950 scopus 로고    scopus 로고
    • Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120
    • Chen L, et al. Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120. Science 2009;326:1123-1127.
    • (2009) Science , vol.326 , pp. 1123-1127
    • Chen, L.1
  • 107
    • 82755184131 scopus 로고    scopus 로고
    • Increasing the potency and breadth of an HIV antibody by using structure-based rational design
    • Diskin R, et al. Increasing the potency and breadth of an HIV antibody by using structure-based rational design. Science 2011;334:1289-1293.
    • (2011) Science , vol.334 , pp. 1289-1293
    • Diskin, R.1
  • 108
    • 34247106331 scopus 로고    scopus 로고
    • An affinity-enhanced neutralizing antibody against the membrane-proximal external region of human immunodeficiency virus type 1 gp41 recognizes an epitope between those of 2F5 and 4E10
    • Nelson JD, et al. An affinity-enhanced neutralizing antibody against the membrane-proximal external region of human immunodeficiency virus type 1 gp41 recognizes an epitope between those of 2F5 and 4E10. J Virol 2007;81:4033-4043.
    • (2007) J Virol , vol.81 , pp. 4033-4043
    • Nelson, J.D.1
  • 109
    • 40849136223 scopus 로고    scopus 로고
    • The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: dominant site of antibody neutralization and target for vaccine design
    • Montero M, van Houten NE, Wang X, Scott JK. The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: dominant site of antibody neutralization and target for vaccine design. Microbiol Mol Biol Rev 2008;72:54-84.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 54-84
    • Montero, M.1    van Houten, N.E.2    Wang, X.3    Scott, J.K.4
  • 110
    • 79959616682 scopus 로고    scopus 로고
    • Targeting HIV-1 gp41 in close proximity to the membrane using antibody and other molecules
    • Gach JS, Leaman DP, Zwick MB. Targeting HIV-1 gp41 in close proximity to the membrane using antibody and other molecules. Curr Top Med Chem 2011;11:2997-3021.
    • (2011) Curr Top Med Chem , vol.11 , pp. 2997-3021
    • Gach, J.S.1    Leaman, D.P.2    Zwick, M.B.3
  • 111
    • 70350309664 scopus 로고    scopus 로고
    • Crystallographic definition of the epitope promiscuity of the broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2F5: vaccine design implications
    • Bryson S, Julien JP, Hynes RC, Pai EF. Crystallographic definition of the epitope promiscuity of the broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2F5: vaccine design implications. J Virol 2009;83:11862-11875.
    • (2009) J Virol , vol.83 , pp. 11862-11875
    • Bryson, S.1    Julien, J.P.2    Hynes, R.C.3    Pai, E.F.4
  • 112
    • 0032980413 scopus 로고    scopus 로고
    • A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity
    • Salzwedel K, West JT, Hunter E. A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity. J Virol 1999;73:2469-2480.
    • (1999) J Virol , vol.73 , pp. 2469-2480
    • Salzwedel, K.1    West, J.T.2    Hunter, E.3
  • 113
    • 34548170245 scopus 로고    scopus 로고
    • Functional links between the fusion peptide-proximal polar segment and membrane-proximal region of human immunodeficiency virus gp41 in distinct phases of membrane fusion
    • Bellamy-McIntyre AK, et al. Functional links between the fusion peptide-proximal polar segment and membrane-proximal region of human immunodeficiency virus gp41 in distinct phases of membrane fusion. J Biol Chem 2007;282:23104-23116.
    • (2007) J Biol Chem , vol.282 , pp. 23104-23116
    • Bellamy-McIntyre, A.K.1
  • 114
    • 0028813111 scopus 로고
    • Determinants of human immunodeficiency virus type 1 envelope glycoprotein oligomeric structure
    • Poumbourios P, el Ahmar W, McPhee DA, Kemp BE. Determinants of human immunodeficiency virus type 1 envelope glycoprotein oligomeric structure. J Virol 1995;69:1209-1218.
    • (1995) J Virol , vol.69 , pp. 1209-1218
    • Poumbourios, P.1    El Ahmar, W.2    McPhee, D.A.3    Kemp, B.E.4
  • 115
    • 0033869815 scopus 로고    scopus 로고
    • Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusion
    • Suarez T, Gallaher WR, Agirre A, Goni FM, Nieva JL. Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusion. J Virol 2000;74:8038-8047.
    • (2000) J Virol , vol.74 , pp. 8038-8047
    • Suarez, T.1    Gallaher, W.R.2    Agirre, A.3    Goni, F.M.4    Nieva, J.L.5
  • 116
    • 0038418536 scopus 로고    scopus 로고
    • The pre-transmembrane region of the human immunodeficiency virus type-1 glycoprotein: a novel fusogenic sequence
    • Suarez T, Nir S, Goni FM, Saez-Cirion A, Nieva JL. The pre-transmembrane region of the human immunodeficiency virus type-1 glycoprotein: a novel fusogenic sequence. FEBS Lett 2000;477:145-149.
    • (2000) FEBS Lett , vol.477 , pp. 145-149
    • Suarez, T.1    Nir, S.2    Goni, F.M.3    Saez-Cirion, A.4    Nieva, J.L.5
  • 117
    • 0037077229 scopus 로고    scopus 로고
    • Sphingomyelin and cholesterol promote HIV-1 gp41 pretransmembrane sequence surface aggregation and membrane restructuring
    • Saez-Cirion A, et al. Sphingomyelin and cholesterol promote HIV-1 gp41 pretransmembrane sequence surface aggregation and membrane restructuring. J Biol Chem 2002;277:21776-21785.
    • (2002) J Biol Chem , vol.277 , pp. 21776-21785
    • Saez-Cirion, A.1
  • 118
    • 0035873475 scopus 로고    scopus 로고
    • Secretory IgA specific for a conserved epitope on gp41 envelope glycoprotein inhibits epithelial transcytosis of HIV-1
    • Alfsen A, Iniguez P, Bouguyon E, Bomsel M. Secretory IgA specific for a conserved epitope on gp41 envelope glycoprotein inhibits epithelial transcytosis of HIV-1. J Immunol 2001;166:6257-6265.
    • (2001) J Immunol , vol.166 , pp. 6257-6265
    • Alfsen, A.1    Iniguez, P.2    Bouguyon, E.3    Bomsel, M.4
  • 119
    • 0037067741 scopus 로고    scopus 로고
    • HIV-1 gp41 envelope residues 650-685 exposed on native virus act as a lectin to bind epithelial cell galactosyl ceramide
    • Alfsen A, Bomsel M. HIV-1 gp41 envelope residues 650-685 exposed on native virus act as a lectin to bind epithelial cell galactosyl ceramide. J Biol Chem 2002;277:25649-25659.
    • (2002) J Biol Chem , vol.277 , pp. 25649-25659
    • Alfsen, A.1    Bomsel, M.2
  • 120
    • 38049031709 scopus 로고    scopus 로고
    • The binding of HIV-1 gp41 membrane proximal domain to its mucosal receptor, galactosyl ceramide, is structure-dependent
    • Yu H, Alfsen A, Tudor D, Bomsel M. The binding of HIV-1 gp41 membrane proximal domain to its mucosal receptor, galactosyl ceramide, is structure-dependent. Cell Calcium 2008;43:73-82.
    • (2008) Cell Calcium , vol.43 , pp. 73-82
    • Yu, H.1    Alfsen, A.2    Tudor, D.3    Bomsel, M.4
  • 121
    • 0035859948 scopus 로고    scopus 로고
    • The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles
    • Schibli DJ, Montelaro RC, Vogel HJ. The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles. Biochemistry 2001;40:9570-9578.
    • (2001) Biochemistry , vol.40 , pp. 9570-9578
    • Schibli, D.J.1    Montelaro, R.C.2    Vogel, H.J.3
  • 122
    • 37849000389 scopus 로고    scopus 로고
    • HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane
    • Sun ZY, et al. HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane. Immunity 2008;28:52-63.
    • (2008) Immunity , vol.28 , pp. 52-63
    • Sun, Z.Y.1
  • 123
    • 69249220320 scopus 로고    scopus 로고
    • A conformational switch in human immunodeficiency virus gp41 revealed by the structures of overlapping epitopes recognized by neutralizing antibodies
    • Pejchal R, et al. A conformational switch in human immunodeficiency virus gp41 revealed by the structures of overlapping epitopes recognized by neutralizing antibodies. J Virol 2009;83:8451-8462.
    • (2009) J Virol , vol.83 , pp. 8451-8462
    • Pejchal, R.1
  • 124
    • 67049156802 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV-1 antibodies disrupt a hinge-related function of gp41 at the membrane interface
    • Song L, et al. Broadly neutralizing anti-HIV-1 antibodies disrupt a hinge-related function of gp41 at the membrane interface. Proc Natl Acad Sci USA 2009;106:9057-9062.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9057-9062
    • Song, L.1
  • 125
    • 80555131011 scopus 로고    scopus 로고
    • Antibody mechanics on a membrane-bound HIV segment essential for GP41-targeted viral neutralization
    • Kim M, et al. Antibody mechanics on a membrane-bound HIV segment essential for GP41-targeted viral neutralization. Nat Struct Mol Biol 2011;18:1235-1243.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 1235-1243
    • Kim, M.1
  • 126
    • 84055181327 scopus 로고    scopus 로고
    • Rapid development of glycan-specific, broad, and potent anti-HIV-1 gp120 neutralizing antibodies in an R5 SIV/HIV chimeric virus infected macaque
    • Walker LM, et al. Rapid development of glycan-specific, broad, and potent anti-HIV-1 gp120 neutralizing antibodies in an R5 SIV/HIV chimeric virus infected macaque. Proc Natl Acad Sci USA 2011;108:20125-20129.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 20125-20129
    • Walker, L.M.1
  • 127
    • 84863115983 scopus 로고    scopus 로고
    • High-mannose glycan-dependent epitopes are frequently targeted in broad neutralizing antibody responses during human immunodeficiency virus type 1 infection
    • Lavine CL, Lao S, Montefiori DC, Haynes BF, Sodroski JG, Yang X. High-mannose glycan-dependent epitopes are frequently targeted in broad neutralizing antibody responses during human immunodeficiency virus type 1 infection. J Virol 2012;86:2153-2164.
    • (2012) J Virol , vol.86 , pp. 2153-2164
    • Lavine, C.L.1    Lao, S.2    Montefiori, D.C.3    Haynes, B.F.4    Sodroski, J.G.5    Yang, X.6
  • 128
    • 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 CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ. 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 1990;265:10373-10382.
    • (1990) J Biol Chem , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 129
    • 77951988965 scopus 로고    scopus 로고
    • Lack of complex N-glycans on HIV-1 envelope glycoproteins preserves protein conformation and entry function
    • Eggink D, et al. Lack of complex N-glycans on HIV-1 envelope glycoproteins preserves protein conformation and entry function. Virology 2010;401:236-247.
    • (2010) Virology , vol.401 , pp. 236-247
    • Eggink, D.1
  • 130
    • 18244422922 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1->2 mannose residues on the outer face of gp120
    • Scanlan CN, et al. The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alpha1->2 mannose residues on the outer face of gp120. J Virol 2002;76:7306-7321.
    • (2002) J Virol , vol.76 , pp. 7306-7321
    • Scanlan, C.N.1
  • 131
    • 0023449237 scopus 로고
    • Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine
    • Walker BD, et al. Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine. Proc Natl Acad Sci USA 1987;84:8120-8124.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8120-8124
    • Walker, B.D.1
  • 132
    • 0034598905 scopus 로고    scopus 로고
    • DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells
    • Geijtenbeek TB, et al. DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells. Cell 2000;100:587-597.
    • (2000) Cell , vol.100 , pp. 587-597
    • Geijtenbeek, T.B.1
  • 133
    • 84860723906 scopus 로고    scopus 로고
    • Two distinct broadly neutralizing antibody specificities of different clonal lineages in a single HIV-1-infected donor: implications for vaccine design
    • Bonsignori M, et al. Two distinct broadly neutralizing antibody specificities of different clonal lineages in a single HIV-1-infected donor: implications for vaccine design. J Virol 2012;86:4688-4692.
    • (2012) J Virol , vol.86 , pp. 4688-4692
    • Bonsignori, M.1
  • 134
    • 82255179322 scopus 로고    scopus 로고
    • A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield
    • Pejchal R, et al. A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield. Science 2011;334:1097-1103.
    • (2011) Science , vol.334 , pp. 1097-1103
    • Pejchal, R.1
  • 135
    • 65549114651 scopus 로고    scopus 로고
    • Efficient recovery of high-affinity antibodies from a single-chain Fab yeast display library
    • Walker LM, Bowley DR, Burton DR. Efficient recovery of high-affinity antibodies from a single-chain Fab yeast display library. J Mol Biol 2009;389:365-375.
    • (2009) J Mol Biol , vol.389 , pp. 365-375
    • Walker, L.M.1    Bowley, D.R.2    Burton, D.R.3
  • 136
    • 77954912140 scopus 로고    scopus 로고
    • Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1
    • Pejchal R, et al. Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1. Proc Natl Acad Sci USA 2010;107:11483-11488.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 11483-11488
    • Pejchal, R.1
  • 137
    • 77954982131 scopus 로고    scopus 로고
    • Crystal structure of PG16 and chimeric dissection with somatically related PG9: structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1
    • Pancera M, et al. Crystal structure of PG16 and chimeric dissection with somatically related PG9: structure-function analysis of two quaternary-specific antibodies that effectively neutralize HIV-1. J Virol 2010;84:8098-8110.
    • (2010) J Virol , vol.84 , pp. 8098-8110
    • Pancera, M.1
  • 138
    • 0020416123 scopus 로고
    • The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype)
    • Caton AJ, Brownlee GG, Yewdell JW, Gerhard W. The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype). Cell 1982;31:417-427.
    • (1982) Cell , vol.31 , pp. 417-427
    • Caton, A.J.1    Brownlee, G.G.2    Yewdell, J.W.3    Gerhard, W.4
  • 139
    • 80052184942 scopus 로고    scopus 로고
    • Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin
    • Whittle JR, et al. Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin. Proc Natl Acad Sci USA 2011;108:14216-14221.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 14216-14221
    • Whittle, J.R.1
  • 140
    • 84866953140 scopus 로고    scopus 로고
    • Cross-neutralization of influenza A viruses mediated by a single antibody loop into the receptor binding site
    • 2012;doi:10.1038/nature11414.
    • Ekiert DC, et al. Cross-neutralization of influenza A viruses mediated by a single antibody loop into the receptor binding site. Nature, 2012;doi:10.1038/nature11414.
    • Nature
    • Ekiert, D.C.1
  • 141
    • 64949164763 scopus 로고    scopus 로고
    • High-throughput isolation of immunoglobulin genes from single human B cells and expression as monoclonal antibodies
    • Liao HX, et al. High-throughput isolation of immunoglobulin genes from single human B cells and expression as monoclonal antibodies. J Virol Methods 2009;158:171-179.
    • (2009) J Virol Methods , vol.158 , pp. 171-179
    • Liao, H.X.1
  • 142
    • 84859510667 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies against influenza virus and prospects for universal therapies
    • Ekiert DC, Wilson IA. Broadly neutralizing antibodies against influenza virus and prospects for universal therapies. Curr Opin Virol 2012;2:134-141.
    • (2012) Curr Opin Virol , vol.2 , pp. 134-141
    • Ekiert, D.C.1    Wilson, I.A.2
  • 143
    • 58049198443 scopus 로고    scopus 로고
    • Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+ memory B cells
    • Throsby M, et al. Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+ memory B cells. PLoS ONE 2008;3:e3942.
    • (2008) PLoS ONE , vol.3
    • Throsby, M.1
  • 144
    • 43149109969 scopus 로고    scopus 로고
    • Combinatorial antibody libraries from survivors of the Turkish H5N1 avian influenza outbreak reveal virus neutralization strategies
    • Kashyap AK, et al. Combinatorial antibody libraries from survivors of the Turkish H5N1 avian influenza outbreak reveal virus neutralization strategies. Proc Natl Acad Sci USA 2008;105:5986-5991.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 5986-5991
    • Kashyap, A.K.1
  • 145
    • 64849114224 scopus 로고    scopus 로고
    • Antibody recognition of a highly conserved influenza virus epitope
    • Ekiert DC, et al. Antibody recognition of a highly conserved influenza virus epitope. Science 2009;324:246-251.
    • (2009) Science , vol.324 , pp. 246-251
    • Ekiert, D.C.1
  • 146
    • 62049083943 scopus 로고    scopus 로고
    • Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses
    • Sui J, et al. Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses. Nat Struct Mol Biol 2009;16:265-273.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 265-273
    • Sui, J.1
  • 147
    • 77951876927 scopus 로고    scopus 로고
    • Heterosubtypic neutralizing antibodies are produced by individuals immunized with a seasonal influenza vaccine
    • Corti D, et al. Heterosubtypic neutralizing antibodies are produced by individuals immunized with a seasonal influenza vaccine. J Clin Invest 2010;120:1663-1673.
    • (2010) J Clin Invest , vol.120 , pp. 1663-1673
    • Corti, D.1
  • 148
    • 78651488739 scopus 로고    scopus 로고
    • Broadly cross-reactive antibodies dominate the human B cell response against 2009 pandemic H1N1 influenza virus infection
    • Wrammert J, et al. Broadly cross-reactive antibodies dominate the human B cell response against 2009 pandemic H1N1 influenza virus infection. J Exp Med 2011;208:181-193.
    • (2011) J Exp Med , vol.208 , pp. 181-193
    • Wrammert, J.1
  • 149
    • 77956119219 scopus 로고    scopus 로고
    • Induction of broadly neutralizing H1N1 influenza antibodies by vaccination
    • Wei CJ, et al. Induction of broadly neutralizing H1N1 influenza antibodies by vaccination. Science 2010;329:1060-1064.
    • (2010) Science , vol.329 , pp. 1060-1064
    • Wei, C.J.1
  • 150
    • 80051635697 scopus 로고    scopus 로고
    • A highly conserved neutralizing epitope on group 2 influenza A viruses
    • Ekiert DC, et al. A highly conserved neutralizing epitope on group 2 influenza A viruses. Science 2011;333:843-850.
    • (2011) Science , vol.333 , pp. 843-850
    • Ekiert, D.C.1
  • 151
    • 80051670323 scopus 로고    scopus 로고
    • A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins
    • Corti D, et al. A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins. Science 2011;333:850-856.
    • (2011) Science , vol.333 , pp. 850-856
    • Corti, D.1
  • 152
    • 84866122029 scopus 로고    scopus 로고
    • Highly conserved protective epitopes on influenza B viruses
    • Dreyfus C, et al. Highly conserved protective epitopes on influenza B viruses. Science 2012;337:1343-1348.
    • (2012) Science , vol.337 , pp. 1343-1348
    • Dreyfus, C.1
  • 153
    • 65749107719 scopus 로고    scopus 로고
    • HIV-1 and influenza antibodies: seeing antigens in new ways
    • Kwong PD, Wilson IA. HIV-1 and influenza antibodies: seeing antigens in new ways. Nat Immunol 2009;10:573-578.
    • (2009) Nat Immunol , vol.10 , pp. 573-578
    • Kwong, P.D.1    Wilson, I.A.2
  • 154
    • 0036063659 scopus 로고    scopus 로고
    • An antibody that prevents the hemagglutinin low pH fusogenic transition
    • Barbey-Martin C, et al. An antibody that prevents the hemagglutinin low pH fusogenic transition. Virology 2002;294:70-74.
    • (2002) Virology , vol.294 , pp. 70-74
    • Barbey-Martin, C.1
  • 156
    • 77957355961 scopus 로고    scopus 로고
    • Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation
    • Mouquet H, et al. Polyreactivity increases the apparent affinity of anti-HIV antibodies by heteroligation. Nature 2010;467:591-595.
    • (2010) Nature , vol.467 , pp. 591-595
    • Mouquet, H.1
  • 157
    • 0019065845 scopus 로고
    • Carbohydrate composition of the oligosaccharide units of the haemagglutinin from the Hong Kong influenza virus A/Memphis/102/72
    • Ward CW, Gleeson PA, Dopheide TA. Carbohydrate composition of the oligosaccharide units of the haemagglutinin from the Hong Kong influenza virus A/Memphis/102/72. Biochem J 1980;189:649-652.
    • (1980) Biochem J , vol.189 , pp. 649-652
    • Ward, C.W.1    Gleeson, P.A.2    Dopheide, T.A.3
  • 158
    • 0031041235 scopus 로고    scopus 로고
    • The glycosylation of the influenza A virus hemagglutinin by mammalian cells. A site-specific study
    • Mir-Shekari SY, Ashford DA, Harvey DJ, Dwek RA, Schulze IT. The glycosylation of the influenza A virus hemagglutinin by mammalian cells. A site-specific study. J Biol Chem 1997;272:4027-4036.
    • (1997) J Biol Chem , vol.272 , pp. 4027-4036
    • Mir-Shekari, S.Y.1    Ashford, D.A.2    Harvey, D.J.3    Dwek, R.A.4    Schulze, I.T.5
  • 159
    • 33846172297 scopus 로고    scopus 로고
    • Rational modifications of HIV-1 envelope glycoproteins for immunogen design
    • Phogat S, Wyatt R. Rational modifications of HIV-1 envelope glycoproteins for immunogen design. Curr Pharm Des 2007;13:213-227.
    • (2007) Curr Pharm Des , vol.13 , pp. 213-227
    • Phogat, S.1    Wyatt, R.2
  • 160
    • 77953543379 scopus 로고    scopus 로고
    • Rational antibody-based HIV-1 vaccine design: current approaches and future directions
    • Walker LM, Burton DR. Rational antibody-based HIV-1 vaccine design: current approaches and future directions. Curr Opin Immunol 2010;22:358-366.
    • (2010) Curr Opin Immunol , vol.22 , pp. 358-366
    • Walker, L.M.1    Burton, D.R.2
  • 161
    • 67249085575 scopus 로고    scopus 로고
    • Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site
    • Dey B, et al. Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site. PLoS Pathog 2009;5:e1000445.
    • (2009) PLoS Pathog , vol.5
    • Dey, B.1
  • 162
    • 77956247505 scopus 로고    scopus 로고
    • Design of a non-glycosylated outer domain-derived HIV-1 gp120 immunogen that binds to CD4 and induces neutralizing antibodies
    • Bhattacharyya S, et al. Design of a non-glycosylated outer domain-derived HIV-1 gp120 immunogen that binds to CD4 and induces neutralizing antibodies. J Biol Chem 2010;285:27100-27110.
    • (2010) J Biol Chem , vol.285 , pp. 27100-27110
    • Bhattacharyya, S.1
  • 163
    • 80054836686 scopus 로고    scopus 로고
    • Computation-guided backbone grafting of a discontinuous motif onto a protein scaffold
    • Azoitei ML, et al. Computation-guided backbone grafting of a discontinuous motif onto a protein scaffold. Science 2011;334:373-376.
    • (2011) Science , vol.334 , pp. 373-376
    • Azoitei, M.L.1
  • 164
    • 82455192354 scopus 로고    scopus 로고
    • Improving immunogenicity of HIV-1 envelope gp120 by glycan removal and immune complex formation
    • Kumar R, Tuen M, Li H, Tse DB, Hioe CE. Improving immunogenicity of HIV-1 envelope gp120 by glycan removal and immune complex formation. Vaccine 2011;29:9064-9074.
    • (2011) Vaccine , vol.29 , pp. 9064-9074
    • Kumar, R.1    Tuen, M.2    Li, H.3    Tse, D.B.4    Hioe, C.E.5
  • 165
    • 84855433610 scopus 로고    scopus 로고
    • An engineered mutant of HIV-1 gp120 formulated with adjuvant Quil A promotes elicitation of antibody responses overlapping the CD4-binding site
    • Ahmed FK, Clark BE, Burton DR, Pantophlet R. An engineered mutant of HIV-1 gp120 formulated with adjuvant Quil A promotes elicitation of antibody responses overlapping the CD4-binding site. Vaccine 2012;30:922-930.
    • (2012) Vaccine , vol.30 , pp. 922-930
    • Ahmed, F.K.1    Clark, B.E.2    Burton, D.R.3    Pantophlet, R.4
  • 166
    • 84863788697 scopus 로고    scopus 로고
    • Partial enzymatic deglycosylation preserves the structure of cleaved recombinant HIV-1 envelope glycoprotein trimers
    • Depetris RS, et al. Partial enzymatic deglycosylation preserves the structure of cleaved recombinant HIV-1 envelope glycoprotein trimers. J Biol Chem 2012;287:24239-24254.
    • (2012) J Biol Chem , vol.287 , pp. 24239-24254
    • Depetris, R.S.1
  • 167
    • 78149242586 scopus 로고    scopus 로고
    • Elicitation of structure-specific antibodies by epitope scaffolds
    • Ofek G, et al. Elicitation of structure-specific antibodies by epitope scaffolds. Proc Natl Acad Sci USA 2010;107:17880-17887.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17880-17887
    • Ofek, G.1
  • 168
    • 82555168289 scopus 로고    scopus 로고
    • Structure-based design of a protein immunogen that displays an HIV-1 gp41 neutralizing epitope
    • Stanfield RL, Julien JP, Pejchal R, Gach JS, Zwick MB, Wilson IA. Structure-based design of a protein immunogen that displays an HIV-1 gp41 neutralizing epitope. J Mol Biol 2011;414:460-476.
    • (2011) J Mol Biol , vol.414 , pp. 460-476
    • Stanfield, R.L.1    Julien, J.P.2    Pejchal, R.3    Gach, J.S.4    Zwick, M.B.5    Wilson, I.A.6
  • 169
    • 84855258847 scopus 로고    scopus 로고
    • Computational design of high-affinity epitope scaffolds by backbone grafting of a linear epitope
    • Azoitei ML, et al. Computational design of high-affinity epitope scaffolds by backbone grafting of a linear epitope. J Mol Biol 2012;415:175-192.
    • (2012) J Mol Biol , vol.415 , pp. 175-192
    • Azoitei, M.L.1
  • 170
    • 73949133588 scopus 로고    scopus 로고
    • Role of HIV membrane in neutralization by two broadly neutralizing antibodies
    • Alam SM, et al. Role of HIV membrane in neutralization by two broadly neutralizing antibodies. Proc Natl Acad Sci USA 2009;106:20234-20239.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20234-20239
    • Alam, S.M.1
  • 171
    • 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. Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region. J Virol 2010;84:2955-2962.
    • (2010) J Virol , vol.84 , pp. 2955-2962
    • Ofek, G.1
  • 172
    • 73849143129 scopus 로고    scopus 로고
    • Interactions between lipids and human anti-HIV antibody 4E10 can be reduced without ablating neutralizing activity
    • Xu H, et al. Interactions between lipids and human anti-HIV antibody 4E10 can be reduced without ablating neutralizing activity. J Virol 2010;84:1076-1088.
    • (2010) J Virol , vol.84 , pp. 1076-1088
    • Xu, H.1
  • 173
    • 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. 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 2010;84:4136-4147.
    • (2010) J Virol , vol.84 , pp. 4136-4147
    • Julien, J.P.1
  • 174
    • 84864621158 scopus 로고    scopus 로고
    • Structure-guided alterations of the gp41-directed HIV-1 broadly neutralizing antibody 2F5 reveal new properties regarding its neutralizing function
    • Guenaga J, Wyatt RT. Structure-guided alterations of the gp41-directed HIV-1 broadly neutralizing antibody 2F5 reveal new properties regarding its neutralizing function. PLoS Pathog 2012;8:e1002806.
    • (2012) PLoS Pathog , vol.8
    • Guenaga, J.1    Wyatt, R.T.2
  • 175
    • 45749122331 scopus 로고    scopus 로고
    • An engineered Saccharomyces cerevisiae strain binds the broadly neutralizing human immunodeficiency virus type 1 antibody 2G12 and elicits mannose-specific gp120-binding antibodies
    • Luallen RJ, et al. An engineered Saccharomyces cerevisiae strain binds the broadly neutralizing human immunodeficiency virus type 1 antibody 2G12 and elicits mannose-specific gp120-binding antibodies. J Virol 2008;82:6447-6457.
    • (2008) J Virol , vol.82 , pp. 6447-6457
    • Luallen, R.J.1
  • 176
    • 45749138808 scopus 로고    scopus 로고
    • A glycoconjugate antigen based on the recognition motif of a broadly neutralizing human immunodeficiency virus antibody, 2G12, is immunogenic but elicits antibodies unable to bind to the self glycans of gp120
    • Astronomo RD, et al. A glycoconjugate antigen based on the recognition motif of a broadly neutralizing human immunodeficiency virus antibody, 2G12, is immunogenic but elicits antibodies unable to bind to the self glycans of gp120. J Virol 2008;82:6359-6368.
    • (2008) J Virol , vol.82 , pp. 6359-6368
    • Astronomo, R.D.1
  • 177
    • 55249109998 scopus 로고    scopus 로고
    • Antigenic mimicry of the HIV envelope by AIDS-associated pathogens
    • Dunlop DC, et al. Antigenic mimicry of the HIV envelope by AIDS-associated pathogens. AIDS 2008;22:2214-2217.
    • (2008) AIDS , vol.22 , pp. 2214-2217
    • Dunlop, D.C.1
  • 178
    • 65349132918 scopus 로고    scopus 로고
    • A yeast glycoprotein shows high-affinity binding to the broadly neutralizing human immunodeficiency virus antibody 2G12 and inhibits gp120 interactions with 2G12 and DC-SIGN
    • Luallen RJ, et al. A yeast glycoprotein shows high-affinity binding to the broadly neutralizing human immunodeficiency virus antibody 2G12 and inhibits gp120 interactions with 2G12 and DC-SIGN. J Virol 2009;83:4861-4870.
    • (2009) J Virol , vol.83 , pp. 4861-4870
    • Luallen, R.J.1
  • 179
    • 77956366187 scopus 로고    scopus 로고
    • Polysaccharide mimicry of the epitope of the broadly neutralizing anti-HIV antibody, 2G12, induces enhanced antibody responses to self oligomannose glycans
    • Dunlop DC, et al. Polysaccharide mimicry of the epitope of the broadly neutralizing anti-HIV antibody, 2G12, induces enhanced antibody responses to self oligomannose glycans. Glycobiology 2010;20:812-823.
    • (2010) Glycobiology , vol.20 , pp. 812-823
    • Dunlop, D.C.1
  • 180
    • 78049254402 scopus 로고    scopus 로고
    • A nonself sugar mimic of the HIV glycan shield shows enhanced antigenicity
    • Doores KJ, et al. A nonself sugar mimic of the HIV glycan shield shows enhanced antigenicity. Proc Natl Acad Sci USA 2010;107:17107-17112.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17107-17112
    • Doores, K.J.1
  • 181
    • 77957201600 scopus 로고    scopus 로고
    • Very few substitutions in a germ line antibody are required to initiate significant domain exchange
    • Huber M, et al. Very few substitutions in a germ line antibody are required to initiate significant domain exchange. J Virol 2010;84:10700-10707.
    • (2010) J Virol , vol.84 , pp. 10700-10707
    • Huber, M.1
  • 182
    • 84862777880 scopus 로고    scopus 로고
    • Characterization of germline antibody libraries from human umbilical cord blood and selection of monoclonal antibodies to viral envelope glycoproteins: implications for mechanisms of immune evasion and design of vaccine immunogens
    • Chen W, Streaker ED, Russ DE, Feng Y, Prabakaran P, Dimitrov DS. Characterization of germline antibody libraries from human umbilical cord blood and selection of monoclonal antibodies to viral envelope glycoproteins: implications for mechanisms of immune evasion and design of vaccine immunogens. Biochem Biophys Res Commun 2012;417:1164-1169.
    • (2012) Biochem Biophys Res Commun , vol.417 , pp. 1164-1169
    • Chen, W.1    Streaker, E.D.2    Russ, D.E.3    Feng, Y.4    Prabakaran, P.5    Dimitrov, D.S.6
  • 183
    • 84860759632 scopus 로고    scopus 로고
    • B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study
    • Haynes BF, Kelsoe G, Harrison SC, Kepler TB. B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study. Nat Biotechnol 2012;30:423-433.
    • (2012) Nat Biotechnol , vol.30 , pp. 423-433
    • Haynes, B.F.1    Kelsoe, G.2    Harrison, S.C.3    Kepler, T.B.4
  • 184
    • 84864363185 scopus 로고    scopus 로고
    • Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120
    • West AP, Jr., Diskin R, Nussenzweig MC, Bjorkman PJ. Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120. Proc Natl Acad Sci USA 2012;109:E2083-E2090.
    • (2012) Proc Natl Acad Sci USA , vol.109
    • West Jr., A.P.1    Diskin, R.2    Nussenzweig, M.C.3    Bjorkman, P.J.4
  • 185
    • 78649953803 scopus 로고    scopus 로고
    • Vaccination with a synthetic peptide from the influenza virus hemagglutinin provides protection against distinct viral subtypes
    • Wang TT, et al. Vaccination with a synthetic peptide from the influenza virus hemagglutinin provides protection against distinct viral subtypes. Proc Natl Acad Sci USA 2010;107:18979-18984.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 18979-18984
    • Wang, T.T.1
  • 186
    • 79952140653 scopus 로고    scopus 로고
    • Influenza virus vaccine based on the conserved hemagglutinin stalk domain
    • Steel J, et al. Influenza virus vaccine based on the conserved hemagglutinin stalk domain. MBio 2010;1:e000018-10.
    • (2010) MBio , vol.1
    • Steel, J.1
  • 187
    • 84863115945 scopus 로고    scopus 로고
    • Hemagglutinin stalk antibodies elicited by the 2009 pandemic influenza virus as a mechanism for the extinction of seasonal H1N1 viruses
    • Pica N, et al. Hemagglutinin stalk antibodies elicited by the 2009 pandemic influenza virus as a mechanism for the extinction of seasonal H1N1 viruses. Proc Natl Acad Sci USA 2012;109:2573-2578.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 2573-2578
    • Pica, N.1
  • 188
    • 84861325359 scopus 로고    scopus 로고
    • Influenza viruses expressing chimeric hemagglutinins: globular head and stalk domains derived from different subtypes
    • Hai R, et al. Influenza viruses expressing chimeric hemagglutinins: globular head and stalk domains derived from different subtypes. J Virol 2012;86:5774-5781.
    • (2012) J Virol , vol.86 , pp. 5774-5781
    • Hai, R.1
  • 189
    • 79956017135 scopus 로고    scopus 로고
    • Computational design of proteins targeting the conserved stem region of influenza hemagglutinin
    • Fleishman SJ, et al. Computational design of proteins targeting the conserved stem region of influenza hemagglutinin. Science 2011;332:816-821.
    • (2011) Science , vol.332 , pp. 816-821
    • Fleishman, S.J.1
  • 190
    • 84862025262 scopus 로고    scopus 로고
    • Optimization of affinity, specificity and function of designed influenza inhibitors using deep sequencing
    • Whitehead TA, et al. Optimization of affinity, specificity and function of designed influenza inhibitors using deep sequencing. Nat Biotechnol 2012;30:543-548.
    • (2012) Nat Biotechnol , vol.30 , pp. 543-548
    • Whitehead, T.A.1
  • 191
    • 80053474133 scopus 로고    scopus 로고
    • A broadly neutralizing human monoclonal antibody that recognizes a conserved, novel epitope on the globular head of the influenza H1N1 virus hemagglutinin
    • Krause JC, Tsibane T, Tumpey TM, Huffman CJ, Basler CF, Crowe JE, Jr.. A broadly neutralizing human monoclonal antibody that recognizes a conserved, novel epitope on the globular head of the influenza H1N1 virus hemagglutinin. J Virol 2011;85:10905-10908.
    • (2011) J Virol , vol.85 , pp. 10905-10908
    • Krause, J.C.1    Tsibane, T.2    Tumpey, T.M.3    Huffman, C.J.4    Basler, C.F.5    Crowe Jr., J.E.6
  • 192
    • 80053557269 scopus 로고    scopus 로고
    • Epitope-specific human influenza antibody repertoires diversify by B cell intraclonal sequence divergence and interclonal convergence
    • Krause JC, et al. Epitope-specific human influenza antibody repertoires diversify by B cell intraclonal sequence divergence and interclonal convergence. J Immunol 2011;187:3704-3711.
    • (2011) J Immunol , vol.187 , pp. 3704-3711
    • Krause, J.C.1
  • 193
    • 84863568230 scopus 로고    scopus 로고
    • Human monoclonal antibodies to pandemic 1957 H2N2 and pandemic 1968 H3N2 influenza viruses
    • Krause JC, et al. Human monoclonal antibodies to pandemic 1957 H2N2 and pandemic 1968 H3N2 influenza viruses. J Virol 2012;86:6334-6340.
    • (2012) J Virol , vol.86 , pp. 6334-6340
    • Krause, J.C.1
  • 194
    • 75749120153 scopus 로고    scopus 로고
    • Monoclonal antibodies in man that neutralized H3N2 influenza viruses were classified into three groups with distinct strain specificity: 1968-1973, 1977-1993 and 1997-2003
    • Okada J, et al. Monoclonal antibodies in man that neutralized H3N2 influenza viruses were classified into three groups with distinct strain specificity: 1968-1973, 1977-1993 and 1997-2003. Virology 2010;397:322-330.
    • (2010) Virology , vol.397 , pp. 322-330
    • Okada, J.1
  • 195
    • 79251501002 scopus 로고    scopus 로고
    • Localization of epitopes recognized by monoclonal antibodies that neutralized the H3N2 influenza viruses in man
    • Okada J, et al. Localization of epitopes recognized by monoclonal antibodies that neutralized the H3N2 influenza viruses in man. J Gen Virol 2011;92:326-335.
    • (2011) J Gen Virol , vol.92 , pp. 326-335
    • Okada, J.1
  • 196
    • 80055111172 scopus 로고    scopus 로고
    • Naturally occurring antibodies in humans can neutralize a variety of influenza virus strains, including H3, H1, H2, and H5
    • Ohshima N, Iba Y, Kubota-Koketsu R, Asano Y, Okuno Y, Kurosawa Y. Naturally occurring antibodies in humans can neutralize a variety of influenza virus strains, including H3, H1, H2, and H5. J Virol 2011;85:11048-11057.
    • (2011) J Virol , vol.85 , pp. 11048-11057
    • Ohshima, N.1    Iba, Y.2    Kubota-Koketsu, R.3    Asano, Y.4    Okuno, Y.5    Kurosawa, Y.6
  • 197
    • 63449125762 scopus 로고    scopus 로고
    • Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of influenza A viruses
    • Yoshida R, et al. Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of influenza A viruses. PLoS Pathog 2009;5:e1000350.
    • (2009) PLoS Pathog , vol.5
    • Yoshida, R.1
  • 198
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Pettersen EF, et al. UCSF Chimera-a visualization system for exploratory research and analysis. J Comput Chem 2004;25:1605-1612.
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 199
    • 0023660979 scopus 로고
    • Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution
    • Sheriff S, Hendrickson WA, Smith JL. Structure of myohemerythrin in the azidomet state at 1.7/1.3 Å resolution. J Mol Biol 1987;197:273-296.
    • (1987) J Mol Biol , vol.197 , pp. 273-296
    • Sheriff, S.1    Hendrickson, W.A.2    Smith, J.L.3


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