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Volumn 332, Issue 1, 2005, Pages 145-156

Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage

Author keywords

Glycoproteins; HIV 1; Precursor cleavage

Indexed keywords

CD4 ANTIGEN; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 160; GLYCOPROTEIN GP 41; NEUTRALIZING ANTIBODY; OLIGOMER; PROTEIN PRECURSOR;

EID: 12344264596     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virol.2004.10.042     Document Type: Article
Times cited : (132)

References (63)
  • 2
    • 0032901996 scopus 로고    scopus 로고
    • Interactions of the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes modulate intracellular and cell-surface expression of envelope glycoproteins
    • C. Berlioz-Torrent, B.L. Shacklett, L. Erdtmann, L. Delamarre, I. Bouchaert, P. Sonigo, M.C. Dokhelar, and R. Benarous Interactions of the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes modulate intracellular and cell-surface expression of envelope glycoproteins J. Virol. 73 2 1999 1350 1361
    • (1999) J. Virol. , vol.73 , Issue.2 , pp. 1350-1361
    • Berlioz-Torrent, C.1    Shacklett, B.L.2    Erdtmann, L.3    Delamarre, L.4    Bouchaert, I.5    Sonigo, P.6    Dokhelar, M.C.7    Benarous, R.8
  • 3
    • 0033985999 scopus 로고    scopus 로고
    • A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure
    • J.M. Binley, R.W. Sanders, B. Clas, N. Schuelke, A. Master, Y. Guo, F. Kajumo, D.J. Anselma, P.J. Maddon, W.C. Olson, and J.P. Moore A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure J. Virol. 74 2 2000 627 643
    • (2000) J. Virol. , vol.74 , Issue.2 , pp. 627-643
    • Binley, J.M.1    Sanders, R.W.2    Clas, B.3    Schuelke, N.4    Master, A.5    Guo, Y.6    Kajumo, F.7    Anselma, D.J.8    Maddon, P.J.9    Olson, W.C.10    Moore, J.P.11
  • 5
    • 0025319347 scopus 로고
    • Mutational analysis of the human immunodeficiency virus type 1 env gene product proteolytic cleavage site
    • V. Bosch, and M. Pawlita Mutational analysis of the human immunodeficiency virus type 1 env gene product proteolytic cleavage site J. Virol. 64 5 1990 2337 2344
    • (1990) J. Virol. , vol.64 , Issue.5 , pp. 2337-2344
    • Bosch, V.1    Pawlita, M.2
  • 7
    • 0036317971 scopus 로고    scopus 로고
    • Oligomeric structure of the human immunodeficiency virus type 1 envelope protein on the virion surface
    • R.J. Center, R.D. Leapman, J. Lebowitz, L.O. Arthur, P.L. Earl, and B. Moss Oligomeric structure of the human immunodeficiency virus type 1 envelope protein on the virion surface J. Virol. 76 15 2002 7863 7867
    • (2002) J. Virol. , vol.76 , Issue.15 , pp. 7863-7867
    • Center, R.J.1    Leapman, R.D.2    Lebowitz, J.3    Arthur, L.O.4    Earl, P.L.5    Moss, B.6
  • 8
    • 0036096976 scopus 로고    scopus 로고
    • Modifications of the human immunodeficiency virus envelope glycoprotein enhance immunogenicity for genetic immunization
    • B.K. Chakrabarti, W.P. Kong, B.Y. Wu, Z.Y. Yang, J. Friborg, X. Ling, S.R. King, D.C. Montefiori, and G.J. Nabel Modifications of the human immunodeficiency virus envelope glycoprotein enhance immunogenicity for genetic immunization J. Virol. 76 11 2002 5357 5368
    • (2002) J. Virol. , vol.76 , Issue.11 , pp. 5357-5368
    • Chakrabarti, B.K.1    Kong, W.P.2    Wu, B.Y.3    Yang, Z.Y.4    Friborg, J.5    Ling, X.6    King, S.R.7    Montefiori, D.C.8    Nabel, G.J.9
  • 9
    • 18844470928 scopus 로고    scopus 로고
    • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
    • J. Chen, K.H. Lee, D.A. Steinhauer, D.J. Stevens, J.J. Skehel, and D.C. Wiley Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation Cell 95 3 1998 409 417
    • (1998) Cell , vol.95 , Issue.3 , pp. 409-417
    • Chen, J.1    Lee, K.H.2    Steinhauer, D.A.3    Stevens, D.J.4    Skehel, J.J.5    Wiley, D.C.6
  • 10
    • 0035083470 scopus 로고    scopus 로고
    • The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion
    • L. Chen, J.J. Gorman, J. McKimm-Breschkin, L.J. Lawrence, P.A. Tulloch, B.J. Smith, P.M. Colman, and M.C. Lawrence The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion Structure (Camb.) 9 3 2001 255 266
    • (2001) Structure (Camb.) , vol.9 , Issue.3 , pp. 255-266
    • Chen, L.1    Gorman, J.J.2    McKimm-Breschkin, J.3    Lawrence, L.J.4    Tulloch, P.A.5    Smith, B.J.6    Colman, P.M.7    Lawrence, M.C.8
  • 11
    • 0036091692 scopus 로고    scopus 로고
    • Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU). Is the primary determinant of SU content of purified human immunodeficiency virus type 1 and simian immunodeficiency virus
    • E. Chertova, J.W. Bess Jr., B.J. Crise, I.R. Sowder, T.M. Schaden, J.M. Hilburn, J.A. Hoxie, R.E. Benveniste, J.D. Lifson, L.E. Henderson, and L.O. Arthur Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU). Is the primary determinant of SU content of purified human immunodeficiency virus type 1 and simian immunodeficiency virus J. Virol. 76 11 2002 5315 5325
    • (2002) J. Virol. , vol.76 , Issue.11 , pp. 5315-5325
    • Chertova, E.1    Bess Jr., J.W.2    Crise, B.J.3    Sowder, I.R.4    Schaden, T.M.5    Hilburn, J.M.6    Hoxie, J.A.7    Benveniste, R.E.8    Lifson, J.D.9    Henderson, L.E.10    Arthur, L.O.11
  • 13
    • 0021751840 scopus 로고
    • The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus
    • A.G. Dalgleish, P.C. Beverley, P.R. Clapham, D.H. Crawford, M.F. Greaves, and R.A. Weiss The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus Nature 312 5996 1984 763 767
    • (1984) Nature , vol.312 , Issue.5996 , pp. 763-767
    • Dalgleish, A.G.1    Beverley, P.C.2    Clapham, P.R.3    Crawford, D.H.4    Greaves, M.F.5    Weiss, R.A.6
  • 15
    • 0029015314 scopus 로고
    • Analysis of the cleavage site of the human immunodeficiency virus type 1 glycoprotein: Requirement of precursor cleavage for glycoprotein incorporation
    • J.W. Dubay, S.R. Dubay, H.J. Shin, and E. Hunter Analysis of the cleavage site of the human immunodeficiency virus type 1 glycoprotein: requirement of precursor cleavage for glycoprotein incorporation J. Virol. 69 8 1995 4675 4682
    • (1995) J. Virol. , vol.69 , Issue.8 , pp. 4675-4682
    • Dubay, J.W.1    Dubay, S.R.2    Shin, H.J.3    Hunter, E.4
  • 16
    • 0035168058 scopus 로고    scopus 로고
    • Immunogenicity and protective efficacy of oligomeric human immunodeficiency virus type 1 gp140
    • P.L. Earl, W. Sugiura, D.C. Montefiori, C.C. Broder, S.A. Lee, C. Wild, J. Lifson, and B. Moss Immunogenicity and protective efficacy of oligomeric human immunodeficiency virus type 1 gp140 J. Virol. 75 2 2001 645 653
    • (2001) J. Virol. , vol.75 , Issue.2 , pp. 645-653
    • Earl, P.L.1    Sugiura, W.2    Montefiori, D.C.3    Broder, C.C.4    Lee, S.A.5    Wild, C.6    Lifson, J.7    Moss, B.8
  • 17
    • 0030897825 scopus 로고    scopus 로고
    • Neutralization of the human immunodeficiency virus type 1 primary isolate JR-FL by human monoclonal antibodies correlates with antibody binding to the oligomeric form of the envelope glycoprotein complex
    • T.R. Fouts, J.M. Binley, A. Trkola, J.E. Robinson, and J.P. Moore Neutralization of the human immunodeficiency virus type 1 primary isolate JR-FL by human monoclonal antibodies correlates with antibody binding to the oligomeric form of the envelope glycoprotein complex J. Virol. 71 4 1997 2779 2785
    • (1997) J. Virol. , vol.71 , Issue.4 , pp. 2779-2785
    • Fouts, T.R.1    Binley, J.M.2    Trkola, A.3    Robinson, J.E.4    Moore, J.P.5
  • 18
    • 1642540249 scopus 로고    scopus 로고
    • Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus
    • D.L. Gibbons, M.C. Vaney, A. Roussel, A. Vigouroux, B. Reilly, J. Lepault, M. Kielian, and F.A. Rey Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus Nature 427 6972 2004 320 325
    • (2004) Nature , vol.427 , Issue.6972 , pp. 320-325
    • Gibbons, D.L.1    Vaney, M.C.2    Roussel, A.3    Vigouroux, A.4    Reilly, B.5    Lepault, J.6    Kielian, M.7    Rey, F.A.8
  • 19
    • 0036121261 scopus 로고    scopus 로고
    • Solid-phase proteoliposomes containing human immunodeficiency virus envelope glycoproteins
    • C. Grundner, T. Mirzabekov, J. Sodroski, and R. Wyatt Solid-phase proteoliposomes containing human immunodeficiency virus envelope glycoproteins J. Virol. 76 7 2002 3511 3521
    • (2002) J. Virol. , vol.76 , Issue.7 , pp. 3511-3521
    • Grundner, C.1    Mirzabekov, T.2    Sodroski, J.3    Wyatt, R.4
  • 21
    • 0026716831 scopus 로고
    • Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160
    • S. Hallenberger, V. Bosch, H. Angliker, E. Shaw, H.D. Klenk, and W. Garten Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160 Nature 360 6402 1992 358 361
    • (1992) Nature , vol.360 , Issue.6402 , pp. 358-361
    • Hallenberger, S.1    Bosch, V.2    Angliker, H.3    Shaw, E.4    Klenk, H.D.5    Garten, W.6
  • 23
    • 0037223708 scopus 로고    scopus 로고
    • Nonneutralizing antibodies to the CD4-binding site on the gp120 subunit of human immunodeficiency virus type 1 do not interfere with the activity of a neutralizing antibody against the same site
    • C. Herrera, C. Spenlehauer, M.S. Fung, D.R. Burton, S. Beddows, and J.P. Moore Nonneutralizing antibodies to the CD4-binding site on the gp120 subunit of human immunodeficiency virus type 1 do not interfere with the activity of a neutralizing antibody against the same site J. Virol. 77 2 2003 1084 1091
    • (2003) J. Virol. , vol.77 , Issue.2 , pp. 1084-1091
    • Herrera, C.1    Spenlehauer, C.2    Fung, M.S.3    Burton, D.R.4    Beddows, S.5    Moore, J.P.6
  • 25
    • 0028774176 scopus 로고
    • Visualization of fusion activation in the Semliki Forest virus spike
    • J.M. Kenney, M. Sjoberg, H. Garoff, and S.D. Fuller Visualization of fusion activation in the Semliki Forest virus spike Structure 2 9 1994 823 832
    • (1994) Structure , vol.2 , Issue.9 , pp. 823-832
    • Kenney, J.M.1    Sjoberg, M.2    Garoff, H.3    Fuller, S.D.4
  • 27
    • 0041920924 scopus 로고    scopus 로고
    • Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition
    • M. Koch, M. Pancera, P.D. Kwong, P. Kolchinsky, C. Grundner, L. Wang, W.A. Hendrickson, J. Sodroski, and R. Wyatt Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition Virology 313 2 2003 387 400
    • (2003) Virology , vol.313 , Issue.2 , pp. 387-400
    • Koch, M.1    Pancera, M.2    Kwong, P.D.3    Kolchinsky, P.4    Grundner, C.5    Wang, L.6    Hendrickson, W.A.7    Sodroski, J.8    Wyatt, R.9
  • 28
    • 0001720445 scopus 로고    scopus 로고
    • Numbering positions in HIV relative to HXBc2
    • J. Sodroski Los Alamos National Laboratory Los Alamos, NM
    • B. Korber, F. Foley, C. Kuiken, S. Pillai, and J. Sodroski Numbering positions in HIV relative to HXBc2 J. Sodroski Human Retroviruses and AIDS 1998 Los Alamos National Laboratory Los Alamos, NM iii-102 iii-103
    • (1998) Human Retroviruses and AIDS
    • Korber, B.1    Foley, F.2    Kuiken, C.3    Pillai, S.4    Sodroski, J.5
  • 29
    • 0027205329 scopus 로고
    • Analysis of protein expression and virus-like particle formation in mammalian cell lines stably expressing HIV-1 gag and env gene products with or without active HIV proteinase
    • H.G. Krausslich, C. Ochsenbauer, A.M. Traenckner, K. Mergener, M. Facke, H.R. Gelderblom, and V. Bosch Analysis of protein expression and virus-like particle formation in mammalian cell lines stably expressing HIV-1 gag and env gene products with or without active HIV proteinase Virology 192 2 1993 605 617
    • (1993) Virology , vol.192 , Issue.2 , pp. 605-617
    • Krausslich, H.G.1    Ochsenbauer, C.2    Traenckner, A.M.3    Mergener, K.4    Facke, M.5    Gelderblom, H.R.6    Bosch, V.7
  • 30
    • 0029127787 scopus 로고
    • A single amino acid change in the cytoplasmic domain of the simian immunodeficiency virus transmembrane molecule increases envelope glycoprotein expression on infected cells
    • C.C. LaBranche, M.M. Sauter, B.S. Haggarty, P.J. Vance, J. Romano, T.K. Hart, P.J. Bugelski, M. Marsh, and J.A. Hoxie A single amino acid change in the cytoplasmic domain of the simian immunodeficiency virus transmembrane molecule increases envelope glycoprotein expression on infected cells J. Virol. 69 9 1995 5217 5227
    • (1995) J. Virol. , vol.69 , Issue.9 , pp. 5217-5227
    • Labranche, C.C.1    Sauter, M.M.2    Haggarty, B.S.3    Vance, P.J.4    Romano, J.5    Hart, T.K.6    Bugelski, P.J.7    Marsh, M.8    Hoxie, J.A.9
  • 31
    • 0036237167 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 neutralization measured by flow cytometric quantitation of single-round infection of primary human T cells
    • J.R. Mascola, M.K. Louder, C. Winter, R. Prabhakara, S.C. De Rosa, D.C. Douek, B.J. Hill, D. Gabuzda, and M. Roederer Human immunodeficiency virus type 1 neutralization measured by flow cytometric quantitation of single-round infection of primary human T cells J. Virol. 76 10 2002 4810 4821
    • (2002) J. Virol. , vol.76 , Issue.10 , pp. 4810-4821
    • Mascola, J.R.1    Louder, M.K.2    Winter, C.3    Prabhakara, R.4    De Rosa, S.C.5    Douek, D.C.6    Hill, B.J.7    Gabuzda, D.8    Roederer, M.9
  • 32
    • 0023921610 scopus 로고
    • Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus
    • J.M. McCune, L.B. Rabin, M.B. Feinberg, M. Lieberman, J.C. Kosek, G.R. Reyes, and I.L. Weissman Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus Cell 53 1 1988 55 67
    • (1988) Cell , vol.53 , Issue.1 , pp. 55-67
    • McCune, J.M.1    Rabin, L.B.2    Feinberg, M.B.3    Lieberman, M.4    Kosek, J.C.5    Reyes, G.R.6    Weissman, I.L.7
  • 33
    • 0030043169 scopus 로고    scopus 로고
    • Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein
    • J.P. Moore, and J. Sodroski Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein J. Virol. 70 3 1996 1863 1872
    • (1996) J. Virol. , vol.70 , Issue.3 , pp. 1863-1872
    • Moore, J.P.1    Sodroski, J.2
  • 34
    • 0037810998 scopus 로고    scopus 로고
    • Structure and function of a paramyxovirus fusion protein
    • T.G. Morrison Structure and function of a paramyxovirus fusion protein Biochim. Biophys. Acta 1614 1 2003 73 84
    • (2003) Biochim. Biophys. Acta , vol.1614 , Issue.1 , pp. 73-84
    • Morrison, T.G.1
  • 35
    • 0038414622 scopus 로고    scopus 로고
    • Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design
    • R. Pantophlet, I.A. Wilson, and D.R. Burton Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design J. Virol. 77 10 2003 5889 5901
    • (2003) J. Virol. , vol.77 , Issue.10 , pp. 5889-5901
    • Pantophlet, R.1    Wilson, I.A.2    Burton, D.R.3
  • 37
    • 0031969423 scopus 로고    scopus 로고
    • Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity
    • P.W. Parren, I. Mondor, D. Naniche, H.J. Ditzel, P.J. Klasse, D.R. Burton, and Q.J. Sattentau Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity J. Virol. 72 5 1998 3512 3519
    • (1998) J. Virol. , vol.72 , Issue.5 , pp. 3512-3519
    • Parren, P.W.1    Mondor, I.2    Naniche, D.3    Ditzel, H.J.4    Klasse, P.J.5    Burton, D.R.6    Sattentau, Q.J.7
  • 38
    • 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
    • P. Poignard, M. Moulard, E. Golez, V. Vivona, M. Franti, S. Venturini, M. Wang, P.W. Parren, and D.R. Burton Heterogeneity of envelope molecules expressed on primary human immunodeficiency virus type 1 particles as probed by the binding of neutralizing and nonneutralizing antibodies J. Virol. 77 1 2003 353 365
    • (2003) J. Virol. , 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.8    Burton, D.R.9
  • 39
    • 0027458347 scopus 로고
    • Neutralization of HIV-1 by F105, a human monoclonal antibody to the CD4 binding site of gp120
    • M.R. Posner, L.A. Cavacini, C.L. Emes, J. Power, and R. Byrn Neutralization of HIV-1 by F105, a human monoclonal antibody to the CD4 binding site of gp120 J. Acquired Immune. Defic. Syndr. 6 1 1993 7 14
    • (1993) J. Acquired Immune. Defic. Syndr. , vol.6 , Issue.1 , pp. 7-14
    • Posner, M.R.1    Cavacini, L.A.2    Emes, C.L.3    Power, J.4    Byrn, R.5
  • 40
    • 0028291731 scopus 로고
    • Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1
    • P. Roben, J.P. Moore, M. Thali, J. Sodroski, C.F. Barbas 3rd, and D.R. Burton Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1 J. Virol. 68 8 1994 4821 4828
    • (1994) J. Virol. , vol.68 , Issue.8 , pp. 4821-4828
    • Roben, P.1    Moore, J.P.2    Thali, M.3    Sodroski, J.4    Barbas III, C.F.5    Burton, D.R.6
  • 41
    • 0036637385 scopus 로고    scopus 로고
    • The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120
    • R.W. Sanders, M. Venturi, L. Schiffner, R. Kalyanaraman, H. Katinger, K.O. Lloyd, P.D. Kwong, and J.P. Moore The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120 J. Virol. 76 14 2002 7293 7305
    • (2002) J. Virol. , vol.76 , Issue.14 , pp. 7293-7305
    • Sanders, R.W.1    Venturi, M.2    Schiffner, L.3    Kalyanaraman, R.4    Katinger, H.5    Lloyd, K.O.6    Kwong, P.D.7    Moore, J.P.8
  • 43
    • 0028999803 scopus 로고
    • Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer
    • Q.J. Sattentau, and J.P. Moore Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer J. Exp. Med. 182 1 1995 185 196
    • (1995) J. Exp. Med. , vol.182 , Issue.1 , pp. 185-196
    • Sattentau, Q.J.1    Moore, J.P.2
  • 46
    • 0035046931 scopus 로고    scopus 로고
    • Envelope glycoprotein determinants of neutralization resistance in a simian-human immunodeficiency virus (SHIV-HXBc2P 3.2) derived by passage in monkeys
    • Z. Si, M. Cayabyab, and J. Sodroski Envelope glycoprotein determinants of neutralization resistance in a simian-human immunodeficiency virus (SHIV-HXBc2P 3.2) derived by passage in monkeys J. Virol. 75 9 2001 4208 4218
    • (2001) J. Virol. , vol.75 , Issue.9 , pp. 4208-4218
    • Si, Z.1    Cayabyab, M.2    Sodroski, J.3
  • 47
    • 0037348281 scopus 로고    scopus 로고
    • Effects of HIV type 1 envelope glycoprotein proteolytic processing on antigenicity
    • Z. Si, N. Phan, E. Kiprilov, and J. Sodroski Effects of HIV type 1 envelope glycoprotein proteolytic processing on antigenicity AIDS Res. Hum. Retroviruses 19 3 2003 217 226
    • (2003) AIDS Res. Hum. Retroviruses , vol.19 , Issue.3 , pp. 217-226
    • Si, Z.1    Phan, N.2    Kiprilov, E.3    Sodroski, J.4
  • 48
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • J.J. Skehel, and D.C. Wiley Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin Annu. Rev. Biochem. 69 2000 531 569
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 49
    • 0141788494 scopus 로고    scopus 로고
    • Purification, characterization, and immunogenicity of a soluble trimeric envelope protein containing a partial deletion of the V2 loop derived from SF162, an R5-tropic human immunodeficiency virus type 1 isolate
    • I.K. Srivastava, L. Stamatatos, E. Kan, M. Vajdy, Y. Lian, S. Hilt, L. Martin, C. Vita, P. Zhu, K.H. Roux, L. Vojtech, D.C. Montefiori, J. Donnelly, J.B. Ulmer, and S.W. Barnett Purification, characterization, and immunogenicity of a soluble trimeric envelope protein containing a partial deletion of the V2 loop derived from SF162, an R5-tropic human immunodeficiency virus type 1 isolate J. Virol. 77 20 2003 11244 11259
    • (2003) J. Virol. , vol.77 , Issue.20 , pp. 11244-11259
    • Srivastava, I.K.1    Stamatatos, L.2    Kan, E.3    Vajdy, M.4    Lian, Y.5    Hilt, S.6    Martin, L.7    Vita, C.8    Zhu, P.9    Roux, K.H.10    Vojtech, L.11    Montefiori, D.C.12    Donnelly, J.13    Ulmer, J.B.14    Barnett, S.W.15
  • 50
    • 0037321708 scopus 로고    scopus 로고
    • Changes in the immunogenic properties of soluble gp140 human immunodeficiency virus envelope constructs upon partial deletion of the second hypervariable region
    • I.K. Srivastava, K. VanDorsten, L. Vojtech, S.W. Barnett, and L. Stamatatos Changes in the immunogenic properties of soluble gp140 human immunodeficiency virus envelope constructs upon partial deletion of the second hypervariable region J. Virol. 77 4 2003 2310 2320
    • (2003) J. Virol. , vol.77 , Issue.4 , pp. 2310-2320
    • Srivastava, I.K.1    Vandorsten, K.2    Vojtech, L.3    Barnett, S.W.4    Stamatatos, L.5
  • 51
    • 0034235058 scopus 로고    scopus 로고
    • Generation and structural analysis of soluble oligomeric gp140 envelope proteins derived from neutralization-resistant and neutralization-susceptible primary HIV type 1 isolates
    • L. Stamatatos, M. Lim, and C. Cheng-Mayer Generation and structural analysis of soluble oligomeric gp140 envelope proteins derived from neutralization-resistant and neutralization-susceptible primary HIV type 1 isolates AIDS Res. Hum. Retroviruses 16 10 2000 981 994
    • (2000) AIDS Res. Hum. Retroviruses , vol.16 , Issue.10 , pp. 981-994
    • Stamatatos, L.1    Lim, M.2    Cheng-Mayer, C.3
  • 52
    • 0029020970 scopus 로고
    • Replicative function and neutralization sensitivity of envelope glycoproteins from primary and T-cell line-passaged human immunodeficiency virus type 1 isolates
    • N. Sullivan, Y. Sun, J. Li, W. Hofmann, and J. Sodroski Replicative function and neutralization sensitivity of envelope glycoproteins from primary and T-cell line-passaged human immunodeficiency virus type 1 isolates J. Virol. 69 7 1995 4413 4422
    • (1995) J. Virol. , vol.69 , Issue.7 , pp. 4413-4422
    • Sullivan, N.1    Sun, Y.2    Li, J.3    Hofmann, W.4    Sodroski, J.5
  • 53
  • 55
    • 0010296944 scopus 로고
    • Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160
    • R.L. Willey, J.S. Bonifacino, B.J. Potts, M.A. Martin, and R.D. Klausner Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160 Proc. Natl. Acad. Sci. U.S.A. 85 24 1988 9580 9584
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , Issue.24 , pp. 9580-9584
    • Willey, R.L.1    Bonifacino, J.S.2    Potts, B.J.3    Martin, M.A.4    Klausner, R.D.5
  • 57
    • 0036776445 scopus 로고    scopus 로고
    • Mutagenic stabilization and/or disruption of a CD4-bound state reveals distinct conformations of the human immunodeficiency virus type 1 gp120 envelope glycoprotein
    • S.H. Xiang, P.D. Kwong, R. Gupta, C.D. Rizzuto, D.J. Casper, R. Wyatt, L. Wang, W.A. Hendrickson, M.L. Doyle, and J. Sodroski Mutagenic stabilization and/or disruption of a CD4-bound state reveals distinct conformations of the human immunodeficiency virus type 1 gp120 envelope glycoprotein J. Virol. 76 19 2002 9888 9899
    • (2002) J. Virol. , vol.76 , Issue.19 , pp. 9888-9899
    • Xiang, S.H.1    Kwong, P.D.2    Gupta, R.3    Rizzuto, C.D.4    Casper, D.J.5    Wyatt, R.6    Wang, L.7    Hendrickson, W.A.8    Doyle, M.L.9    Sodroski, J.10
  • 58
    • 0034004321 scopus 로고    scopus 로고
    • Modifications that stabilize human immunodeficiency virus envelope glycoprotein trimers in solution
    • X. Yang, L. Florin, M. Farzan, P. Kolchinsky, P.D. Kwong, J. Sodroski, and R. Wyatt Modifications that stabilize human immunodeficiency virus envelope glycoprotein trimers in solution J. Virol. 74 10 2000 4746 4754
    • (2000) J. Virol. , vol.74 , Issue.10 , pp. 4746-4754
    • Yang, X.1    Florin, L.2    Farzan, M.3    Kolchinsky, P.4    Kwong, P.D.5    Sodroski, J.6    Wyatt, R.7
  • 59
    • 0035155850 scopus 로고    scopus 로고
    • Improved elicitation of neutralizing antibodies against primary human immunodeficiency viruses by soluble stabilized envelope glycoprotein trimers
    • X. Yang, R. Wyatt, and J. Sodroski Improved elicitation of neutralizing antibodies against primary human immunodeficiency viruses by soluble stabilized envelope glycoprotein trimers J. Virol. 75 3 2001 1165 1171
    • (2001) J. Virol. , vol.75 , Issue.3 , pp. 1165-1171
    • Yang, X.1    Wyatt, R.2    Sodroski, J.3
  • 60
    • 0036231093 scopus 로고    scopus 로고
    • Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin
    • X. Yang, J. Lee, E.M. Mahony, P.D. Kwong, R. Wyatt, and J. Sodroski Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin J. Virol. 76 9 2002 4634 4642
    • (2002) J. Virol. , vol.76 , Issue.9 , pp. 4634-4642
    • Yang, X.1    Lee, J.2    Mahony, E.M.3    Kwong, P.D.4    Wyatt, R.5    Sodroski, J.6
  • 61
    • 0035120591 scopus 로고    scopus 로고
    • Antibody binding and neutralization of primary and T-cell line-adapted isolates of human immunodeficiency virus type 1
    • J. York, K.E. Follis, M. Trahey, P.N. Nyambi, S. Zolla-Pazner, and J.H. Nunberg Antibody binding and neutralization of primary and T-cell line-adapted isolates of human immunodeficiency virus type 1 J. Virol. 75 6 2001 2741 2752
    • (2001) J. Virol. , vol.75 , Issue.6 , pp. 2741-2752
    • York, J.1    Follis, K.E.2    Trahey, M.3    Nyambi, P.N.4    Zolla-Pazner, S.5    Nunberg, J.H.6
  • 62
    • 0035955695 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant HIV gp140. The gp41 ectodomain of HIV or simian immunodeficiency virus is sufficient to maintain the retroviral envelope glycoprotein as a trimer
    • C.W. Zhang, Y. Chishti, R.E. Hussey, and E.L. Reinherz Expression, purification, and characterization of recombinant HIV gp140. The gp41 ectodomain of HIV or simian immunodeficiency virus is sufficient to maintain the retroviral envelope glycoprotein as a trimer J. Biol. Chem. 276 43 2001 39577 39585
    • (2001) J. Biol. Chem. , vol.276 , Issue.43 , pp. 39577-39585
    • Zhang, C.W.1    Chishti, Y.2    Hussey, R.E.3    Reinherz, E.L.4


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