메뉴 건너뛰기




Volumn 88, Issue 1, 2014, Pages 21-40

The selection of low envelope glycoprotein reactivity to soluble CD4 and cold during simian-human immunodeficiency virus infection of rhesus macaques

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; CHEMOKINE RECEPTOR CCR5; ENVELOPE REACTIVITY ANTIBODY; GLYCOPROTEIN GP 120; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG; VIRUS ANTIBODY; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN;

EID: 84890869444     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01558-13     Document Type: Article
Times cited : (14)

References (102)
  • 3
    • 0021833513 scopus 로고
    • Characterization of envelope and core structural gene products of HTLV-III with sera from AIDS patients
    • Robey WG, Safai B, Oroszlan S, Arthur LO, Gonda MA, Gallo RC, Fischinger PJ. 1985. Characterization of envelope and core structural gene products of HTLV-III with sera from AIDS patients. Science 228: 593-595. http://dx.doi.org/10.1126/science.2984774.
    • (1985) Science , vol.228 , pp. 593-595
    • Robey, W.G.1    Safai, B.2    Oroszlan, S.3    Arthur, L.O.4    Gonda, M.A.5    Gallo, R.C.6    Fischinger, P.J.7
  • 4
    • 0022352075 scopus 로고
    • Characterization of gp41 as the transmembrane protein coded by the HTLV-III/LAV envelope gene
    • Veronese FD, DeVico AL, Copeland TD, Oroszlan S, Gallo RC, Sarngadharan MG. 1985. Characterization of gp41 as the transmembrane protein coded by the HTLV-III/LAV envelope gene. Science 229: 1402-1405. http://dx.doi.org/10.1126/science.2994223.
    • (1985) Science , vol.229 , pp. 1402-1405
    • Veronese, F.D.1    DeVico, A.L.2    Copeland, T.D.3    Oroszlan, S.4    Gallo, R.C.5    Sarngadharan, M.G.6
  • 5
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens
    • Wyatt R, Sodroski J. 1998. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 280:1884-1888. http://dx.doi.org /10.1126/science.280.5371.1884.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 6
    • 0030018156 scopus 로고    scopus 로고
    • CC CKR5: a RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1
    • Alkhatib G, Combadiere C, Broder CC, Feng Y, Kennedy PE, Murphy PM, Berger EA. 1996. CC CKR5: a RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1. Science 272: 1955-1958. http://dx.doi.org/10.1126/science.272.5270.1955.
    • (1996) Science , vol.272 , pp. 1955-1958
    • Alkhatib, G.1    Combadiere, C.2    Broder, C.C.3    Feng, Y.4    Kennedy, P.E.5    Murphy, P.M.6    Berger, E.A.7
  • 8
    • 0021751840 scopus 로고
    • The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus
    • Dalgleish AG, Beverley PC, Clapham PR, Crawford DH, Greaves MF, Weiss RA. 1984. The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature 312:763-767. http://dx.doi.org /10.1038/312763a0.
    • (1984) Nature , vol.312 , 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
  • 11
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng Y, Broder CC, Kennedy PE, Berger EA. 1996. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 272:872-877. http://dx.doi.org/10.1126/science.272.5263 .872.
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 13
    • 51349162563 scopus 로고    scopus 로고
    • Molecular architecture of native HIV-1 gp120 trimers
    • Liu J, Bartesaghi A, Borgnia MJ, Sapiro G, Subramaniam S. 2008. Molecular architecture of native HIV-1 gp120 trimers. Nature 455:109- 113. http://dx.doi.org/10.1038/nature07159.
    • (2008) Nature , vol.455
    • Liu, J.1    Bartesaghi, A.2    Borgnia, M.J.3    Sapiro, G.4    Subramaniam, S.5
  • 15
    • 0027488547 scopus 로고
    • Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding
    • Sattentau QJ, Moore JP, Vignaux F, Traincard F, Poignard P. 1993. Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding. J. Virol. 67:7383-7393.
    • (1993) J. Virol. , vol.67 , pp. 7383-7393
    • Sattentau, Q.J.1    Moore, J.P.2    Vignaux, F.3    Traincard, F.4    Poignard, P.5
  • 16
    • 0026095929 scopus 로고
    • Effects of changes in gp120-CD4 binding affinity on human immunodeficiency virus type 1 envelope glycoprotein function and soluble CD4 sensitivity
    • Thali M, Olshevsky U, Furman C, Gabuzda D, Li J, Sodroski J. 1991. Effects of changes in gp120-CD4 binding affinity on human immunodeficiency virus type 1 envelope glycoprotein function and soluble CD4 sensitivity. J. Virol. 65:5007-5012.
    • (1991) J. Virol. , vol.65 , pp. 5007-5012
    • Thali, M.1    Olshevsky, U.2    Furman, C.3    Gabuzda, D.4    Li, J.5    Sodroski, J.6
  • 17
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert DM, Kim PS. 2001. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70:777-810. http://dx.doi.org/10 .1146/annurev.biochem.70.1.777.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 22
    • 58149487645 scopus 로고    scopus 로고
    • Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection
    • Sather DN, Armann J, Ching LK, Mavrantoni A, Sellhorn G, Caldwell Z, Yu X, Wood B, Self S, Kalams S, Stamatatos L. 2009. Factors associated with the development of cross-reactive neutralizing antibodies during human immunodeficiency virus type 1 infection. J. Virol. 83: 757-769. http://dx.doi.org/10.1128/JVI.02036-08.
    • (2009) J. Virol. , vol.83 , pp. 757-769
    • Sather, D.N.1    Armann, J.2    Ching, L.K.3    Mavrantoni, A.4    Sellhorn, G.5    Caldwell, Z.6    Yu, X.7    Wood, B.8    Self, S.9    Kalams, S.10    Stamatatos, L.11
  • 25
    • 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, Rakasz EG, Poignard P, Hangartner L, Landucci G, Forthal DN, Koff WC, Watkins DI, Burton DR. 2009. Broadly neutralizing human anti-HIV antibody 2G12 is effective in protection against mucosal SHIV challenge even at low serum neutralizing titers. PLoS Pathog. 5:e1000433. http://dx.doi.org/10.1371/journal.ppat.1000433.
    • (2009) PLoS Pathog. , vol.5
    • Hessell, A.J.1    Rakasz, E.G.2    Poignard, P.3    Hangartner, L.4    Landucci, G.5    Forthal, D.N.6    Koff, W.C.7    Watkins, D.I.8    Burton, D.R.9
  • 26
    • 73949154006 scopus 로고    scopus 로고
    • Broadly neutralizing monoclonal antibodies 2F5 and 4E10 directed against the human immunodeficiency virus type 1 gp41 membraneproximal external region protect against mucosal challenge by simianhuman immunodeficiency virus SHIVBa-L
    • Hessell AJ, Rakasz EG, Tehrani DM, Huber M, Weisgrau KL, Landucci G, Forthal DN, Koff WC, Poignard P, Watkins DI, Burton DR. 2010. Broadly neutralizing monoclonal antibodies 2F5 and 4E10 directed against the human immunodeficiency virus type 1 gp41 membraneproximal external region protect against mucosal challenge by simianhuman immunodeficiency virus SHIVBa-L. J. Virol. 84:1302-1313. http: //dx.doi.org/10.1128/JVI.01272-09.
    • (2010) J. Virol. , vol.84 , pp. 1302-1313
    • Hessell, A.J.1    Rakasz, E.G.2    Tehrani, D.M.3    Huber, M.4    Weisgrau, K.L.5    Landucci, G.6    Forthal, D.N.7    Koff, W.C.8    Poignard, P.9    Watkins, D.I.10    Burton, D.R.11
  • 29
    • 18144397438 scopus 로고    scopus 로고
    • Selection for human immunodeficiency virus type 1 envelope glycosylation variants with shorter V1-V2 loop sequences occurs during transmission of certain genetic subtypes and may impact viral RNA levels
    • Chohan B, Lang D, Sagar M, Korber B, Lavreys L, Richardson B, Overbaugh J. 2005. Selection for human immunodeficiency virus type 1 envelope glycosylation variants with shorter V1-V2 loop sequences occurs during transmission of certain genetic subtypes and may impact viral RNA levels. J. Virol. 79:6528-6531. http://dx.doi.org/10.1128/JVI .79.10.6528-6531.2005.
    • (2005) J. Virol. , vol.79 , pp. 6528-6531
    • Chohan, B.1    Lang, D.2    Sagar, M.3    Korber, B.4    Lavreys, L.5    Richardson, B.6    Overbaugh, J.7
  • 32
    • 33748925430 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity
    • Sagar M, Wu X, Lee S, Overbaugh J. 2006. Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity. J. Virol. 80:9586-9598. http://dx.doi .org/10.1128/JVI.00141-06.
    • (2006) J. Virol. , vol.80 , pp. 9586-9598
    • Sagar, M.1    Wu, X.2    Lee, S.3    Overbaugh, J.4
  • 34
    • 49149118421 scopus 로고    scopus 로고
    • Autologous neutralizing humoral immunity and evolution of the viral envelope in the course of subtype B human immunodeficiency virus type 1 infection
    • Bunnik EM, Pisas L, van Nuenen AC, Schuitemaker H. 2008. Autologous neutralizing humoral immunity and evolution of the viral envelope in the course of subtype B human immunodeficiency virus type 1 infection. J. Virol. 82:7932-7941. http://dx.doi.org/10.1128/JVI.00757-08.
    • (2008) J. Virol. , vol.82 , pp. 7932-7941
    • Bunnik, E.M.1    Pisas, L.2    van Nuenen, A.C.3    Schuitemaker, H.4
  • 35
    • 0033033625 scopus 로고    scopus 로고
    • Selection for neutralization resistance of the simian/human immunodeficiency virus SHIVSF33A variant in vivo by virtue of sequence changes in the extracellular envelope glycoprotein that modify N-linked glycosylation
    • Cheng-Mayer C, Brown A, Harouse J, Luciw PA, Mayer AJ. 1999. Selection for neutralization resistance of the simian/human immunodeficiency virus SHIVSF33A variant in vivo by virtue of sequence changes in the extracellular envelope glycoprotein that modify N-linked glycosylation. J. Virol. 73:5294-5300.
    • (1999) J. Virol. , vol.73 , pp. 5294-5300
    • Cheng-Mayer, C.1    Brown, A.2    Harouse, J.3    Luciw, P.A.4    Mayer, A.J.5
  • 37
    • 0031666748 scopus 로고    scopus 로고
    • Characterization of simianhuman immunodeficiency virus envelope glycoprotein epitopes recognized by neutralizing antibodies from infected monkeys
    • Etemad-Moghadam B, Karlsson GB, Halloran M, Sun Y, Schenten D, Fernandes M, Letvin NL, Sodroski J. 1998. Characterization of simianhuman immunodeficiency virus envelope glycoprotein epitopes recognized by neutralizing antibodies from infected monkeys. J. Virol. 72: 8437-8445.
    • (1998) J. Virol. , vol.72 , pp. 8437-8445
    • Etemad-Moghadam, B.1    Karlsson, G.B.2    Halloran, M.3    Sun, Y.4    Schenten, D.5    Fernandes, M.6    Letvin, N.L.7    Sodroski, J.8
  • 38
    • 0032849335 scopus 로고    scopus 로고
    • Determinants of neutralization resistance in the envelope glycoproteins of a simian-human immunodeficiency virus passaged in vivo
    • Etemad-Moghadam B, Sun Y, Nicholson EK, Karlsson GB, Schenten D, Sodroski J. 1999. Determinants of neutralization resistance in the envelope glycoproteins of a simian-human immunodeficiency virus passaged in vivo. J. Virol. 73:8873-8879.
    • (1999) J. Virol. , vol.73 , pp. 8873-8879
    • Etemad-Moghadam, B.1    Sun, Y.2    Nicholson, E.K.3    Karlsson, G.B.4    Schenten, D.5    Sodroski, J.6
  • 39
    • 0031901463 scopus 로고    scopus 로고
    • Neutralizing antibodies in sera from macaques infected with chimeric simianhuman immunodeficiency virus containing the envelope glycoproteins of either a laboratory-adapted variant or a primary isolate of human immunodeficiency virus type 1
    • Montefiori DC, Reimann KA, Wyand MS, Manson K, Lewis MG, Collman RG, Sodroski JG, Bolognesi DP, Letvin NL. 1998. Neutralizing antibodies in sera from macaques infected with chimeric simianhuman immunodeficiency virus containing the envelope glycoproteins of either a laboratory-adapted variant or a primary isolate of human immunodeficiency virus type 1. J. Virol. 72:3427-3431.
    • (1998) J. Virol. , vol.72 , pp. 3427-3431
    • Montefiori, D.C.1    Reimann, K.A.2    Wyand, M.S.3    Manson, K.4    Lewis, M.G.5    Collman, R.G.6    Sodroski, J.G.7    Bolognesi, D.P.8    Letvin, N.L.9
  • 41
    • 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
    • Si Z, Cayabyab M, Sodroski J. 2001. Envelope glycoprotein determinants of neutralization resistance in a simian-human immunodeficiency virus (SHIV-HXBc2P 3.2) derived by passage in monkeys. J. Virol. 75: 4208-4218. http://dx.doi.org/10.1128/JVI.75.9.4208-4218.2001.
    • (2001) J. Virol , vol.75 , pp. 4208-4218
    • Si, Z.1    Cayabyab, M.2    Sodroski, J.3
  • 42
    • 38949119472 scopus 로고    scopus 로고
    • Antibody-mediated neutralization and simian immunodeficiency virus models of HIV/AIDS
    • Sato S, Johnson W. 2007. Antibody-mediated neutralization and simian immunodeficiency virus models of HIV/AIDS. Curr. HIV Res. 5:594- 607. http://dx.doi.org/10.2174/157016207782418515.
    • (2007) Curr. HIV Res. , vol.5
    • Sato, S.1    Johnson, W.2
  • 43
    • 0344352497 scopus 로고    scopus 로고
    • Mucosal transmission of pathogenic CXCR4- utilizing SHIVSF33A variants in rhesus macaques
    • Harouse JM, Tan RC, Gettie A, Dailey P, Marx PA, Luciw PA, Cheng-Mayer C. 1998. Mucosal transmission of pathogenic CXCR4- utilizing SHIVSF33A variants in rhesus macaques. Virology 248:95-107. http://dx.doi.org/10.1006/viro.1998.9236.
    • (1998) Virology , vol.248 , pp. 95-107
    • Harouse, J.M.1    Tan, R.C.2    Gettie, A.3    Dailey, P.4    Marx, P.A.5    Luciw, P.A.6    Cheng-Mayer, C.7
  • 46
    • 0038163800 scopus 로고    scopus 로고
    • Characterization of a simian human immunodeficiency virus encoding the envelope gene from the CCR5-tropic HIV-1 Ba-L
    • Pal R, Taylor B, Foulke JS, Woodward R, Merges M, Praschunus R, Gibson A, Reitz M. 2003. Characterization of a simian human immunodeficiency virus encoding the envelope gene from the CCR5-tropic HIV-1 Ba-L. J. Acquir. Immune Defic. Syndr. 33:300-307. http://dx.doi .org/10.1097/00126334-200307010-00003.
    • (2003) J. Acquir. Immune Defic. Syndr. , vol.33 , pp. 300-307
    • Pal, R.1    Taylor, B.2    Foulke, J.S.3    Woodward, R.4    Merges, M.5    Praschunus, R.6    Gibson, A.7    Reitz, M.8
  • 48
    • 0033176826 scopus 로고    scopus 로고
    • In vivo adaptation of SHIV(SF162): chimeric virus expressing a NSI, CCR5-specific envelope protein
    • Tan RC, Harouse JM, Gettie A, Cheng-Mayer C. 1999. In vivo adaptation of SHIV(SF162): chimeric virus expressing a NSI, CCR5-specific envelope protein. J. Med. Primatol. 28:164-168. http://dx.doi.org/10 .1111/j.1600-0684.1999.tb00265.x.
    • (1999) J. Med. Primatol. , vol.28 , pp. 164-168
    • Tan, R.C.1    Harouse, J.M.2    Gettie, A.3    Cheng-Mayer, C.4
  • 49
    • 0031575431 scopus 로고    scopus 로고
    • Change in coreceptor use correlates with disease progression in HIV-1-infected individuals
    • Connor RI, Sheridan KE, Ceradini D, Choe S, Landau NR. 1997. Change in coreceptor use correlates with disease progression in HIV-1-infected individuals. J. Exp. Med. 185:621-628. http://dx.doi.org/10 .1084/jem.185.4.621.
    • (1997) J. Exp. Med. , vol.185 , pp. 621-628
    • Connor, R.I.1    Sheridan, K.E.2    Ceradini, D.3    Choe, S.4    Landau, N.R.5
  • 50
    • 0028076036 scopus 로고
    • MT-2 cell tropism of human immunodeficiency virus type 1 isolates as a marker for response to treatment and development of drugresistance
    • Karlsson A, Parsmyr K, Aperia K, Sandstrom E, Fenyo EM, Albert J. 1994. MT-2 cell tropism of human immunodeficiency virus type 1 isolates as a marker for response to treatment and development of drugresistance. J. Infect. Dis. 170:1367-1375. http://dx.doi.org/10.1093 /infdis/170.6.1367.
    • (1994) J. Infect. Dis. , vol.170 , pp. 1367-1375
    • Karlsson, A.1    Parsmyr, K.2    Aperia, K.3    Sandstrom, E.4    Fenyo, E.M.5    Albert, J.6
  • 51
    • 0026070668 scopus 로고
    • Monocytotropic human immunodeficiency virus type 1 (HIV-1) variants detectable in all stages of HIV-1 infection lack T-cell line tropism and syncytium-inducing ability in primary T-cell culture
    • Schuitemaker H, Kootstra NA, de Goede RE, de Wolf F, Miedema F, Tersmette M. 1991. Monocytotropic human immunodeficiency virus type 1 (HIV-1) variants detectable in all stages of HIV-1 infection lack T-cell line tropism and syncytium-inducing ability in primary T-cell culture. J. Virol. 65:356-363.
    • (1991) J. Virol. , vol.65 , pp. 356-363
    • Schuitemaker, H.1    Kootstra, N.A.2    de Goede, R.E.3    de Wolf, F.4    Miedema, F.5    Tersmette, M.6
  • 55
    • 0029794529 scopus 로고    scopus 로고
    • A chimeric simian/human immunodeficiency virus expressing a primary patient human immunodeficiency virus type 1 isolate env causes an AIDS-like disease after in vivo passage in rhesus monkeys
    • Reimann KA, Li JT, Veazey R, Halloran M, Park IW, Karlsson GB, Sodroski J, Letvin NL. 1996. A chimeric simian/human immunodeficiency virus expressing a primary patient human immunodeficiency virus type 1 isolate env causes an AIDS-like disease after in vivo passage in rhesus monkeys. J. Virol. 70:6922-6928.
    • (1996) J. Virol. , vol.70 , pp. 6922-6928
    • Reimann, K.A.1    Li, J.T.2    Veazey, R.3    Halloran, M.4    Park, I.W.5    Karlsson, G.B.6    Sodroski, J.7    Letvin, N.L.8
  • 62
    • 66149136375 scopus 로고    scopus 로고
    • Identification of a human immunodeficiency virus type 1 envelope glycoprotein variant resistant to cold inactivation
    • Kassa A, Finzi A, Pancera M, Courter JR, Smith AB, III, Sodroski J. 2009. Identification of a human immunodeficiency virus type 1 envelope glycoprotein variant resistant to cold inactivation. J. Virol. 83:4476-4488. http://dx.doi.org/10.1128/JVI.02110-08.
    • (2009) J. Virol. , vol.83 , pp. 4476-4488
    • Kassa, A.1    Finzi, A.2    Pancera, M.3    Courter, J.R.4    Smith, A.B.5    Sodroski, J.6
  • 65
    • 84875516588 scopus 로고    scopus 로고
    • The HIV-1 gp120 major variable regions modulate cold inactivation
    • Medjahed H, Pacheco B, Desormeaux A, Sodroski J, Finzi A. 2013. The HIV-1 gp120 major variable regions modulate cold inactivation. J. Virol. 87:4103-4111. http://dx.doi.org/10.1128/JVI.03124-12.
    • (2013) J. Virol. , vol.87 , pp. 4103-4111
    • Medjahed, H.1    Pacheco, B.2    Desormeaux, A.3    Sodroski, J.4    Finzi, A.5
  • 66
    • 0038619031 scopus 로고    scopus 로고
    • Cytolysis by CCR5-using human immunodeficiency virus type 1 envelope glycoproteins is dependent on membrane fusion and can be inhibited by high levels of CD4 expression
    • LaBonte JA, Madani N, Sodroski J. 2003. Cytolysis by CCR5-using human immunodeficiency virus type 1 envelope glycoproteins is dependent on membrane fusion and can be inhibited by high levels of CD4 expression. J. Virol. 77:6645-6659. http://dx.doi.org/10.1128/JVI.77.12 .6645-6659.2003.
    • (2003) J. Virol. , vol.77 , pp. 6645-6659
    • LaBonte, J.A.1    Madani, N.2    Sodroski, J.3
  • 67
    • 0344766077 scopus 로고    scopus 로고
    • Primary human immunodeficiency virus type 2 (HIV-2) isolates, like HIV-1 isolates, frequently use CCR5 but show promiscuity in coreceptor usage
    • Morner A, Bjorndal A, Albert J, Kewalramani VN, Littman DR, Inoue R, Thorstensson R, Fenyo EM, Bjorling E. 1999. Primary human immunodeficiency virus type 2 (HIV-2) isolates, like HIV-1 isolates, frequently use CCR5 but show promiscuity in coreceptor usage. J. Virol. 73:2343-2349.
    • (1999) J. Virol. , vol.73 , pp. 2343-2349
    • Morner, A.1    Bjorndal, A.2    Albert, J.3    Kewalramani, V.N.4    Littman, D.R.5    Inoue, R.6    Thorstensson, R.7    Fenyo, E.M.8    Bjorling, E.9
  • 70
    • 0028291731 scopus 로고
    • Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1
    • Roben P, Moore JP, Thali M, Sodroski J, Barbas CF, III, Burton DR. 1994. Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1. J. Virol. 68:4821-4828.
    • (1994) J. Virol. , vol.68 , pp. 4821-4828
    • Roben, P.1    Moore, J.P.2    Thali, M.3    Sodroski, J.4    Barbas, C.F.5    Burton, D.R.6
  • 71
    • 0026001658 scopus 로고
    • An IgG human monoclonal antibody that reacts with HIV-1/ GP120, inhibits virus binding to cells, and neutralizes infection
    • Posner MR, Hideshima T, Cannon T, Mukherjee M, Mayer KH, Byrn RA. 1991. An IgG human monoclonal antibody that reacts with HIV-1/ GP120, inhibits virus binding to cells, and neutralizes infection. J. Immunol. 146:4325-4332.
    • (1991) J. Immunol. , vol.146 , pp. 4325-4332
    • Posner, M.R.1    Hideshima, T.2    Cannon, T.3    Mukherjee, M.4    Mayer, K.H.5    Byrn, R.A.6
  • 73
    • 0027256814 scopus 로고
    • Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali M, Moore JP, Furman C, Charles M, Ho DD, Robinson J, Sodroski J. 1993. Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol. 67:3978-3988.
    • (1993) J. Virol. , vol.67 , pp. 3978-3988
    • Thali, M.1    Moore, J.P.2    Furman, C.3    Charles, M.4    Ho, D.D.5    Robinson, J.6    Sodroski, J.7
  • 76
    • 8644270507 scopus 로고    scopus 로고
    • Characterization of the outer domain of the gp120 glycoprotein from human immunodeficiency virus type 1
    • Yang X, Tomov V, Kurteva S, Wang L, Ren X, Gorny MK, Zolla-Pazner S, Sodroski J. 2004. Characterization of the outer domain of the gp120 glycoprotein from human immunodeficiency virus type 1. J. Virol. 78: 12975-12986. doi:http://dx.doi.org/10.1128/JVI.78.23.12975-12986.2004.
    • (2004) J. Virol. , vol.78 , pp. 12975-12986
    • Yang, X.1    Tomov, V.2    Kurteva, S.3    Wang, L.4    Ren, X.5    Gorny, M.K.6    Zolla-Pazner, S.7    Sodroski, J.8
  • 78
    • 77957198704 scopus 로고    scopus 로고
    • Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16
    • Doores KJ, Burton DR. 2010. Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16. J. Virol. 84:10510-10521. http://dx.doi.org/10.1128/JVI.00552-10.
    • (2010) J. Virol. , vol.84 , pp. 10510-10521
    • Doores, K.J.1    Burton, D.R.2
  • 79
    • 0035012787 scopus 로고    scopus 로고
    • Membrane-fusing capacity of the human immunodeficiency virus envelope proteins determines the efficiency of CD+ T-cell depletion in macaques infected by a simian-human immunodeficiency virus
    • Etemad-Moghadam B, Rhone D, Steenbeke T, Sun Y, Manola J,Gelman R, Fanton JW, Racz P, Tenner-Racz K, Axthelm MK, Letvin NL, Sodroski J. 2001. Membrane-fusing capacity of the human immunodeficiency virus envelope proteins determines the efficiency of CD+ T-cell depletion in macaques infected by a simian-human immunodeficiency virus. J. Virol. 75:5646-5655. http://dx.doi.org/10.1128/JVI.75.12 .5646-5655.2001.
    • (2001) J. Virol. , vol.75 , pp. 5646-5655
    • Etemad-Moghadam, B.1    Rhone, D.2    Steenbeke, T.3    Sun, Y.4    Manola, J.5    Gelman, R.6    Fanton, J.W.7    Racz, P.8    Tenner-Racz, K.9    Axthelm, M.K.10    Letvin, N.L.11    Sodroski, J.12
  • 80
    • 79551518897 scopus 로고    scopus 로고
    • Characteristics of the earliest cross-neutralizing antibody response to HIV-1
    • Mikell I, Sather DN, Kalams SA, Altfeld M, Alter G, Stamatatos L. 2011. Characteristics of the earliest cross-neutralizing antibody response to HIV-1. PLoS Pathog. 7:e1001251. http://dx.doi.org/10.1371/journal .ppat.1001251.
    • (2011) PLoS Pathog. , vol.7
    • Mikell, I.1    Sather, D.N.2    Kalams, S.A.3    Altfeld, M.4    Alter, G.5    Stamatatos, L.6
  • 83
    • 30344476119 scopus 로고    scopus 로고
    • Consistent patterns of change during the divergence of human immunodeficiency virus type 1 envelope from that of the inoculated virus in simian/human immunodeficiency virus-infected macaques
    • Blay WM, Gnanakaran S, Foley B, Doria-Rose NA, Korber BT, Haigwood NL. 2006. Consistent patterns of change during the divergence of human immunodeficiency virus type 1 envelope from that of the inoculated virus in simian/human immunodeficiency virus-infected macaques. J. Virol. 80:999-1014. http://dx.doi.org/10.1128/JVI.80.2.999 -1014.2006.
    • (2006) J. Virol. , vol.80 , pp. 999-1014
    • Blay, W.M.1    Gnanakaran, S.2    Foley, B.3    Doria-Rose, N.A.4    Korber, B.T.5    Haigwood, N.L.6
  • 84
    • 0025267919 scopus 로고
    • Rapid development of isolate-specific neutralizing antibodies after primary HIV-1 infection and consequent emergence of virus variants which resist neutralization by autologous sera
    • Albert J, Abrahamsson B, Nagy K, Aurelius E, Gaines H, Nystrom G, Fenyo EM. 1990. Rapid development of isolate-specific neutralizing antibodies after primary HIV-1 infection and consequent emergence of virus variants which resist neutralization by autologous sera. AIDS 4:107-112. http://dx.doi.org/10.1097/00002030-199002000-00002.
    • (1990) AIDS , vol.4 , pp. 107-112
    • Albert, J.1    Abrahamsson, B.2    Nagy, K.3    Aurelius, E.4    Gaines, H.5    Nystrom, G.6    Fenyo, E.M.7
  • 85
    • 0026544650 scopus 로고
    • Autologous HIV-1 neutralizing antibodies: emergence of neutralization-resistant escape virus and subsequent development of escape virus neutralizing antibodies
    • Arendrup M, Nielsen C, Hansen JE, Pedersen C, Mathiesen L, Nielsen JO. 1992. Autologous HIV-1 neutralizing antibodies: emergence of neutralization-resistant escape virus and subsequent development of escape virus neutralizing antibodies. J. Acquir. Immune Defic. Syndr. 5:303-307.
    • (1992) J. Acquir. Immune Defic. Syndr. , vol.5 , pp. 303-307
    • Arendrup, M.1    Nielsen, C.2    Hansen, J.E.3    Pedersen, C.4    Mathiesen, L.5    Nielsen, J.O.6
  • 86
    • 69549126129 scopus 로고    scopus 로고
    • Specificity of the autologous neutralizing antibody response
    • Moore PL, Gray ES, Morris L. 2009. Specificity of the autologous neutralizing antibody response. Curr. Opin. HIV AIDS 4:358-363. http: //dx.doi.org/10.1097/COH.0b013e32832ea7e8.
    • (2009) Curr. Opin. HIV AIDS , vol.4 , pp. 358-363
    • Moore, P.L.1    Gray, E.S.2    Morris, L.3
  • 88
    • 0037389643 scopus 로고    scopus 로고
    • Rapid evolution of the neutralizing antibody response to HIV type 1 infection
    • Richman DD, Wrin T, Little SJ, Petropoulos CJ. 2003. Rapid evolution of the neutralizing antibody response to HIV type 1 infection. Proc. Natl. Acad. Sci. U. S. A. 100:4144 -4149. http://dx.doi.org /10.1073/pnas.0630530100.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100
    • Richman, D.D.1    Wrin, T.2    Little, S.J.3    Petropoulos, C.J.4
  • 92
    • 74249089192 scopus 로고    scopus 로고
    • Escape from autologous humoral immunity of HIV-1 is not associated with a decrease in replicative capacity
    • Bunnik EM, Lobbrecht MS, van Nuenen AC, Schuitemaker H. 2010. Escape from autologous humoral immunity of HIV-1 is not associated with a decrease in replicative capacity. Virology 397:224-230. http://dx .doi.org/10.1016/j.virol.2009.11.009.
    • (2010) Virology , vol.397 , pp. 224-230
    • Bunnik, E.M.1    Lobbrecht, M.S.2    van Nuenen, A.C.3    Schuitemaker, H.4
  • 97
    • 0030744820 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 mutants that escape neutralization by human monoclonal antibody IgG1b12
    • Mo H, Stamatatos L, Ip JE, Barbas CF, Parren PW, Burton DR, Moore JP, Ho DD. 1997. Human immunodeficiency virus type 1 mutants that escape neutralization by human monoclonal antibody IgG1b12. J. Virol. 71:6869-6874.
    • (1997) J. Virol. , vol.71 , pp. 6869-6874
    • Mo, H.1    Stamatatos, L.2    Ip, J.E.3    Barbas, C.F.4    Parren, P.W.5    Burton, D.R.6    Moore, J.P.7    Ho, D.D.8
  • 98
    • 77950816445 scopus 로고    scopus 로고
    • Two N-linked glycosylation sites in the V2 and C2 regions of human immunodeficiency virus type 1 CRF01_AE envelope glycoprotein gp120 regulate viral neutralization susceptibility to the human monoclonal antibody specific for the CD4 binding domain
    • Utachee P, Nakamura S, Isarangkura-Na-Ayuthaya P, Tokunaga K, Sawanpanyalert P, Ikuta K, Auwanit W, Kameoka M. 2010. Two N-linked glycosylation sites in the V2 and C2 regions of human immunodeficiency virus type 1 CRF01_AE envelope glycoprotein gp120 regulate viral neutralization susceptibility to the human monoclonal antibody specific for the CD4 binding domain. J. Virol. 84:4311-4320. http: //dx.doi.org/10.1128/JVI.02619-09.
    • (2010) J. Virol. , vol.84 , pp. 4311-4320
    • Utachee, P.1    Nakamura, S.2    Isarangkura-Na-Ayuthaya, P.3    Tokunaga, K.4    Sawanpanyalert, P.5    Ikuta, K.6    Auwanit, W.7    Kameoka, M.8
  • 99
    • 81255167375 scopus 로고    scopus 로고
    • Efficiency of neutralizing antibodies targeting the CD4-binding site: influence of conformational masking by the V2 loop in R5-tropic clade C simian-human immunodeficiency virus
    • Watkins JD, Diaz-Rodriguez J, Siddappa NB, Corti D, Ruprecht RM. 2011. Efficiency of neutralizing antibodies targeting the CD4-binding site: influence of conformational masking by the V2 loop in R5-tropic clade C simian-human immunodeficiency virus. J. Virol. 85:12811-12814. http://dx.doi.org/10.1128/JVI.05994-11.
    • (2011) J. Virol. , vol.85 , pp. 12811-12814
    • Watkins, J.D.1    Diaz-Rodriguez, J.2    Siddappa, N.B.3    Corti, D.4    Ruprecht, R.M.5
  • 100
    • 79960093929 scopus 로고    scopus 로고
    • Adoption of an "open" envelope conformation facilitating CD4 binding and structural remodeling precedes coreceptor switch in R5 SHIV-infected macaques
    • Zhuang K, Finzi A, Tasca S, Shakirzyanova M, Knight H, Westmoreland S, Sodroski J, Cheng-Mayer C. 2011. Adoption of an "open" envelope conformation facilitating CD4 binding and structural remodeling precedes coreceptor switch in R5 SHIV-infected macaques. PLoS One 6:e21350. http://dx.doi.org/10.1371/journal.pone.0021350.
    • (2011) PLoS One , vol.6
    • Zhuang, K.1    Finzi, A.2    Tasca, S.3    Shakirzyanova, M.4    Knight, H.5    Westmoreland, S.6    Sodroski, J.7    Cheng-Mayer, C.8
  • 101
    • 84870897823 scopus 로고    scopus 로고
    • Identification of interdependent variables that influence coreceptor switch in R5 SHIVSF162P3N-infected macaques
    • Zhuang K, Finzi A, Toma J, Frantzell A, Huang W, Sodroski J, Cheng-Mayer C. 2012. Identification of interdependent variables that influence coreceptor switch in R5 SHIVSF162P3N-infected macaques. Retrovirology 9:106. http://dx.doi.org/10.1186/1742-4690-9-106.
    • (2012) Retrovirology , vol.9 , pp. 106
    • Zhuang, K.1    Finzi, A.2    Toma, J.3    Frantzell, A.4    Huang, W.5    Sodroski, J.6    Cheng-Mayer, C.7
  • 102
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0
    • Guindon S, Dufayard JF, Lefort V, Anisimova M, Hordijk W, Gascuel O. 2010. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst. Biol. 59:307-321. http://dx.doi.org/10.1093/sysbio/syq010.
    • (2010) Syst. Biol. , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.