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Volumn 90, Issue 2, 2016, Pages 829-841

Conserved role of an N-linked glycan on the surface antigen of human immunodeficiency virus type 1 modulating virus sensitivity to broadly neutralizing antibodies against the receptor and coreceptor binding sites

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIBODY; EPITOPE; GLYCAN; GLYCOPROTEIN GP 120; MEMBRANE ANTIGEN; MONOCLONAL ANTIBODY; N7 GLYCAN; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG; GP120 PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; HUMAN IMMUNODEFICIENCY VIRUS ANTIGEN; POLYSACCHARIDE;

EID: 84954101840     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02321-15     Document Type: Article
Times cited : (21)

References (102)
  • 1
    • 84860492563 scopus 로고    scopus 로고
    • VRC01 provides sterilizing protection to non human primates from mucosal SHIV challenges
    • Pegu AYZ, Chen X, Todd JP, McKee K, Rao S, Mascola J, Nabel G. 2011. VRC01 provides sterilizing protection to non human primates from mucosal SHIV challenges. J Immunol 186:11.
    • (2011) J Immunol , vol.186 , pp. 11
    • Pegu, A.Y.Z.1    Chen, X.2    Todd, J.P.3    McKee, K.4    Rao, S.5    Mascola, J.6    Nabel, G.7
  • 2
    • 64949118709 scopus 로고    scopus 로고
    • Passive immunization with human neutralizing monoclonal antibodies against HIV-1 in macaque models: experimental approaches
    • Ruprecht RM. 2009. Passive immunization with human neutralizing monoclonal antibodies against HIV-1 in macaque models: experimental approaches. Methods Mol Biol 525:559-566, xiv. http://dx.doi.org/10.1007/978-1-59745-554-1_31.
    • (2009) Methods Mol Biol , vol.525
    • Ruprecht, R.M.1
  • 3
    • 0037708018 scopus 로고    scopus 로고
    • Antibody protection: passive immunization of neonates against oral AIDS virus challenge
    • Ruprecht RM, Ferrantelli F, Kitabwalla M, Xu W, McClure HM. 2003. Antibody protection: passive immunization of neonates against oral AIDS virus challenge. Vaccine 21:3370-3373. http://dx.doi.org/10.1016/S0264-410X(03)00335-9.
    • (2003) Vaccine , vol.21 , pp. 3370-3373
    • Ruprecht, R.M.1    Ferrantelli, F.2    Kitabwalla, M.3    Xu, W.4    McClure, H.M.5
  • 5
    • 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
  • 6
    • 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. 2012. Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses. Science 337:183-186. http://dx.doi.org/10.1126/science.1225416.
    • (2012) Science , vol.337 , pp. 183-186
    • Burton, D.R.1    Poignard, P.2    Stanfield, R.L.3    Wilson, I.A.4
  • 7
    • 84866495323 scopus 로고    scopus 로고
    • Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies
    • Kwong PD, Mascola JR. 2012. Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies. Immunity 37:412-425. http://dx.doi.org/10.1016/j.immuni.2012.08.012.
    • (2012) Immunity , vol.37 , pp. 412-425
    • Kwong, P.D.1    Mascola, J.R.2
  • 8
    • 84862732215 scopus 로고    scopus 로고
    • The design and evaluation of HIV-1 vaccines
    • Saunders KO, Rudicell RS, Nabel GJ. 2012. The design and evaluation of HIV-1 vaccines. AIDS 26:1293-1302. http://dx.doi.org/10.1097/QAD.0b013e32835474d2.
    • (2012) AIDS , vol.26 , pp. 1293-1302
    • Saunders, K.O.1    Rudicell, R.S.2    Nabel, G.J.3
  • 9
    • 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. 2012. B-cell-lineage immunogen design in vaccine development with HIV-1 as a case study. Nat Biotechnol 30:423-433. http://dx.doi.org/10.1038/nbt.2197.
    • (2012) Nat Biotechnol , vol.30 , pp. 423-433
    • Haynes, B.F.1    Kelsoe, G.2    Harrison, S.C.3    Kepler, T.B.4
  • 10
    • 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
  • 11
    • 77952311370 scopus 로고    scopus 로고
    • The role of antibodies in HIV vaccines
    • Mascola JR, Montefiori DC. 2010. The role of antibodies in HIV vaccines. Annu Rev Immunol 28:413-444. http://dx.doi.org/10.1146/annurev-immunol-030409-101256.
    • (2010) Annu Rev Immunol , vol.28 , pp. 413-444
    • Mascola, J.R.1    Montefiori, D.C.2
  • 14
    • 0026671622 scopus 로고
    • Alterations in potential sites for glycosylation predominate during evolution of the simian immunodeficiency virus envelope gene in macaques
    • Overbaugh J, Rudensey LM. 1992. Alterations in potential sites for glycosylation predominate during evolution of the simian immunodeficiency virus envelope gene in macaques. J Virol 66:5937-5948.
    • (1992) J Virol , vol.66 , pp. 5937-5948
    • Overbaugh, J.1    Rudensey, L.M.2
  • 17
    • 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
  • 18
    • 0031749469 scopus 로고    scopus 로고
    • A role for carbohydrates in immune evasion in AIDS
    • Reitter JN, Means RE, Desrosiers RC. 1998. A role for carbohydrates in immune evasion in AIDS. Nat Med 4:679-684. http://dx.doi.org/10.1038/nm0698-679.
    • (1998) Nat Med , vol.4 , pp. 679-684
    • Reitter, J.N.1    Means, R.E.2    Desrosiers, R.C.3
  • 19
    • 9744280420 scopus 로고    scopus 로고
    • Tracking global patterns of N-linked glycosylation site variation in highly variable viral glycoproteins: HIV, SIV, and HCV envelopes and influenza hemagglutinin
    • Zhang M, Gaschen B, Blay W, Foley B, Haigwood N, Kuiken C, Korber B. 2004. Tracking global patterns of N-linked glycosylation site variation in highly variable viral glycoproteins: HIV, SIV, and HCV envelopes and influenza hemagglutinin. Glycobiology 14:1229-1246. http://dx.doi.org/10.1093/glycob/cwh106.
    • (2004) Glycobiology , vol.14 , pp. 1229-1246
    • Zhang, M.1    Gaschen, B.2    Blay, W.3    Foley, B.4    Haigwood, N.5    Kuiken, C.6    Korber, B.7
  • 21
    • 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, Cleveland B, Klots I, Travis B, Richardson BA, Anderson D, Montefiori D, Polacino P, Hu SL. 2008. 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 82: 638-651. http://dx.doi.org/10.1128/JVI.01691-07.
    • (2008) J Virol , vol.82 , pp. 638-651
    • Li, Y.1    Cleveland, B.2    Klots, I.3    Travis, B.4    Richardson, B.A.5    Anderson, D.6    Montefiori, D.7    Polacino, P.8    Hu, S.L.9
  • 22
    • 0035100868 scopus 로고    scopus 로고
    • Loss of a single N-linked glycan allows CD4-independent human immunodeficiency virus type 1 infection by altering the position of the gp120 V1/V2 variable loops
    • Kolchinsky P, Kiprilov E, Bartley P, Rubinstein R, Sodroski J. 2001. Loss of a single N-linked glycan allows CD4-independent human immunodeficiency virus type 1 infection by altering the position of the gp120 V1/V2 variable loops. J Virol 75:3435-3443. http://dx.doi.org/10.1128/JVI.75.7.3435-3443.2001.
    • (2001) J Virol , vol.75 , pp. 3435-3443
    • Kolchinsky, P.1    Kiprilov, E.2    Bartley, P.3    Rubinstein, R.4    Sodroski, J.5
  • 23
    • 84855343161 scopus 로고    scopus 로고
    • Highly conserved HIV-1 gp120 glycans proximal to CD4-binding region affect viral infectivity and neutralizing antibody induction
    • Huang X, Jin W, Hu K, Luo S, Du T, Griffin GE, Shattock RJ, Hu Q. 2012. Highly conserved HIV-1 gp120 glycans proximal to CD4-binding region affect viral infectivity and neutralizing antibody induction. Virology 423:97-106. http://dx.doi.org/10.1016/j.virol.2011.11.023.
    • (2012) Virology , vol.423 , pp. 97-106
    • Huang, X.1    Jin, W.2    Hu, K.3    Luo, S.4    Du, T.5    Griffin, G.E.6    Shattock, R.J.7    Hu, Q.8
  • 24
    • 25144519185 scopus 로고    scopus 로고
    • Identification of two Nlinked glycosylation sites within the core of the simian immunodeficiency virus glycoprotein whose removal enhances sensitivity to soluble CD4
    • Pikora C, Wittish C, Desrosiers RC. 2005. Identification of two Nlinked glycosylation sites within the core of the simian immunodeficiency virus glycoprotein whose removal enhances sensitivity to soluble CD4. J Virol 79:12575-12583. http://dx.doi.org/10.1128/JVI.79.19.12575-12583.2005.
    • (2005) J Virol , vol.79 , pp. 12575-12583
    • Pikora, C.1    Wittish, C.2    Desrosiers, R.C.3
  • 25
    • 75849146082 scopus 로고    scopus 로고
    • Temporal analysis of HIV envelope sequence evolution and antibody escape in a subtype A-infected individual with a broad neutralizing antibody response
    • Bosch KA, Rainwater S, Jaoko W, Overbaugh J. 2010. Temporal analysis of HIV envelope sequence evolution and antibody escape in a subtype A-infected individual with a broad neutralizing antibody response. Virology 398:115-124. http://dx.doi.org/10.1016/j.virol.2009.11.032.
    • (2010) Virology , vol.398 , pp. 115-124
    • Bosch, K.A.1    Rainwater, S.2    Jaoko, W.3    Overbaugh, J.4
  • 28
    • 2942687021 scopus 로고    scopus 로고
    • Biological analysis of human immunodeficiency virus type 1 R5 envelopes amplified from brain and lymph node tissues of AIDS patients with neuropathology reveals two distinct tropism phenotypes and identifies envelopes in the brain that confer an enhanced tropism and fusigenicity for macrophages
    • Peters PJ, Bhattacharya J, Hibbitts S, Dittmar MT, Simmons G, Bell J, Simmonds P, Clapham PR. 2004. Biological analysis of human immunodeficiency virus type 1 R5 envelopes amplified from brain and lymph node tissues of AIDS patients with neuropathology reveals two distinct tropism phenotypes and identifies envelopes in the brain that confer an enhanced tropism and fusigenicity for macrophages. J Virol 78:6915-6926. http://dx.doi.org/10.1128/JVI.78.13.6915-6926.2004.
    • (2004) J Virol , vol.78 , pp. 6915-6926
    • Peters, P.J.1    Bhattacharya, J.2    Hibbitts, S.3    Dittmar, M.T.4    Simmons, G.5    Bell, J.6    Simmonds, P.7    Clapham, P.R.8
  • 29
    • 0023214674 scopus 로고
    • Dual infection of the central nervous system by AIDS viruses with distinct cellular tropisms
    • Koyanagi Y, Miles S, Mitsuyasu RT, Merrill JE, Vinters HV, Chen IS. 1987. Dual infection of the central nervous system by AIDS viruses with distinct cellular tropisms. Science 236:819-822. http://dx.doi.org/10.1126/science.3646751.
    • (1987) Science , vol.236 , pp. 819-822
    • Koyanagi, Y.1    Miles, S.2    Mitsuyasu, R.T.3    Merrill, J.E.4    Vinters, H.V.5    Chen, I.S.6
  • 30
    • 0031025113 scopus 로고    scopus 로고
    • Macrophage tropism of human immunodeficiency virus type 1 and utilization of the CC-CKR5 coreceptor
    • Cheng-Mayer C, Liu R, Landau NR, Stamatatos L. 1997. Macrophage tropism of human immunodeficiency virus type 1 and utilization of the CC-CKR5 coreceptor. J Virol 71:1657-1661.
    • (1997) J Virol , vol.71 , pp. 1657-1661
    • Cheng-Mayer, C.1    Liu, R.2    Landau, N.R.3    Stamatatos, L.4
  • 31
    • 10044223604 scopus 로고    scopus 로고
    • Infectious molecular clone of a recently transmitted pediatric human immunodeficiency virus clade C isolate from Africa: evidence of intraclade recombination
    • Grisson RD, Chenine AL, Yeh LY, He J, Wood C, Bhat GJ, Xu W, Kankasa C, Ruprecht RM. 2004. Infectious molecular clone of a recently transmitted pediatric human immunodeficiency virus clade C isolate from Africa: evidence of intraclade recombination. J Virol 78:14066-14069. http://dx.doi.org/10.1128/JVI.78.24.14066-14069.2004.
    • (2004) J Virol , vol.78 , pp. 14066-14069
    • Grisson, R.D.1    Chenine, A.L.2    Yeh, L.Y.3    He, J.4    Wood, C.5    Bhat, G.J.6    Xu, W.7    Kankasa, C.8    Ruprecht, R.M.9
  • 34
    • 0035701421 scopus 로고    scopus 로고
    • A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1
    • Stiegler G, Kunert R, Purtscher M, Wolbank S, Voglauer R, Steindl F, Katinger H. 2001. A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1. AIDS Res Hum Retroviruses 17:1757-1765. http://dx.doi.org/10.1089/08892220152741450.
    • (2001) AIDS Res Hum Retroviruses , vol.17 , pp. 1757-1765
    • Stiegler, G.1    Kunert, R.2    Purtscher, M.3    Wolbank, S.4    Voglauer, R.5    Steindl, F.6    Katinger, H.7
  • 38
    • 0025838698 scopus 로고
    • A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals
    • Burton DR, Barbas CF, III, Persson MA, Koenig S, Chanock RM, Lerner RA. 1991. A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals. Proc Natl Acad Sci U S A 88: 10134-10137. http://dx.doi.org/10.1073/pnas.88.22.10134.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 10134-10137
    • Burton, D.R.1    Barbas, C.F.2    Persson, M.A.3    Koenig, S.4    Chanock, R.M.5    Lerner, R.A.6
  • 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
    • 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
  • 41
    • 0028815001 scopus 로고
    • Enhanced sensitivity to neutralizing antibodies in a variant of equine infectious anemia virus is linked to amino acid substitutions in the surface unit envelope glycoprotein
    • Cook RF, Berger SL, Rushlow KE, McManus JM, Cook SJ, Harrold S, Raabe ML, Montelaro RC, Issel CJ. 1995. Enhanced sensitivity to neutralizing antibodies in a variant of equine infectious anemia virus is linked to amino acid substitutions in the surface unit envelope glycoprotein. J Virol 69:1493-1499.
    • (1995) J Virol , vol.69 , pp. 1493-1499
    • Cook, R.F.1    Berger, S.L.2    Rushlow, K.E.3    McManus, J.M.4    Cook, S.J.5    Harrold, S.6    Raabe, M.L.7    Montelaro, R.C.8    Issel, C.J.9
  • 44
    • 0027311936 scopus 로고
    • Repertoire of neutralizing human monoclonal antibodies specific for the V3 domain of HIV-1 gp120
    • Gorny MK, Xu JY, Karwowska S, Buchbinder A, Zolla-Pazner S. 1993. Repertoire of neutralizing human monoclonal antibodies specific for the V3 domain of HIV-1 gp120. J Immunol 150:635-643.
    • (1993) J Immunol , vol.150 , pp. 635-643
    • Gorny, M.K.1    Xu, J.Y.2    Karwowska, S.3    Buchbinder, A.4    Zolla-Pazner, S.5
  • 45
    • 0031710046 scopus 로고    scopus 로고
    • Mapping of epitopes exposed on intact human immunodeficiency virus type 1 (HIV-1) virions: a new strategy for studying the immunologic relatedness of HIV-1
    • Nyambi PN, Gorny MK, Bastiani L, van der Groen G, Williams C, Zolla-Pazner S. 1998. Mapping of epitopes exposed on intact human immunodeficiency virus type 1 (HIV-1) virions: a new strategy for studying the immunologic relatedness of HIV-1. J Virol 72:9384-9391.
    • (1998) J Virol , vol.72 , pp. 9384-9391
    • Nyambi, P.N.1    Gorny, M.K.2    Bastiani, L.3    van der Groen, G.4    Williams, C.5    Zolla-Pazner, S.6
  • 46
    • 0029039317 scopus 로고
    • Serotyping of primary human immunodeficiency virus type 1 isolates from diverse geographic locations by flow cytometry
    • Zolla-Pazner S, O'Leary J, Burda S, Gorny MK, Kim M, Mascola J, McCutchan F. 1995. Serotyping of primary human immunodeficiency virus type 1 isolates from diverse geographic locations by flow cytometry. J Virol 69:3807-3815.
    • (1995) J Virol , vol.69 , pp. 3807-3815
    • Zolla-Pazner, S.1    O'Leary, J.2    Burda, S.3    Gorny, M.K.4    Kim, M.5    Mascola, J.6    McCutchan, F.7
  • 48
    • 0031023939 scopus 로고    scopus 로고
    • Prevalence of a V2 epitope in clade B primary isolates and its recognition by sera from HIV-1-infected individuals
    • Israel ZR, Gorny MK, Palmer C, McKeating JA, Zolla-Pazner S. 1997. Prevalence of a V2 epitope in clade B primary isolates and its recognition by sera from HIV-1-infected individuals. AIDS 11:128-130.
    • (1997) AIDS , vol.11 , pp. 128-130
    • Israel, Z.R.1    Gorny, M.K.2    Palmer, C.3    McKeating, J.A.4    Zolla-Pazner, S.5
  • 49
    • 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. 1998. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393: 648-659. http://dx.doi.org/10.1038/31405.
    • (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
  • 50
    • 0031902829 scopus 로고    scopus 로고
    • CD4-Induced conformational changes in the human immunodeficiency virus type 1 gp120 glycoprotein: consequences for virus entry and neutralization
    • Sullivan N, Sun Y, Sattentau Q, Thali M, Wu D, Denisova G, Gershoni J, Robinson J, Moore J, Sodroski J. 1998. CD4-Induced conformational changes in the human immunodeficiency virus type 1 gp120 glycoprotein: consequences for virus entry and neutralization. J Virol 72:4694-4703.
    • (1998) J Virol , vol.72 , pp. 4694-4703
    • Sullivan, N.1    Sun, Y.2    Sattentau, Q.3    Thali, M.4    Wu, D.5    Denisova, G.6    Gershoni, J.7    Robinson, J.8    Moore, J.9    Sodroski, J.10
  • 51
    • 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
  • 54
    • 0029119783 scopus 로고
    • Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding
    • Wyatt R, Moore J, Accola M, Desjardin E, Robinson J, Sodroski J. 1995. Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding. J Virol 69:5723-5733.
    • (1995) J Virol , vol.69 , pp. 5723-5733
    • Wyatt, R.1    Moore, J.2    Accola, M.3    Desjardin, E.4    Robinson, J.5    Sodroski, J.6
  • 55
    • 0025329476 scopus 로고
    • Escherichia coli expression, purification, and biological activity of a truncated soluble CD4
    • Garlick RL, Kirschner RJ, Eckenrode FM, Tarpley WG, Tomich CS. 1990. Escherichia coli expression, purification, and biological activity of a truncated soluble CD4. AIDS Res Hum Retroviruses 6:465-479. http://dx.doi.org/10.1089/aid.1990.6.465.
    • (1990) AIDS Res Hum Retroviruses , vol.6 , pp. 465-479
    • Garlick, R.L.1    Kirschner, R.J.2    Eckenrode, F.M.3    Tarpley, W.G.4    Tomich, C.S.5
  • 58
    • 45849125030 scopus 로고    scopus 로고
    • Evaluating neutralizing antibodies against HIV, SIV, and SHIV in luciferase reporter gene assays
    • Chapter 12, Unit 12.11
    • Montefiori DC. 2005. Evaluating neutralizing antibodies against HIV, SIV, and SHIV in luciferase reporter gene assays. Curr Protoc Immunol Chapter 12:Unit 12.11.
    • (2005) Curr Protoc Immunol
    • Montefiori, D.C.1
  • 59
    • 43049120226 scopus 로고    scopus 로고
    • Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet
    • Abdiche Y, Malashock D, Pinkerton A, Pons J. 2008. Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet. Anal Biochem 377:209-217. http://dx.doi.org/10.1016/j.ab.2008.03.035.
    • (2008) Anal Biochem , vol.377 , pp. 209-217
    • Abdiche, Y.1    Malashock, D.2    Pinkerton, A.3    Pons, J.4
  • 60
    • 84880816240 scopus 로고    scopus 로고
    • Epitope mapping of conformational V2-specific anti-HIV human monoclonal antibodies reveals an immunodominant site in V2
    • Mayr LM, Cohen S, Spurrier B, Kong XP, Zolla-Pazner S. 2013. Epitope mapping of conformational V2-specific anti-HIV human monoclonal antibodies reveals an immunodominant site in V2. PLoS One 8:e70859. http://dx.doi.org/10.1371/journal.pone.0070859.
    • (2013) PLoS One , vol.8
    • Mayr, L.M.1    Cohen, S.2    Spurrier, B.3    Kong, X.P.4    Zolla-Pazner, S.5
  • 61
    • 84878255015 scopus 로고    scopus 로고
    • Purification of recombinant vaccinia virus-expressed monomeric HIV-1 gp120 to apparent homogeneity
    • Guo W, Cleveland B, Davenport TM, Lee KK, Hu SL. 2013. Purification of recombinant vaccinia virus-expressed monomeric HIV-1 gp120 to apparent homogeneity. Protein Expr Purif 90:34-39. http://dx.doi.org/10.1016/j.pep.2013.04.009.
    • (2013) Protein Expr Purif , vol.90 , pp. 34-39
    • Guo, W.1    Cleveland, B.2    Davenport, T.M.3    Lee, K.K.4    Hu, S.L.5
  • 63
    • 0035199412 scopus 로고    scopus 로고
    • N-linked glycosylation in the V3 region of HIV type 1 surface antigen modulates coreceptor usage in viral infection
    • Li Y, Rey-Cuille MA, Hu SL. 2001. N-linked glycosylation in the V3 region of HIV type 1 surface antigen modulates coreceptor usage in viral infection. AIDS Res Hum Retroviruses 17:1473-1479. http://dx.doi.org/10.1089/08892220152644179.
    • (2001) AIDS Res Hum Retroviruses , vol.17 , pp. 1473-1479
    • Li, Y.1    Rey-Cuille, M.A.2    Hu, S.L.3
  • 64
    • 0025807938 scopus 로고
    • Envelope proteins from clinical isolates of human immunodeficiency virus type 1 that are refractory to neutralization by soluble CD4 possess high affinity for the CD4 receptor
    • Brighty DW, Rosenberg M, Chen IS, Ivey-Hoyle M. 1991. Envelope proteins from clinical isolates of human immunodeficiency virus type 1 that are refractory to neutralization by soluble CD4 possess high affinity for the CD4 receptor. Proc Natl Acad Sci U S A 88:7802-7805. http://dx.doi.org/10.1073/pnas.88.17.7802.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 7802-7805
    • Brighty, D.W.1    Rosenberg, M.2    Chen, I.S.3    Ivey-Hoyle, M.4
  • 65
    • 0026098754 scopus 로고
    • Envelope glycoproteins from biologically diverse isolates of immunodeficiency viruses have widely different affinities for CD4
    • Ivey-Hoyle M, Culp JS, Chaikin MA, Hellmig BD, Matthews TJ, Sweet RW, Rosenberg M. 1991. Envelope glycoproteins from biologically diverse isolates of immunodeficiency viruses have widely different affinities for CD4. Proc Natl Acad Sci U S A 88:512-516. http://dx.doi.org/10.1073/pnas.88.2.512.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 512-516
    • Ivey-Hoyle, M.1    Culp, J.S.2    Chaikin, M.A.3    Hellmig, B.D.4    Matthews, T.J.5    Sweet, R.W.6    Rosenberg, M.7
  • 66
    • 0026587795 scopus 로고
    • Human immunodeficiency virus type 2 envelope glycoprotein: differential CD4 interactions of soluble gp120 versus the assembled envelope complex
    • Mulligan MJ, Ritter GD, Jr, Chaikin MA, Yamshchikov GV, Kumar P, Hahn BH, Sweet RW, Compans RW. 1992. Human immunodeficiency virus type 2 envelope glycoprotein: differential CD4 interactions of soluble gp120 versus the assembled envelope complex. Virology 187:233-241. http://dx.doi.org/10.1016/0042-6822(92)90311-C.
    • (1992) Virology , vol.187 , pp. 233-241
    • Mulligan, M.J.1    Ritter, G.D.2    Chaikin, M.A.3    Yamshchikov, G.V.4    Kumar, P.5    Hahn, B.H.6    Sweet, R.W.7    Compans, R.W.8
  • 71
    • 0035220578 scopus 로고    scopus 로고
    • gp120: biologic aspects of structural features
    • Poignard P, Saphire EO, Parren PW, Burton DR. 2001. gp120: biologic aspects of structural features. Annu Rev Immunol 19:253-274. http://dx.doi.org/10.1146/annurev.immunol.19.1.253.
    • (2001) Annu Rev Immunol , vol.19 , pp. 253-274
    • Poignard, P.1    Saphire, E.O.2    Parren, P.W.3    Burton, D.R.4
  • 72
    • 0025075412 scopus 로고
    • Oligomeric organization of gp120 on infectious human immunodeficiency virus type 1 particles
    • Weiss CD, Levy JA, White JM. 1990. Oligomeric organization of gp120 on infectious human immunodeficiency virus type 1 particles. J Virol 64:5674-5677.
    • (1990) J Virol , vol.64 , pp. 5674-5677
    • Weiss, C.D.1    Levy, J.A.2    White, J.M.3
  • 73
  • 76
    • 84869140656 scopus 로고    scopus 로고
    • Sequences in glycoprotein gp41, the CD4 binding site, and the V2 domain regulate sensitivity and resistance of HIV-1 to broadly neutralizing antibodies
    • O'Rourke SM, Schweighardt B, Phung P, Mesa KA, Vollrath AL, Tatsuno GP, To B, Sinangil F, Limoli K, Wrin T, Berman PW. 2012. Sequences in glycoprotein gp41, the CD4 binding site, and the V2 domain regulate sensitivity and resistance of HIV-1 to broadly neutralizing antibodies. J Virol 86:12105-12114. http://dx.doi.org/10.1128/JVI.01352-12.
    • (2012) J Virol , vol.86 , pp. 12105-12114
    • O'Rourke, S.M.1    Schweighardt, B.2    Phung, P.3    Mesa, K.A.4    Vollrath, A.L.5    Tatsuno, G.P.6    To, B.7    Sinangil, F.8    Limoli, K.9    Wrin, T.10    Berman, P.W.11
  • 77
    • 0031975860 scopus 로고    scopus 로고
    • HLA-DR-positive dendritic cells of the normal human choroid plexus: a potential reservoir of HIV in the central nervous system
    • Hanly A, Petito CK. 1998. HLA-DR-positive dendritic cells of the normal human choroid plexus: a potential reservoir of HIV in the central nervous system.HumPathol 29:88-93. http://dx.doi.org/10.1016/S0046-8177(98)90395-1.
    • (1998) Hum Pathol , vol.29 , pp. 88-93
    • Hanly, A.1    Petito, C.K.2
  • 79
    • 32844457281 scopus 로고    scopus 로고
    • HIV-1 tropism for the central nervous system: brainderived envelope glycoproteins with lowerCD4dependence and reduced sensitivity to a fusion inhibitor
    • Martín-García J, Cao W, Varela-Rohena A, Plassmeyer ML, Gonzalez-Scarano F. 2006. HIV-1 tropism for the central nervous system: brainderived envelope glycoproteins with lowerCD4dependence and reduced sensitivity to a fusion inhibitor. Virology 346:169-179. http://dx.doi.org/10.1016/j.virol.2005.10.031.
    • (2006) Virology , vol.346 , pp. 169-179
    • Martín-García, J.1    Cao, W.2    Varela-Rohena, A.3    Plassmeyer, M.L.4    Gonzalez-Scarano, F.5
  • 80
    • 55649084842 scopus 로고    scopus 로고
    • The V1-V3 region of a brain-derived HIV-1 envelope glycoprotein determines macrophage tropism, low CD4 dependence, increased fusogenicity and altered sensitivity to entry inhibitors
    • Rossi F, Querido B, Nimmagadda M, Cocklin S, Navas-Martin S, Martin-Garcia J. 2008. The V1-V3 region of a brain-derived HIV-1 envelope glycoprotein determines macrophage tropism, low CD4 dependence, increased fusogenicity and altered sensitivity to entry inhibitors. Retrovirology 5:89. http://dx.doi.org/10.1186/1742-4690-5-89.
    • (2008) Retrovirology , vol.5 , pp. 89
    • Rossi, F.1    Querido, B.2    Nimmagadda, M.3    Cocklin, S.4    Navas-Martin, S.5    Martin-Garcia, J.6
  • 81
    • 16244419386 scopus 로고    scopus 로고
    • Identification of a new quaternary neutralizing epitope on human immunodeficiency virus type 1 virus particles
    • Gorny MK, Stamatatos L, Volsky B, Revesz K, Williams C, Wang XH, Cohen S, Staudinger R, Zolla-Pazner S. 2005. Identification of a new quaternary neutralizing epitope on human immunodeficiency virus type 1 virus particles. J Virol 79:5232-5237. http://dx.doi.org/10.1128/JVI.79.8.5232-5237.2005.
    • (2005) J Virol , vol.79 , pp. 5232-5237
    • Gorny, M.K.1    Stamatatos, L.2    Volsky, B.3    Revesz, K.4    Williams, C.5    Wang, X.H.6    Cohen, S.7    Staudinger, R.8    Zolla-Pazner, S.9
  • 83
    • 0025743908 scopus 로고
    • Posttranslational modifications within the HIV-1 envelope glycoprotein which restrict virus assembly and CD4-dependent infection
    • Haggerty S, Dempsey MP, Bukrinsky MI, Guo L, Stevenson M. 1991. Posttranslational modifications within the HIV-1 envelope glycoprotein which restrict virus assembly and CD4-dependent infection. AIDS Res Hum Retroviruses 7:501-510. http://dx.doi.org/10.1089/aid.1991.7.501.
    • (1991) AIDS Res Hum Retroviruses , vol.7 , pp. 501-510
    • Haggerty, S.1    Dempsey, M.P.2    Bukrinsky, M.I.3    Guo, L.4    Stevenson, M.5
  • 84
    • 0025074483 scopus 로고
    • Derivatives of amphotericin inhibit infection with human immunodeficiency virus in vitro by different modes of action
    • Hansen JE, Witzke NM, Nielsen C, Mathiesen LR, Teglbjaerg LS, Nielsen CM, Nielsen JO. 1990. Derivatives of amphotericin inhibit infection with human immunodeficiency virus in vitro by different modes of action. Antiviral Res 14:149-159. http://dx.doi.org/10.1016/0166-3542(90)90031-2.
    • (1990) Antiviral Res , vol.14 , pp. 149-159
    • Hansen, J.E.1    Witzke, N.M.2    Nielsen, C.3    Mathiesen, L.R.4    Teglbjaerg, L.S.5    Nielsen, C.M.6    Nielsen, J.O.7
  • 85
    • 0028244285 scopus 로고
    • An N-glycan within the human immunodeficiency virus type 1 gp120 V3 loop affects virus neutralization
    • Back NK, Smit L, De Jong JJ, Keulen W, Schutten M, Goudsmit J, Tersmette M. 1994. An N-glycan within the human immunodeficiency virus type 1 gp120 V3 loop affects virus neutralization. Virology 199: 431-438. http://dx.doi.org/10.1006/viro.1994.1141.
    • (1994) Virology , vol.199 , pp. 431-438
    • Back, N.K.1    Smit, L.2    De Jong, J.J.3    Keulen, W.4    Schutten, M.5    Goudsmit, J.6    Tersmette, M.7
  • 86
    • 33644609596 scopus 로고    scopus 로고
    • CCR5 use by human immunodeficiency virus type 1 is associated closely with the gp120 V3 loop N-linked glycosylation site
    • Clevestig P, Pramanik L, Leitner T, Ehrnst A. 2006. CCR5 use by human immunodeficiency virus type 1 is associated closely with the gp120 V3 loop N-linked glycosylation site. J Gen Virol 87:607-612. http://dx.doi.org/10.1099/vir.0.81510-0.
    • (2006) J Gen Virol , vol.87 , pp. 607-612
    • Clevestig, P.1    Pramanik, L.2    Leitner, T.3    Ehrnst, A.4
  • 87
    • 9944225582 scopus 로고    scopus 로고
    • Modified HIV envelope proteins with enhanced binding to neutralizing monoclonal antibodies
    • Kang SM, Quan FS, Huang C, Guo L, Ye L, Yang C, Compans RW. 2005. Modified HIV envelope proteins with enhanced binding to neutralizing monoclonal antibodies. Virology 331:20-32. http://dx.doi.org/10.1016/j.virol.2004.10.005.
    • (2005) Virology , vol.331 , pp. 20-32
    • Kang, S.M.1    Quan, F.S.2    Huang, C.3    Guo, L.4    Ye, L.5    Yang, C.6    Compans, R.W.7
  • 89
    • 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. 2004. 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 78:3279-3295. http://dx.doi.org/10.1128/JVI.78.7.3279-3295.2004.
    • (2004) J Virol , vol.78 , pp. 3279-3295
    • McCaffrey, R.A.1    Saunders, C.2    Hensel, M.3    Stamatatos, L.4
  • 90
    • 2942525411 scopus 로고    scopus 로고
    • HIV-1 acute infection env glycomutants designed from 3D model: effects on processing, antigenicity, and neutralization sensitivity
    • Reynard F, Fatmi A, Verrier B, Bedin F. 2004. HIV-1 acute infection env glycomutants designed from 3D model: effects on processing, antigenicity, and neutralization sensitivity. Virology 324:90-102. http://dx.doi.org/10.1016/j.virol.2004.03.022.
    • (2004) Virology , vol.324 , pp. 90-102
    • Reynard, F.1    Fatmi, A.2    Verrier, B.3    Bedin, F.4
  • 91
    • 0027462394 scopus 로고
    • Specificity of antibodies produced against native or desialylated human immunodeficiency virus type 1 recombinant gp160
    • Benjouad A, Gluckman JC, Montagnier L, Bahraoui E. 1993. Specificity of antibodies produced against native or desialylated human immunodeficiency virus type 1 recombinant gp160. J Virol 67:1693-1697.
    • (1993) J Virol , vol.67 , pp. 1693-1697
    • Benjouad, A.1    Gluckman, J.C.2    Montagnier, L.3    Bahraoui, E.4
  • 92
    • 0035851347 scopus 로고    scopus 로고
    • Enhanced immunogenicity of a human immunodeficiency virus type 1 env DNA vaccine by manipulating N-glycosylation signals. Effects of elimination of the V3 N306 glycan
    • Bolmstedt A, Hinkula J, Rowcliffe E, Biller M, Wahren B, Olofsson S. 2001. Enhanced immunogenicity of a human immunodeficiency virus type 1 env DNA vaccine by manipulating N-glycosylation signals. Effects of elimination of the V3 N306 glycan. Vaccine 20:397-405.
    • (2001) Vaccine , vol.20 , pp. 397-405
    • Bolmstedt, A.1    Hinkula, J.2    Rowcliffe, E.3    Biller, M.4    Wahren, B.5    Olofsson, S.6
  • 95
    • 0036229473 scopus 로고    scopus 로고
    • Role of N-linked glycans in a human immunodeficiency virus envelope glycoprotein: effects on protein function and the neutralizing antibody response
    • Quiñones-Kochs MI, Buonocore L, Rose JK. 2002. Role of N-linked glycans in a human immunodeficiency virus envelope glycoprotein: effects on protein function and the neutralizing antibody response. J Virol 76:4199-4211. http://dx.doi.org/10.1128/JVI.76.9.4199-4211.2002.
    • (2002) J Virol , vol.76 , pp. 4199-4211
    • Quiñones-Kochs, M.I.1    Buonocore, L.2    Rose, J.K.3
  • 98
    • 53849098568 scopus 로고    scopus 로고
    • A single site for N-linked glycosylation in the envelope glycoprotein of feline immunodeficiency virus modulates the virus-receptor interaction
    • Willett BJ, McMonagle EL, Logan N, Samman A, Hosie MJ. 2008. A single site for N-linked glycosylation in the envelope glycoprotein of feline immunodeficiency virus modulates the virus-receptor interaction. Retrovirology 5:77. http://dx.doi.org/10.1186/1742-4690-5-77.
    • (2008) Retrovirology , vol.5 , pp. 77
    • Willett, B.J.1    McMonagle, E.L.2    Logan, N.3    Samman, A.4    Hosie, M.J.5
  • 99
    • 0025004459 scopus 로고
    • Viral determinants of human immunodeficiency virus type 1 T-cell or macrophage tropism, cytopathogenicity, and CD4 antigen modulation
    • Cheng-Mayer C, Quiroga M, Tung JW, Dina D, Levy JA. 1990. Viral determinants of human immunodeficiency virus type 1 T-cell or macrophage tropism, cytopathogenicity, and CD4 antigen modulation. J Virol 64:4390-4398.
    • (1990) J Virol , vol.64 , pp. 4390-4398
    • Cheng-Mayer, C.1    Quiroga, M.2    Tung, J.W.3    Dina, D.4    Levy, J.A.5
  • 100
    • 3142679567 scopus 로고    scopus 로고
    • Intrinsic obstacles to human immunodeficiency virus type 1 coreceptor switching
    • Pastore C, Ramos A, Mosier DE. 2004. Intrinsic obstacles to human immunodeficiency virus type 1 coreceptor switching. J Virol 78:7565-7574. http://dx.doi.org/10.1128/JVI.78.14.7565-7574.2004.
    • (2004) J Virol , vol.78 , pp. 7565-7574
    • Pastore, C.1    Ramos, A.2    Mosier, D.E.3


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