메뉴 건너뛰기




Volumn 82, Issue 12, 2008, Pages 5912-5921

Characterization of neutralizing antibody responses elicited by clade a envelope immunogens derived from early transmitted viruses

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN GP 140; GLYCOPROTEIN GP 160; NEUTRALIZING ANTIBODY;

EID: 44949262146     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00389-08     Document Type: Article
Times cited : (17)

References (71)
  • 1
    • 0028244285 scopus 로고
    • An N-glycan within the human immunodeficiency virus type 1 gp120 V3 loop affects virus neutralization
    • Back, N. K. T., L. Smit, J.-J. De Jong, W. Keulen, M. Schutten, J. Goudsmit, and M. Tersmette. 1994. An N-glycan within the human immunodeficiency virus type 1 gp120 V3 loop affects virus neutralization. Virology 199:431-438.
    • (1994) Virology , vol.199 , pp. 431-438
    • Back, N.K.T.1    Smit, L.2    De Jong, J.-J.3    Keulen, W.4    Schutten, M.5    Goudsmit, J.6    Tersmette, M.7
  • 3
    • 33947590277 scopus 로고    scopus 로고
    • A comparative immunogenicity study in rabbits of disulfide-stabilized, proteolytically cleaved, soluble trimeric human immunodeficiency virus type 1 gp140, trimeric cleavage-defective gp140 and monomeric gp120
    • Beddows, S., M. Franti, A. K. Dey, M. Kirschner, S. P. Iyer, D. C. Fisch, T. Ketas, E. Yuste, R. C. Desrosiers, P. J. Klasse, P. J. Maddon, W. C. Olson, and J. P. Moore. 2007. A comparative immunogenicity study in rabbits of disulfide-stabilized, proteolytically cleaved, soluble trimeric human immunodeficiency virus type 1 gp140, trimeric cleavage-defective gp140 and monomeric gp120. Virology 360:329-340.
    • (2007) Virology , vol.360 , pp. 329-340
    • Beddows, S.1    Franti, M.2    Dey, A.K.3    Kirschner, M.4    Iyer, S.P.5    Fisch, D.C.6    Ketas, T.7    Yuste, E.8    Desrosiers, R.C.9    Klasse, P.J.10    Maddon, P.J.11    Olson, W.C.12    Moore, J.P.13
  • 4
    • 21644445378 scopus 로고    scopus 로고
    • Evaluating the immunogenicity of a disulfide-stabilized, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1
    • Beddows, S., N. Schülke, M. Kirschner, K. Barnes, M. Franti, E. Michael, T. Ketas, R. W. Sanders, P. J. Maddon, W. C. Olson, and J. P. Moore. 2005. Evaluating the immunogenicity of a disulfide-stabilized, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1. J. Virol. 79:8812-8827.
    • (2005) J. Virol , vol.79 , pp. 8812-8827
    • Beddows, S.1    Schülke, N.2    Kirschner, M.3    Barnes, K.4    Franti, M.5    Michael, E.6    Ketas, T.7    Sanders, R.W.8    Maddon, P.J.9    Olson, W.C.10    Moore, J.P.11
  • 5
    • 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
    • Binley, J. M., 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. 2000. 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. 74:627-643.
    • (2000) J. Virol , vol.74 , 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
  • 6
    • 34147180438 scopus 로고    scopus 로고
    • HIV-1 subtype A envelope variants from early in infection have variable sensitivity to neutralization and to inhibitors of viral entry
    • Blish, C. A., R. Nedellec, K. Mandaliya, D. E. Mosier, and J. Overbaugh. 2007. HIV-1 subtype A envelope variants from early in infection have variable sensitivity to neutralization and to inhibitors of viral entry. AIDS 21: 693-702.
    • (2007) AIDS , vol.21 , pp. 693-702
    • Blish, C.A.1    Nedellec, R.2    Mandaliya, K.3    Mosier, D.E.4    Overbaugh, J.5
  • 7
    • 38849205377 scopus 로고    scopus 로고
    • Enhancing exposure of HIV-1 neutralization epitopes through mutations in gp41
    • Blish, C. A., M. A. Nguyen, and J. Overbaugh. 2008. Enhancing exposure of HIV-1 neutralization epitopes through mutations in gp41. PLoS Med. 5:e9.
    • (2008) PLoS Med , vol.5
    • Blish, C.A.1    Nguyen, M.A.2    Overbaugh, J.3
  • 9
    • 34648824673 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 subtype distribution in the worldwide epidemic: Pathogenetic and therapeutic implications
    • Buonaguro, L., M. L. Tornesello, and F. M. Buonaguro. 2007. Human immunodeficiency virus type 1 subtype distribution in the worldwide epidemic: pathogenetic and therapeutic implications. J. Virol. 81:10209-10219.
    • (2007) J. Virol , vol.81 , pp. 10209-10219
    • Buonaguro, L.1    Tornesello, M.L.2    Buonaguro, F.M.3
  • 10
    • 0034634910 scopus 로고    scopus 로고
    • Bures, R., A. Gaitan, T. Zhu, C. Graziosi, K. M. McGrath, J. Tartaglia, P. Caudrelier, R. El Habib, M. Klein, A. Lazzarin, D. M. Stablein, M. Deers, L. Corey, M. L. Greenberg, D. H. Schwartz, and D. C. Montefiori. 2000. Immunization with recombinant canarypox vectors expressing membrane-anchored glycoprotein 120 followed by glycoprotein 160 boosting fails to generate antibodies that neutralize R5 primary isolates of human immunodeficiency virus type 1. AIDS Res. Hum. Retrovir. 16:2019-2035.
    • Bures, R., A. Gaitan, T. Zhu, C. Graziosi, K. M. McGrath, J. Tartaglia, P. Caudrelier, R. El Habib, M. Klein, A. Lazzarin, D. M. Stablein, M. Deers, L. Corey, M. L. Greenberg, D. H. Schwartz, and D. C. Montefiori. 2000. Immunization with recombinant canarypox vectors expressing membrane-anchored glycoprotein 120 followed by glycoprotein 160 boosting fails to generate antibodies that neutralize R5 primary isolates of human immunodeficiency virus type 1. AIDS Res. Hum. Retrovir. 16:2019-2035.
  • 12
    • 0030812563 scopus 로고    scopus 로고
    • Replication and neutralization of human immunodeficiency virus type 1 lacking the V1 and V2 variable loops of the gp120 envelope glycoprotein
    • Cao, J., N. Sullivan, E. Desjardin, C. Parolin, J. Robinson, R. Wyatt, and J. Sodroski. 1997. Replication and neutralization of human immunodeficiency virus type 1 lacking the V1 and V2 variable loops of the gp120 envelope glycoprotein. J. Virol. 71:9808-9812.
    • (1997) J. Virol , vol.71 , pp. 9808-9812
    • Cao, J.1    Sullivan, N.2    Desjardin, E.3    Parolin, C.4    Robinson, J.5    Wyatt, R.6    Sodroski, J.7
  • 13
    • 1242319460 scopus 로고    scopus 로고
    • Center, R. J., J. Lebowitz, R. D. Leapman, and B. Moss. 2004. Promoting trimerizalion of soluble human immunodeficiency virus type 1 (HIV-1) Env through the use of HIV-1/simian immunodeficiency virus chimeras. J. Virol. 78:2265-2276.
    • Center, R. J., J. Lebowitz, R. D. Leapman, and B. Moss. 2004. Promoting trimerizalion of soluble human immunodeficiency virus type 1 (HIV-1) Env through the use of HIV-1/simian immunodeficiency virus chimeras. J. Virol. 78:2265-2276.
  • 14
    • 0030862430 scopus 로고    scopus 로고
    • Compact, synthetic, vaccinia virus early/late promoter for protein expression
    • Chakrabarti, S., J. R. Sisler, and B. Moss. 1997. Compact, synthetic, vaccinia virus early/late promoter for protein expression. BioTechniques 23:1094-1097.
    • (1997) BioTechniques , vol.23 , pp. 1094-1097
    • Chakrabarti, S.1    Sisler, J.R.2    Moss, B.3
  • 15
    • 37848999666 scopus 로고    scopus 로고
    • The first hypervariable region of the gp120 Env glycoprotein defines the neutralizing susceptibility of heterologous human immunodeficiency virus type 1 isolates to neutralizing antibodies elicited by the SF162gp140 immunogen
    • Ching, L. K., G. Vlachogiannis, K. A. Bosch, and L. Stamatatos. 2008. The first hypervariable region of the gp120 Env glycoprotein defines the neutralizing susceptibility of heterologous human immunodeficiency virus type 1 isolates to neutralizing antibodies elicited by the SF162gp140 immunogen. J. Virol. 82:949-956.
    • (2008) J. Virol , vol.82 , pp. 949-956
    • Ching, L.K.1    Vlachogiannis, G.2    Bosch, K.A.3    Stamatatos, L.4
  • 16
    • 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., D. Lang, M. Sagar, B. Korber, L. Lavreys, B. Richardson, and J. Overbaugh. 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.
    • (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
  • 19
    • 34249827906 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 monomeric and trimeric gp120 glycoproteins stabilized in the CD4-bound state: Antigenicity biophysics, and immunogenicity
    • Dey, B., M. Pancera, K. Svehla, Y. Shu, S.-H. Xiang, J. Vainshtein, Y. Li, J. Sodroski, P. D. Kwong, J. R. Mascola, and R. Wyatt. 2007. Characterization of human immunodeficiency virus type 1 monomeric and trimeric gp120 glycoproteins stabilized in the CD4-bound state: antigenicity biophysics, and immunogenicity. J. Virol. 81:5579-5593.
    • (2007) J. Virol , vol.81 , pp. 5579-5593
    • Dey, B.1    Pancera, M.2    Svehla, K.3    Shu, Y.4    Xiang, S.-H.5    Vainshtein, J.6    Li, Y.7    Sodroski, J.8    Kwong, P.D.9    Mascola, J.R.10    Wyatt, R.11
  • 21
    • 0035168058 scopus 로고    scopus 로고
    • Immunogenicity and protective efficacy of oligomeric human immunodeficiency virus type 1 gp140
    • Earl, P. L., W. Sugiura, D. C. Montefiori, C. C. Broder, S. A. Lee, C. Wild, J. Lifson, and B. Moss. 2001. Immunogenicity and protective efficacy of oligomeric human immunodeficiency virus type 1 gp140. J. Virol. 75:645-653.
    • (2001) J. Virol , vol.75 , 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
  • 22
    • 0031846234 scopus 로고    scopus 로고
    • Stabilization of human immunodeficiency virus type 1 envelope glycoprotein trimers by disulfide bonds introduced into the gp41 glycoprotein ectodomain
    • Farzan, M., H. Choe, E. Desjardins, Y. Sun, J. Kuhn, J. Cao, D. Archambault, P. Kolchinsky, M. Koch, R. Wyatt, and J. Sodroski. 1998. Stabilization of human immunodeficiency virus type 1 envelope glycoprotein trimers by disulfide bonds introduced into the gp41 glycoprotein ectodomain. J. Virol. 72:7620-7625.
    • (1998) J. Virol , vol.72 , pp. 7620-7625
    • Farzan, M.1    Choe, H.2    Desjardins, E.3    Sun, Y.4    Kuhn, J.5    Cao, J.6    Archambault, D.7    Kolchinsky, P.8    Koch, M.9    Wyatt, R.10    Sodroski, J.11
  • 24
    • 34247595321 scopus 로고    scopus 로고
    • Clade-specific differences between human immunodeficiency virus type 1 clades B and C: Diversity and correlations in C3-V4 regions of gp120
    • Gnanakaran, S., D. Lang, M. Daniels, T. Bhattacharya, C. A. Derdeyn, and B. Korber. 2007. Clade-specific differences between human immunodeficiency virus type 1 clades B and C: diversity and correlations in C3-V4 regions of gp120. J. Virol. 81:4886-4891.
    • (2007) J. Virol , vol.81 , pp. 4886-4891
    • Gnanakaran, S.1    Lang, D.2    Daniels, M.3    Bhattacharya, T.4    Derdeyn, C.A.5    Korber, B.6
  • 25
    • 0036720793 scopus 로고    scopus 로고
    • Human monoclonal antibodies specific for conformation-sensitive epitopes of V3 neutralize human immunodeficiency virus type 1 primary isolates from various clades
    • Gorny, M. K., C. Williams, B. Volsky, K. Revesz, S. Cohen, V. R. Polonis, W. J. Honnen, S. C. Kayman, C. Krachmarov, A. Pinter, and S. Zolla-Pazner. 2002. Human monoclonal antibodies specific for conformation-sensitive epitopes of V3 neutralize human immunodeficiency virus type 1 primary isolates from various clades. J. Virol. 76:9035-9045.
    • (2002) J. Virol , vol.76 , pp. 9035-9045
    • Gorny, M.K.1    Williams, C.2    Volsky, B.3    Revesz, K.4    Cohen, S.5    Polonis, V.R.6    Honnen, W.J.7    Kayman, S.C.8    Krachmarov, C.9    Pinter, A.10    Zolla-Pazner, S.11
  • 27
    • 9944264023 scopus 로고    scopus 로고
    • Analysis of the neutralizing antibody response elicited in rabbits by repeated inoculation with trimeric HIV-1 envelope glycoproteins
    • Grundner, C., Y. Li, M. Louder, J. Mascola, X. Yang, J. Sodroski, and R. Wyatt. 2005. Analysis of the neutralizing antibody response elicited in rabbits by repeated inoculation with trimeric HIV-1 envelope glycoproteins. Virology 331:33-46.
    • (2005) Virology , vol.331 , pp. 33-46
    • Grundner, C.1    Li, Y.2    Louder, M.3    Mascola, J.4    Yang, X.5    Sodroski, J.6    Wyatt, R.7
  • 29
    • 0028449193 scopus 로고
    • Measuring vaccine-induced HIV neutralization: Report of a workshop
    • Hanson, C. V. 1994. Measuring vaccine-induced HIV neutralization: report of a workshop. AIDS Res. Hum. Retrovir. 10:645-648.
    • (1994) AIDS Res. Hum. Retrovir , vol.10 , pp. 645-648
    • Hanson, C.V.1
  • 30
    • 0022472989 scopus 로고
    • Expression of AIDS virus envelope gene in recombinant vaccinia viruses
    • Hu, S. L., S. G. Kosowski, and J. M. Dalrymple. 1986. Expression of AIDS virus envelope gene in recombinant vaccinia viruses. Nature 320:537-540.
    • (1986) Nature , vol.320 , pp. 537-540
    • Hu, S.L.1    Kosowski, S.G.2    Dalrymple, J.M.3
  • 31
    • 0036167956 scopus 로고    scopus 로고
    • A replication-competent, neutralization-sensitive variant of simian immunodeficiency virus lacking 100 amino acids of envelope
    • Johnson, W. E., J. Morgan, J. Reitter, B. A. Puffer, S. Czajak, R. W. Doms, and R. C. Desrosiers. 2002. A replication-competent, neutralization-sensitive variant of simian immunodeficiency virus lacking 100 amino acids of envelope. J. Virol. 76:2075-2086.
    • (2002) J. Virol , vol.76 , pp. 2075-2086
    • Johnson, W.E.1    Morgan, J.2    Reitter, J.3    Puffer, B.A.4    Czajak, S.5    Doms, R.W.6    Desrosiers, R.C.7
  • 32
    • 0141458878 scopus 로고    scopus 로고
    • Assorted mutations in the envelope gene of simian immunodeficiency virus lead to loss of neutralization resistance against antibodies representing a broad spectrum of specificities
    • Johnson, W. E., H. Sanford, L. Schwall, D. R. Burton, P. W. H. I. Parren, J. E. Robinson, and R. C. Desrosiers. 2003. Assorted mutations in the envelope gene of simian immunodeficiency virus lead to loss of neutralization resistance against antibodies representing a broad spectrum of specificities. J. Virol. 77:9993-10003.
    • (2003) J. Virol , vol.77 , pp. 9993-10003
    • Johnson, W.E.1    Sanford, H.2    Schwall, L.3    Burton, D.R.4    Parren, P.W.H.I.5    Robinson, J.E.6    Desrosiers, R.C.7
  • 34
    • 0041920924 scopus 로고    scopus 로고
    • Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition
    • Koch, M., M. Pancera, P. D. Kwong, P. Kolchinsky, C. Grundner, L. Wang, W. A. Hendrickson, J. Sodroski, and R. Wyatt. 2003. Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition. Virology 313:387-400.
    • (2003) Virology , vol.313 , 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
  • 35
    • 11144233210 scopus 로고    scopus 로고
    • Antibodies that are cross-reactive for human immunodeficiency virus type 1 clade A and clade B V3 domains are common in patient sera from Cameroon, but their neutralization activity is usually restricted by epitope masking
    • Krachmarov, C., A. Pinter, W. J. Honnen, M. K. Gorny, P. N. Nyambi, S. Zolla-Pazner, and S. C. Kayman. 2005. Antibodies that are cross-reactive for human immunodeficiency virus type 1 clade A and clade B V3 domains are common in patient sera from Cameroon, but their neutralization activity is usually restricted by epitope masking. J. Virol. 79:780-790.
    • (2005) J. Virol , vol.79 , pp. 780-790
    • Krachmarov, C.1    Pinter, A.2    Honnen, W.J.3    Gorny, M.K.4    Nyambi, P.N.5    Zolla-Pazner, S.6    Kayman, S.C.7
  • 38
    • 31144451337 scopus 로고    scopus 로고
    • Characterization of antibody responses elicited by human immunodeficiency virus type 1 primary isolate trimeric and monomeric envelope glycoproteins in selected adjuvants
    • Li, Y., K. Svehla, N. L. Mathy, G. Voss, J. R. Mascola, and R. Wyatt. 2006. Characterization of antibody responses elicited by human immunodeficiency virus type 1 primary isolate trimeric and monomeric envelope glycoproteins in selected adjuvants. J. Virol. 80:1414-1426.
    • (2006) J. Virol , vol.80 , pp. 1414-1426
    • Li, Y.1    Svehla, K.2    Mathy, N.L.3    Voss, G.4    Mascola, J.R.5    Wyatt, R.6
  • 39
    • 0036260635 scopus 로고    scopus 로고
    • HIV type 1 variants transmitted to women in Kenya require the CCR5 coreceptor for entry, regardless of the genetic complexity of the infecting virus
    • Long, E. M., S. M. Rainwater, L. Lavreys, K. Mandaliya, and J. Overbaugh. 2002. HIV type 1 variants transmitted to women in Kenya require the CCR5 coreceptor for entry, regardless of the genetic complexity of the infecting virus. AIDS Res. Hum. Retrovir. 18:567-576.
    • (2002) AIDS Res. Hum. Retrovir , vol.18 , pp. 567-576
    • Long, E.M.1    Rainwater, S.M.2    Lavreys, L.3    Mandaliya, K.4    Overbaugh, J.5
  • 40
    • 0033942750 scopus 로고    scopus 로고
    • V2 loop glycosylation of the human immunodeficiency virus type 1 SF162 envelope facilitates interaction of this protein with CD4 and CCR5 receptors and protects the virus from neutralization by anti-V3 loop and anti-CD4 binding site antibodies
    • Ly, A., and L. Stamatatos. 2000. V2 loop glycosylation of the human immunodeficiency virus type 1 SF162 envelope facilitates interaction of this protein with CD4 and CCR5 receptors and protects the virus from neutralization by anti-V3 loop and anti-CD4 binding site antibodies. J. Virol. 74: 6769-6776.
    • (2000) J. Virol , vol.74 , pp. 6769-6776
    • Ly, A.1    Stamatatos, L.2
  • 41
    • 0034469170 scopus 로고    scopus 로고
    • The N-terminal V3 loop glycan modulates the interaction of clade A and B human immunodeficiency virus type 1 envelopes with CD4 and chemokine receptors
    • Malenbaum, S. E., D. Yang, L. Cavacini, M. Posner, J. Robinson, and C. Cheng-Mayer. 2000. The N-terminal V3 loop glycan modulates the interaction of clade A and B human immunodeficiency virus type 1 envelopes with CD4 and chemokine receptors. J. Virol. 74:11008-11016.
    • (2000) J. Virol , vol.74 , pp. 11008-11016
    • Malenbaum, S.E.1    Yang, D.2    Cavacini, L.3    Posner, M.4    Robinson, J.5    Cheng-Mayer, C.6
  • 42
    • 19144365910 scopus 로고    scopus 로고
    • Mascola, J. R., S. W. Snyder, O. S. Weislow, S. M. Belay, R. B. Belshe, D. H. Schwartz, M. L. Clements, R. Dolin, B. S. Graham, G. J. Gorse, M. C. Keefer, M. J. McElrath, M. C. Walker, K. F. Wagner, J. G. McNeil, F. E. McCutchan, D. S. Burke, and the NIAID AIDS Vaccine Evaluation Group. 1996. Immunization with envelope subunit vaccine products elicits neutralizing antibodies against laboratory-adapted but not primary isolates of human immunodeficiency virus type 1. J. Infect. Dis. 173:340-348.
    • Mascola, J. R., S. W. Snyder, O. S. Weislow, S. M. Belay, R. B. Belshe, D. H. Schwartz, M. L. Clements, R. Dolin, B. S. Graham, G. J. Gorse, M. C. Keefer, M. J. McElrath, M. C. Walker, K. F. Wagner, J. G. McNeil, F. E. McCutchan, D. S. Burke, and the NIAID AIDS Vaccine Evaluation Group. 1996. Immunization with envelope subunit vaccine products elicits neutralizing antibodies against laboratory-adapted but not primary isolates of human immunodeficiency virus type 1. J. Infect. Dis. 173:340-348.
  • 43
    • 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, R. A., C. Saunders, M. Hensel, and L. Stamatatos. 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.
    • (2004) J. Virol , vol.78 , pp. 3279-3295
    • McCaffrey, R.A.1    Saunders, C.2    Hensel, M.3    Stamatatos, L.4
  • 44
    • 38849090714 scopus 로고    scopus 로고
    • Moore, P. L., E. S. Gray, I. A. Choge, N. Ranchobe, K. Mlisana, S. S. Abdool Karim, C. Williamson, L. Morris, and the CAPRISA 002 Study Team. 2008. The C3-V4 region is a major target of autologous neutralizing antibodies in human immunodeficiency virus type 1 subtype C infection. J. Virol. 82:1860-1869.
    • Moore, P. L., E. S. Gray, I. A. Choge, N. Ranchobe, K. Mlisana, S. S. Abdool Karim, C. Williamson, L. Morris, and the CAPRISA 002 Study Team. 2008. The C3-V4 region is a major target of autologous neutralizing antibodies in human immunodeficiency virus type 1 subtype C infection. J. Virol. 82:1860-1869.
  • 45
    • 0346365289 scopus 로고    scopus 로고
    • Intrapatient alterations in the human immunodeficiency virus type 1 gp120 V1V2 and V3 regions differentially modulate coreceptor usage, virus inhibition by CC/CXC chemokines, soluble CD4, and the b12 and 2G12 monoclonal antibodies
    • Nabatov, A. A., G. Pollakis, T. Linnemann, A. Kliphius, M. I. Chalaby, and W. A. Paxton. 2004. Intrapatient alterations in the human immunodeficiency virus type 1 gp120 V1V2 and V3 regions differentially modulate coreceptor usage, virus inhibition by CC/CXC chemokines, soluble CD4, and the b12 and 2G12 monoclonal antibodies. J. Virol. 78:524-530.
    • (2004) J. Virol , vol.78 , pp. 524-530
    • Nabatov, A.A.1    Pollakis, G.2    Linnemann, T.3    Kliphius, A.4    Chalaby, M.I.5    Paxton, W.A.6
  • 46
    • 0026671622 scopus 로고
    • Alterations in potential sites for glycosylation predominate during evolution of the simian immunodeficiency virus envelope gene in macaques
    • Overbaugh, J., and L. M. Rudensey. 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
  • 47
    • 22544471847 scopus 로고    scopus 로고
    • Soluble mimetics of human immunodeficiency virus type 1 viral spikes produced by replacement of the native trimerization domain with a heterologous trimerization motif: Characterization and ligand binding analysis
    • Pancera, M., J. Lebowitz, A. Schön, P. Zhu, E. Freire, P. D. Kwong, K. H. Roux, J. Sodroski, and R. Wyatt. 2005. Soluble mimetics of human immunodeficiency virus type 1 viral spikes produced by replacement of the native trimerization domain with a heterologous trimerization motif: characterization and ligand binding analysis. J. Virol. 79:9954-9969.
    • (2005) J. Virol , vol.79 , pp. 9954-9969
    • Pancera, M.1    Lebowitz, J.2    Schön, A.3    Zhu, P.4    Freire, E.5    Kwong, P.D.6    Roux, K.H.7    Sodroski, J.8    Wyatt, R.9
  • 48
    • 2342644898 scopus 로고    scopus 로고
    • The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection
    • Pinter, A., W. J. Honnen, Y. He, M. K. Gorny, S. Zolla-Pazner, and S. C. Kayman. 2004. The V1/V2 domain of gp120 is a global regulator of the sensitivity of primary human immunodeficiency virus type 1 isolates to neutralization by antibodies commonly induced upon infection. J. Virol. 78: 5205-5215.
    • (2004) J. Virol , vol.78 , pp. 5205-5215
    • Pinter, A.1    Honnen, W.J.2    He, Y.3    Gorny, M.K.4    Zolla-Pazner, S.5    Kayman, S.C.6
  • 49
    • 0031749469 scopus 로고    scopus 로고
    • A role for carbohydrates in immune evasion in AIDS
    • Reitter, J. N., R. E. Means, and R. C. Desrosiers. 1998. A role for carbohydrates in immune evasion in AIDS. Nat. Med. 4:679-684.
    • (1998) Nat. Med , vol.4 , pp. 679-684
    • Reitter, J.N.1    Means, R.E.2    Desrosiers, R.C.3
  • 53
    • 21644446614 scopus 로고    scopus 로고
    • The V1, V2, and V3 regions of the human immunodeficiency virus type 1 envelope differentially affect the viral phenotype in an isolate-dependent manner
    • Saunders, C. J., R. A. McCaffrey, I. Zharkikh, Z. Kraft, S. E. Malenbaum, B. Burke, C. Cheng-Mayer, and L. Stamatatos. 2005. The V1, V2, and V3 regions of the human immunodeficiency virus type 1 envelope differentially affect the viral phenotype in an isolate-dependent manner. J. Virol. 79:9069-9080.
    • (2005) J. Virol , vol.79 , pp. 9069-9080
    • Saunders, C.J.1    McCaffrey, R.A.2    Zharkikh, I.3    Kraft, Z.4    Malenbaum, S.E.5    Burke, B.6    Cheng-Mayer, C.7    Stamatatos, L.8
  • 55
    • 34548695901 scopus 로고    scopus 로고
    • Standardized assessment of NAb responses elicited in rhesus monkeys immunized with single- or multi-clade HIV-1 envelope immunogens
    • Seaman, M. S., D. F. Leblanc, L. E. Grandpre, M. T. Bartman, D. C. Montefiori, N. L. Letvin, and J. R. Mascola. 2007. Standardized assessment of NAb responses elicited in rhesus monkeys immunized with single- or multi-clade HIV-1 envelope immunogens. Virology 367:175-186.
    • (2007) Virology , vol.367 , pp. 175-186
    • Seaman, M.S.1    Leblanc, D.F.2    Grandpre, L.E.3    Bartman, M.T.4    Montefiori, D.C.5    Letvin, N.L.6    Mascola, J.R.7
  • 56
    • 20144387694 scopus 로고    scopus 로고
    • Vaccine-elicited memory cytotoxic T lymphocytes contribute to Mamu-A*01-associated control of simian/human immunodeficiency virus 89.6P replication in rhesus monkeys
    • Seaman, M. S., S. Santra, M. H. Newberg, V. Philippon, K. Manson, L. Xu, R. S. Gelman, D. Panicali, J. R. Mascola, G. J. Nabel, and N. L. Letvin. 2005. Vaccine-elicited memory cytotoxic T lymphocytes contribute to Mamu-A*01-associated control of simian/human immunodeficiency virus 89.6P replication in rhesus monkeys. J. Virol. 79:4580-4588.
    • (2005) J. Virol , vol.79 , pp. 4580-4588
    • Seaman, M.S.1    Santra, S.2    Newberg, M.H.3    Philippon, V.4    Manson, K.5    Xu, L.6    Gelman, R.S.7    Panicali, D.8    Mascola, J.R.9    Nabel, G.J.10    Letvin, N.L.11
  • 57
    • 0026089184 scopus 로고
    • Macrophage and T cell-line tropisms of HIV-1 are determined by specific regions of the envelope gp120 gene
    • Shioda, T., J. A. Levy, and C. Cheng-Mayer. 1991. Macrophage and T cell-line tropisms of HIV-1 are determined by specific regions of the envelope gp120 gene. Nature (London) 349:167-169.
    • (1991) Nature (London) , vol.349 , pp. 167-169
    • Shioda, T.1    Levy, J.A.2    Cheng-Mayer, C.3
  • 58
    • 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
    • Srivastava, I. K., 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. 2003. 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. 77:11244-11259.
    • (2003) J. Virol , vol.77 , 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
  • 60
    • 0031666180 scopus 로고    scopus 로고
    • An envelope modification that renders a primary, neutralization-resistant, clade B human immunodeficiency virus type 1 isolate highly susceptible to neutralization by sera from other clades
    • Stamatatos, L., and C. Cheng-Mayer. 1998. An envelope modification that renders a primary, neutralization-resistant, clade B human immunodeficiency virus type 1 isolate highly susceptible to neutralization by sera from other clades. J. Virol. 72:7840-7845.
    • (1998) J. Virol , vol.72 , pp. 7840-7845
    • Stamatatos, L.1    Cheng-Mayer, C.2
  • 61
    • 0034235058 scopus 로고    scopus 로고
    • Generation and structural analysis of soluble oligomeric envelope proteins derived from neutralization-resistant and neutralization-susceptible primary HIV-1 isolates
    • Stamatatos, L., M. Lim, and C. Cheng-Mayer. 2000. Generation and structural analysis of soluble oligomeric envelope proteins derived from neutralization-resistant and neutralization-susceptible primary HIV-1 isolates. AIDS Res. Hum. Retrovir. 16:981-994.
    • (2000) AIDS Res. Hum. Retrovir , vol.16 , pp. 981-994
    • Stamatatos, L.1    Lim, M.2    Cheng-Mayer, C.3
  • 62
    • 33746651142 scopus 로고    scopus 로고
    • Polyvalent HIV-1 Env vaccine formulations delivered by the DNA priming plus protein boosting approach are effective in generating neutralizing antibodies against primary human immunodeficiency virus type 1 isolates from subtypes A, B, C, D and E
    • Wang, S., R. Pal, J. R. Mascola, T. H. Chou, I. Mboudjeka, S. Shen, Q. Liu, S. Whitney, T. Keen, B. C. Nair, V. S. Kalyanaraman, P. Markham, and S. Lu. 2006. Polyvalent HIV-1 Env vaccine formulations delivered by the DNA priming plus protein boosting approach are effective in generating neutralizing antibodies against primary human immunodeficiency virus type 1 isolates from subtypes A, B, C, D and E. Virology 350:34-47.
    • (2006) Virology , vol.350 , pp. 34-47
    • Wang, S.1    Pal, R.2    Mascola, J.R.3    Chou, T.H.4    Mboudjeka, I.5    Shen, S.6    Liu, Q.7    Whitney, S.8    Keen, T.9    Nair, B.C.10    Kalyanaraman, V.S.11    Markham, P.12    Lu, S.13
  • 63
    • 33744470143 scopus 로고    scopus 로고
    • Cross-clade recognition and neutralization by the V3 region from clade C human immunodeficiency virus-1 envelope
    • Wu, L., Z. Y. Yang, L. Xu, B. Welcher, S. Winfrey, Y. Shao, J. R. Mascola, and G. J. Nabel. 2006. Cross-clade recognition and neutralization by the V3 region from clade C human immunodeficiency virus-1 envelope. Vaccine 24:4995-5002.
    • (2006) Vaccine , vol.24 , pp. 4995-5002
    • Wu, L.1    Yang, Z.Y.2    Xu, L.3    Welcher, B.4    Winfrey, S.5    Shao, Y.6    Mascola, J.R.7    Nabel, G.J.8
  • 64
    • 33846224780 scopus 로고    scopus 로고
    • Characterization of immune responses elicited in macaques immunized sequentially with chimeric VEE/SIN alphavirus replicon particles expressing SIVGag and/or HIVEnv and with recombinant HIVgp140Env protein
    • Xu, R., I. K. Srivastava, C. E. Greer, I. Zarkikh, Z. Kraft, L. Kuller, J. M. Polo, S. W. Barnett, and L. Stamatatos. 2006. Characterization of immune responses elicited in macaques immunized sequentially with chimeric VEE/SIN alphavirus replicon particles expressing SIVGag and/or HIVEnv and with recombinant HIVgp140Env protein. AIDS Res. Hum. Retrovir. 22: 1022-1030.
    • (2006) AIDS Res. Hum. Retrovir , vol.22 , pp. 1022-1030
    • Xu, R.1    Srivastava, I.K.2    Greer, C.E.3    Zarkikh, I.4    Kraft, Z.5    Kuller, L.6    Polo, J.M.7    Barnett, S.W.8    Stamatatos, L.9
  • 65
    • 33646863044 scopus 로고    scopus 로고
    • Immunization with HIV-1 SF162-derived envelope gp140 proteins does not protect macaques from heterologous simian-human immunodeficiency virus SHIV89.6P infection
    • Xu, R., I. K. Srivastava, L. Kuller, I. Zarkikh, Z. Kraft, Z. Fagrouch, N. L. Letvin, J. L. Heeney, S. W. Barnett, and L. Stamatatos. 2006. Immunization with HIV-1 SF162-derived envelope gp140 proteins does not protect macaques from heterologous simian-human immunodeficiency virus SHIV89.6P infection. Virology 349:276-289.
    • (2006) Virology , vol.349 , pp. 276-289
    • Xu, R.1    Srivastava, I.K.2    Kuller, L.3    Zarkikh, I.4    Kraft, Z.5    Fagrouch, Z.6    Letvin, N.L.7    Heeney, J.L.8    Barnett, S.W.9    Stamatatos, L.10
  • 66
    • 0034004321 scopus 로고    scopus 로고
    • Modifications that stabilize human immunodeficiency virus envelope glycoprotein trimers in solution
    • Yang, X., L. Florin, M. Farzan, P. Kolchinsky, P. D. Kwong, J. Sodroski, and R. Wyatt. 2000. Modifications that stabilize human immunodeficiency virus envelope glycoprotein trimers in solution. J. Virol. 74:4746-4754.
    • (2000) J. Virol , vol.74 , 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
  • 67
    • 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
    • Yang, X., J. Lee, E. M. Mahony, P. D. Kwong, R. Wyatt, and J. Sodroski. 2002. Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin. J. Virol. 76:4634-4642.
    • (2002) J. Virol , vol.76 , pp. 4634-4642
    • Yang, X.1    Lee, J.2    Mahony, E.M.3    Kwong, P.D.4    Wyatt, R.5    Sodroski, J.6
  • 68
    • 0035155850 scopus 로고    scopus 로고
    • Improved elicitation of neutralizing antibodies against primary human immunodeficiency viruses by soluble stabilized envelope glycoprotein trimers
    • Yang, X., R. Wyatt, and J. Sodroski. 2001. Improved elicitation of neutralizing antibodies against primary human immunodeficiency viruses by soluble stabilized envelope glycoprotein trimers. J. Virol. 75:1165-1171.
    • (2001) J. Virol , vol.75 , pp. 1165-1171
    • Yang, X.1    Wyatt, R.2    Sodroski, J.3
  • 69
    • 0034467915 scopus 로고    scopus 로고
    • Association of structural changes in the V2 and V3 loops of the gp120 envelope glycoprotein with acquisition of neutralization resistance in a simian-human immunodeficiency virus passaged in vivo
    • Ye, Y., Z. H. Si, J. P. Moore, and J. Sodroski. 2000. Association of structural changes in the V2 and V3 loops of the gp120 envelope glycoprotein with acquisition of neutralization resistance in a simian-human immunodeficiency virus passaged in vivo. J. Virol. 74:11955-11962.
    • (2000) J. Virol , vol.74 , pp. 11955-11962
    • Ye, Y.1    Si, Z.H.2    Moore, J.P.3    Sodroski, J.4
  • 70
    • 0022555930 scopus 로고
    • T-cell responses to human AIDS virus in macaques immunized with recombinant vaccinia viruses
    • Zarling, J. M., W. Morton, P. A. Moran, J. McClure, S. G. Kosowski, and S. L. Hu. 1986. T-cell responses to human AIDS virus in macaques immunized with recombinant vaccinia viruses. Nature 323:344-346.
    • (1986) Nature , vol.323 , pp. 344-346
    • Zarling, J.M.1    Morton, W.2    Moran, P.A.3    McClure, J.4    Kosowski, S.G.5    Hu, S.L.6
  • 71
    • 34547154404 scopus 로고    scopus 로고
    • Zhang, P. F., F. Cham, M. Dong, A. Choudhary, P. Bouma, Z. Zhang, Y. Shao, Y. R. Feng, L. Wang, N. Mathy, G. Voss, C. C. Broder, and G. V. Quinnan, Jr. 2007. Extensively cross-reactive anti-HIV-1 neutralizing antibodies induced by gp140 immunization. Proc. Natl. Acad. Sci. USA 104: 10193-10198.
    • Zhang, P. F., F. Cham, M. Dong, A. Choudhary, P. Bouma, Z. Zhang, Y. Shao, Y. R. Feng, L. Wang, N. Mathy, G. Voss, C. C. Broder, and G. V. Quinnan, Jr. 2007. Extensively cross-reactive anti-HIV-1 neutralizing antibodies induced by gp140 immunization. Proc. Natl. Acad. Sci. USA 104: 10193-10198.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.