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Volumn 398-399, Issue 1, 2013, Pages 1-18

Mathematical models: A key to understanding HIV envelope interactions?

Author keywords

Epitope masking by variable loops 1 and 2; Human immunodeficiency virus envelope interactions; Mathematical models; Quaternary epitopes

Indexed keywords

EPITOPE; NEUTRALIZING ANTIBODY; VIRUS ENVELOPE PROTEIN;

EID: 84888206204     PISSN: 00221759     EISSN: 18727905     Source Type: Journal    
DOI: 10.1016/j.jim.2013.09.002     Document Type: Article
Times cited : (5)

References (91)
  • 5
    • 84863774072 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses
    • Burton D.R., Poignard P., Stanfield R.L., Wilson I.A. Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses. Science 2012, 337:183.
    • (2012) Science , vol.337 , pp. 183
    • Burton, D.R.1    Poignard, P.2    Stanfield, R.L.3    Wilson, I.A.4
  • 6
    • 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., Sullivan N., Desjardin E., Parolin C., Robinson J., Wyatt R., Sodroski J. Replication and neutralization of human immunodeficiency virus type 1 lacking the V1 and V2 variable loops of the gp120 envelope glycoprotein. J. Virol. 1997, 71:9808.
    • (1997) J. Virol. , vol.71 , pp. 9808
    • Cao, J.1    Sullivan, N.2    Desjardin, E.3    Parolin, C.4    Robinson, J.5    Wyatt, R.6    Sodroski, J.7
  • 7
    • 0030842609 scopus 로고    scopus 로고
    • Specific N-linked and O-linked glycosylation modifications in the envelope V1 domain of simian immunodeficiency virus variants that evolve in the host alter recognition by neutralizing antibodies
    • Chackerian B., Rudensey L., Overbaugh J. Specific N-linked and O-linked glycosylation modifications in the envelope V1 domain of simian immunodeficiency virus variants that evolve in the host alter recognition by neutralizing antibodies. J. Virol. 1997, 71:7719.
    • (1997) J. Virol. , vol.71 , pp. 7719
    • Chackerian, B.1    Rudensey, L.2    Overbaugh, J.3
  • 9
    • 18144397438 scopus 로고    scopus 로고
    • Selection for human immunodeficiency virus type I 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. Selection for human immunodeficiency virus type I envelope glycosylation variants with shorter V1-V2 loop sequences occurs during transmission of certain genetic subtypes and may impact viral RNA levels. J. Virol. 2005, 79:6528.
    • (2005) J. Virol. , vol.79 , pp. 6528
    • Chohan, B.1    Lang, D.2    Sagar, M.3    Korber, B.4    Lavreys, L.5    Richardson, B.6    Overbaugh, J.7
  • 12
    • 0025286391 scopus 로고
    • Human immunodeficiency virus types 1 and 2 and simian immunodeficiency virus env proteins possess a functionally conserved assembly domain
    • Doms R.W., Earl P.L., Chakrabarti S., Moss B. Human immunodeficiency virus types 1 and 2 and simian immunodeficiency virus env proteins possess a functionally conserved assembly domain. J. Virol. 1990, 64:3537.
    • (1990) J. Virol. , vol.64 , pp. 3537
    • Doms, R.W.1    Earl, P.L.2    Chakrabarti, S.3    Moss, B.4
  • 13
    • 77957198704 scopus 로고    scopus 로고
    • Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16
    • Doores K.J., Burton D.R. Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16. Journal Of Virology 2010, 84:10510.
    • (2010) Journal Of Virology , vol.84 , pp. 10510
    • Doores, K.J.1    Burton, D.R.2
  • 16
    • 0031060154 scopus 로고    scopus 로고
    • Length polymorphism within the second variable region of the human immunodeficiency virus type 1 envelope glycoprotein affects accessibility of the receptor binding site
    • Fox D., Balfe P., Palmer C., May J., Arnold C., McKeating J. Length polymorphism within the second variable region of the human immunodeficiency virus type 1 envelope glycoprotein affects accessibility of the receptor binding site. J. Virol. 1997, 71:759.
    • (1997) J. Virol. , vol.71 , pp. 759
    • Fox, D.1    Balfe, P.2    Palmer, C.3    May, J.4    Arnold, C.5    McKeating, J.6
  • 18
    • 84866172362 scopus 로고    scopus 로고
    • Neutralizing antibody escape during HIV-1 mother-to-child transmission involves conformational masking of distal epitopes in envelope
    • Goo L., Milligan C., Simonich C.A., Nduati R., Overbaugh J. Neutralizing antibody escape during HIV-1 mother-to-child transmission involves conformational masking of distal epitopes in envelope. J. Virol. 2012, 86:9566.
    • (2012) J. Virol. , vol.86 , pp. 9566
    • Goo, L.1    Milligan, C.2    Simonich, C.A.3    Nduati, R.4    Overbaugh, J.5
  • 21
    • 34248393059 scopus 로고    scopus 로고
    • Independent evolution of human immunodeficiency virus type 1 env V1/V2 and V4/V5 hypervariable regions during chronic infection
    • Harrington P.R., Nelson J.A.E., Kitrinos K.M., Swanstrom R. Independent evolution of human immunodeficiency virus type 1 env V1/V2 and V4/V5 hypervariable regions during chronic infection. J. Virol. 2007, 81:5413.
    • (2007) J. Virol. , vol.81 , pp. 5413
    • Harrington, P.R.1    Nelson, J.A.E.2    Kitrinos, K.M.3    Swanstrom, R.4
  • 22
    • 33745833942 scopus 로고    scopus 로고
    • Dominant-negative effect of hetero-oligomerization on the function of the human immunodeficiency virus type 1 envelope glycoprotein complex
    • Herrera C., Klasse P.J., Kibler C.W., Michael E., Moore J.P., Beddows S. Dominant-negative effect of hetero-oligomerization on the function of the human immunodeficiency virus type 1 envelope glycoprotein complex. Virology 2006, 351:121.
    • (2006) Virology , vol.351 , pp. 121
    • Herrera, C.1    Klasse, P.J.2    Kibler, C.W.3    Michael, E.4    Moore, J.P.5    Beddows, S.6
  • 23
    • 77951882041 scopus 로고    scopus 로고
    • Toward an antibody-based HIV-1 vaccine
    • Hoxie J.A. Toward an antibody-based HIV-1 vaccine. Annu Rev Med 2010, 61:135.
    • (2010) Annu Rev Med , vol.61 , pp. 135
    • Hoxie, J.A.1
  • 24
    • 79952368717 scopus 로고    scopus 로고
    • Structural comparison of HIV-1 envelope spikes with and without the V1/V2 loop
    • Hu G., Liu J., Taylor K.A., Roux K.H. Structural comparison of HIV-1 envelope spikes with and without the V1/V2 loop. J. Virol. 2011, 85:2741.
    • (2011) J. Virol. , vol.85 , pp. 2741
    • Hu, G.1    Liu, J.2    Taylor, K.A.3    Roux, K.H.4
  • 25
    • 0030666591 scopus 로고    scopus 로고
    • Investigation of population diversity of human immunodeficiency virus type 1 in vivo by nucleotide sequencing and length polymorphism analysis of the V1/V2 hypervariable region of env
    • Hughes E.S., Bell J.E., Simmonds P. Investigation of population diversity of human immunodeficiency virus type 1 in vivo by nucleotide sequencing and length polymorphism analysis of the V1/V2 hypervariable region of env. J. Gen. Virol. 1997, 78(Pt 11):2871.
    • (1997) J. Gen. Virol. , vol.78 , Issue.PART 11 , pp. 2871
    • Hughes, E.S.1    Bell, J.E.2    Simmonds, P.3
  • 26
    • 0036167956 scopus 로고    scopus 로고
    • A replication-competent, neutralization-sensitive variant of simian immunodeficiency virus lacking 100 amino acids of envelope
    • Johnson W.E., Morgan J., Reitter J., Puffer B.A., Czajak S., Doms R.W., Desrosiers R.C. A replication-competent, neutralization-sensitive variant of simian immunodeficiency virus lacking 100 amino acids of envelope. J. Virol. 2002, 76:2075.
    • (2002) J. Virol. , vol.76 , pp. 2075
    • 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
  • 28
    • 36048944421 scopus 로고    scopus 로고
    • Modeling how many envelope glycoprotein trimers per virion participate in human immunodeficiency virus infectivity and its neutralization by antibody
    • Klasse P.J. Modeling how many envelope glycoprotein trimers per virion participate in human immunodeficiency virus infectivity and its neutralization by antibody. Virology 2007, 369:245.
    • (2007) Virology , vol.369 , pp. 245
    • Klasse, P.J.1
  • 29
    • 0036711665 scopus 로고    scopus 로고
    • Occupancy and mechanism in antibody-mediated neutralization of animal viruses
    • Klasse P.J., Sattentau Q.J. Occupancy and mechanism in antibody-mediated neutralization of animal viruses. J. Gen. Virol. 2002, 83:2091.
    • (2002) J. Gen. Virol. , vol.83 , pp. 2091
    • Klasse, P.J.1    Sattentau, Q.J.2
  • 30
    • 0028293281 scopus 로고
    • Functional role of the V1/V2 region of human immunodeficiency virus type 1 envelope glycoprotein gp120 in infection of primary macrophages and soluble CD4 neutralization
    • Koito A., Harrowe G., Levy J.A., Cheng-Mayer C. Functional role of the V1/V2 region of human immunodeficiency virus type 1 envelope glycoprotein gp120 in infection of primary macrophages and soluble CD4 neutralization. J. Virol. 1994, 68:2253.
    • (1994) J. Virol. , vol.68 , pp. 2253
    • Koito, A.1    Harrowe, G.2    Levy, J.A.3    Cheng-Mayer, C.4
  • 31
    • 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. 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. 2001, 75:3435.
    • (2001) J. Virol. , vol.75 , pp. 3435
    • Kolchinsky, P.1    Kiprilov, E.2    Bartley, P.3    Rubinstein, R.4    Sodroski, J.5
  • 32
    • 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., Pinter A., Honnen W.J., Gorny M.K., Nyambi P.N., Zolla-Pazner S., Kayman S.C. 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. 2005, 79:780.
    • (2005) J. Virol. , vol.79 , pp. 780
    • 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
  • 34
    • 84866495323 scopus 로고    scopus 로고
    • Human antibodies that neutralize HIV-1: Identification, structures, and B cell ontogenies
    • Kwong P.D., Mascola J.R. Human antibodies that neutralize HIV-1: Identification, structures, and B cell ontogenies. Immunity 2012, 37:412.
    • (2012) Immunity , vol.37 , pp. 412
    • Kwong, P.D.1    Mascola, J.R.2
  • 37
    • 0027176286 scopus 로고
    • Independent variation and positive selection in env V1 and V2 domains within maternal-infant strains of human immunodeficiency virus type 1 in vivo
    • Lamers S.L., Sleasman J.W., She J.X., Barrie K.A., Pomeroy S.M., Barrett D.J., Goodenow M.M. Independent variation and positive selection in env V1 and V2 domains within maternal-infant strains of human immunodeficiency virus type 1 in vivo. J. Virol. 1993, 67:3951.
    • (1993) J. Virol. , vol.67 , pp. 3951
    • Lamers, S.L.1    Sleasman, J.W.2    She, J.X.3    Barrie, K.A.4    Pomeroy, S.M.5    Barrett, D.J.6    Goodenow, M.M.7
  • 38
    • 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 B.A., Anderson D., Montefiori D., Polacino P., Hu S.L. Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses. J. Virol. 2008, 82:638.
    • (2008) J. Virol. , vol.82 , pp. 638
    • 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
  • 40
    • 84055178652 scopus 로고    scopus 로고
    • Intraprotomer masking of third variable loop (V3) epitopes by the first and second variable loops (V1V2) within the native HIV-1 envelope glycoprotein trimer
    • Liu L., Cimbro R., Lusso P., Berger E.A. Intraprotomer masking of third variable loop (V3) epitopes by the first and second variable loops (V1V2) within the native HIV-1 envelope glycoprotein trimer. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:20148.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 20148
    • Liu, L.1    Cimbro, R.2    Lusso, P.3    Berger, E.A.4
  • 41
    • 0034821095 scopus 로고    scopus 로고
    • Protection of neutralization epitopes in the V3 loop of oligomeric human immunodeficiency virus type 1 glycoprotein 120 by N-linked oligosaccharides in the V1 region
    • Losman B., Bolmstedt A., Schonning K., Bjorndal A., Westin C., Fenyo E.M., Olofsson S. Protection of neutralization epitopes in the V3 loop of oligomeric human immunodeficiency virus type 1 glycoprotein 120 by N-linked oligosaccharides in the V1 region. AIDS Res. Hum. Retroviruses 2001, 17:1067.
    • (2001) AIDS Res. Hum. Retroviruses , vol.17 , pp. 1067
    • Losman, B.1    Bolmstedt, A.2    Schonning, K.3    Bjorndal, A.4    Westin, C.5    Fenyo, E.M.6    Olofsson, S.7
  • 42
    • 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., Stamatatos L. 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. 2000, 74:6769.
    • (2000) J. Virol. , vol.74 , pp. 6769
    • Ly, A.1    Stamatatos, L.2
  • 43
    • 77950803185 scopus 로고    scopus 로고
    • Estimating the stoichiometry of HIV neutralization
    • Magnus C., Regoes R.R. Estimating the stoichiometry of HIV neutralization. PLoS Comput. Biol. 2010, 6:e1000713. 10.1371/journal.pcbi.1000713.
    • (2010) PLoS Comput. Biol. , vol.6
    • Magnus, C.1    Regoes, R.R.2
  • 44
    • 84859123277 scopus 로고    scopus 로고
    • Analysis of the subunit stoichiometries in viral entry
    • Magnus C., Regoes R.R. Analysis of the subunit stoichiometries in viral entry. PLoS One 2012, 7:e33441.
    • (2012) PLoS One , vol.7
    • Magnus, C.1    Regoes, R.R.2
  • 45
    • 59749083598 scopus 로고    scopus 로고
    • Estimating the stoichiometry of human immunodeficiency virus entry
    • Magnus C., Rusert P., Bonhoeffer S., Trkola A., Regoes R.R. Estimating the stoichiometry of human immunodeficiency virus entry. J. Virol. 2009, 83:1523.
    • (2009) J. Virol. , vol.83 , pp. 1523
    • Magnus, C.1    Rusert, P.2    Bonhoeffer, S.3    Trkola, A.4    Regoes, R.R.5
  • 50
    • 60349089294 scopus 로고    scopus 로고
    • Measuring HIV neutralization in a luciferase reporter gene assay
    • Montefiori D.C.D. Measuring HIV neutralization in a luciferase reporter gene assay. Methods Mol. Biol. 2008, 485:395.
    • (2008) Methods Mol. Biol. , vol.485 , pp. 395
    • Montefiori, D.C.D.1
  • 51
    • 0030694769 scopus 로고    scopus 로고
    • The V1/V2 region of human immunodeficiency virus type 1 modulates the sensitivity to neutralization by soluble CD4 and cellular tropism
    • Morikita T., Maeda Y., Fujii S., Matsushita S., Obaru K., Takatsuki K. The V1/V2 region of human immunodeficiency virus type 1 modulates the sensitivity to neutralization by soluble CD4 and cellular tropism. AIDS Res. Hum. Retroviruses 1997, 13:1291.
    • (1997) AIDS Res. Hum. Retroviruses , vol.13 , pp. 1291
    • Morikita, T.1    Maeda, Y.2    Fujii, S.3    Matsushita, S.4    Obaru, K.5    Takatsuki, K.6
  • 52
    • 77957940271 scopus 로고    scopus 로고
    • Mutation at a single position in the V2 domain of the HIV-1 envelope protein confers neutralization sensitivity to a highly neutralization-resistant virus
    • O'Rourke S.M., Schweighardt B., Phung P., Fonseca D.P., Terry K., Wrin T., Sinangil F., Berman P.W. Mutation at a single position in the V2 domain of the HIV-1 envelope protein confers neutralization sensitivity to a highly neutralization-resistant virus. J. Virol. 2010, 84:11200.
    • (2010) J. Virol. , vol.84 , pp. 11200
    • O'Rourke, S.M.1    Schweighardt, B.2    Phung, P.3    Fonseca, D.P.4    Terry, K.5    Wrin, T.6    Sinangil, F.7    Berman, P.W.8
  • 53
    • 0029929738 scopus 로고    scopus 로고
    • Functional characterization of the V1V2 region of human immunodeficiency virus type 1
    • Palmer C., Balfe P., Fox D., May J., Frederiksson R., Fenyo E., McKeating J. Functional characterization of the V1V2 region of human immunodeficiency virus type 1. Virology 1996, 220:436.
    • (1996) Virology , vol.220 , pp. 436
    • Palmer, C.1    Balfe, P.2    Fox, D.3    May, J.4    Frederiksson, R.5    Fenyo, E.6    McKeating, J.7
  • 54
    • 30344443665 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 coreceptor switching: V1/V2 gain-of-fitness mutations compensate for V3 loss-of-fitness mutations
    • Pastore C., Nedellec R., Ramos A., Pontow S., Ratner L., Mosier D.E. Human immunodeficiency virus type 1 coreceptor switching: V1/V2 gain-of-fitness mutations compensate for V3 loss-of-fitness mutations. J. Virol. 2006, 80:750.
    • (2006) J. Virol. , vol.80 , pp. 750
    • Pastore, C.1    Nedellec, R.2    Ramos, A.3    Pontow, S.4    Ratner, L.5    Mosier, D.E.6
  • 55
    • 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., Honnen W.J., He Y., Gorny M.K., Zolla-Pazner S., Kayman S.C. 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. 2004, 78:5205.
    • (2004) J. Virol. , vol.78 , pp. 5205
    • Pinter, A.1    Honnen, W.J.2    He, Y.3    Gorny, M.K.4    Zolla-Pazner, S.5    Kayman, S.C.6
  • 56
    • 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
    • Quinones-Kochs M.I., Buonocore L., Rose J.K. Role of N-linked glycans in a human immunodeficiency virus envelope glycoprotein: effects on protein function and the neutralizing antibody response. J. Virol. 2002, 76:4199.
    • (2002) J. Virol. , vol.76 , pp. 4199
    • Quinones-Kochs, M.I.1    Buonocore, L.2    Rose, J.K.3
  • 57
    • 17444384573 scopus 로고    scopus 로고
    • An unrelated monoclonal antibody neutralizes human immunodeficiency virus type 1 by binding to an artificial epitope engineered in a functionally neutral region of the viral envelope glycoproteins
    • Ren X., Sodroski J., Yang X. An unrelated monoclonal antibody neutralizes human immunodeficiency virus type 1 by binding to an artificial epitope engineered in a functionally neutral region of the viral envelope glycoproteins. J. Virol. 2005, 79:5616. 10.1128/JVI.79.9.5616-5624.2005.
    • (2005) J. Virol. , vol.79 , pp. 5616
    • Ren, X.1    Sodroski, J.2    Yang, X.3
  • 59
    • 0021833513 scopus 로고
    • Characterization of envelope and core structural gene-products of HTLV-III with sera from AIDS patients
    • Robey W., Safai B., Oroszlan S., Arthur L., Gonda M., Gallo R., Fischinger P. Characterization of envelope and core structural gene-products of HTLV-III with sera from AIDS patients. Science 1985, 228:593.
    • (1985) Science , vol.228 , pp. 593
    • Robey, W.1    Safai, B.2    Oroszlan, S.3    Arthur, L.4    Gonda, M.5    Gallo, R.6    Fischinger, P.7
  • 60
    • 77949411309 scopus 로고    scopus 로고
    • Quaternary epitope specificities of anti-HIV-1 neutralizing antibodies generated in rhesus macaques infected by the simian/human immunodeficiency virus SHIVSF162P4
    • Robinson J.E., Franco K., Elliott D.H., Maher M.J., Reyna A., Montefiori D.C., Zolla-Pazner S., Gorny M.K., Kraft Z., Stamatatos L. Quaternary epitope specificities of anti-HIV-1 neutralizing antibodies generated in rhesus macaques infected by the simian/human immunodeficiency virus SHIVSF162P4. J. Virol. 2010, 84:3443.
    • (2010) J. Virol. , vol.84 , pp. 3443
    • Robinson, J.E.1    Franco, K.2    Elliott, D.H.3    Maher, M.J.4    Reyna, A.5    Montefiori, D.C.6    Zolla-Pazner, S.7    Gorny, M.K.8    Kraft, Z.9    Stamatatos, L.10
  • 61
    • 0032560559 scopus 로고    scopus 로고
    • The ability of HIV type 1 to use CCR-3 as a coreceptor is controlled by envelope V1/V2 sequences acting in conjunction with a CCR-5 tropic V3 loop
    • Ross T.M., Cullen B.R. The ability of HIV type 1 to use CCR-3 as a coreceptor is controlled by envelope V1/V2 sequences acting in conjunction with a CCR-5 tropic V3 loop. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:7682.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7682
    • Ross, T.M.1    Cullen, B.R.2
  • 63
    • 33748925430 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1V1-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. Human immunodeficiency virus type 1V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity. J. Virol. 2006, 80:9586.
    • (2006) J. Virol. , vol.80 , pp. 9586
    • Sagar, M.1    Wu, X.2    Lee, S.3    Overbaugh, J.4
  • 64
    • 0033749617 scopus 로고    scopus 로고
    • Cooperative subunit interactions within the oligomeric envelope glycoprotein of hiv-1: functional complementation of specific defects in gp120 and gp41
    • Salzwedel K., Berger E. Cooperative subunit interactions within the oligomeric envelope glycoprotein of hiv-1: functional complementation of specific defects in gp120 and gp41. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:12794.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 12794
    • Salzwedel, K.1    Berger, E.2
  • 65
    • 0028999803 scopus 로고
    • Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer
    • Sattentau Q.J., Moore J.P. Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer. J. Exp. Med. 1995, 182:185.
    • (1995) J. Exp. Med. , vol.182 , pp. 185
    • Sattentau, Q.J.1    Moore, J.P.2
  • 66
    • 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., McCaffrey R.A., Zharkikh I., Kraft Z., Malenbaum S.E., Burke B., Cheng-Mayer C., Stamatatos L. 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. 2005, 79:9069.
    • (2005) J. Virol. , vol.79 , pp. 9069
    • 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
  • 67
    • 0032850727 scopus 로고    scopus 로고
    • Stoichiometry of monoclonal antibody neutralization of T-cell line-adapted human immunodeficiency virus type 1
    • Schonning K., Lund O., Lund O.S., Hansen J.E.S. Stoichiometry of monoclonal antibody neutralization of T-cell line-adapted human immunodeficiency virus type 1. J. Virol. 1999, 8364-8370.
    • (1999) J. Virol.
    • Schonning, K.1    Lund, O.2    Lund, O.S.3    Hansen, J.E.S.4
  • 68
    • 34247156283 scopus 로고    scopus 로고
    • Impact of V2 mutations on escape from a potent neutralizing anti-V3 monoclonal antibody during in vitro selection of a primary human immunodeficiency virus type 1 isolate
    • Shibata J., Yoshimura K., Honda A., Koito A., Murakami T., Matsushita S. Impact of V2 mutations on escape from a potent neutralizing anti-V3 monoclonal antibody during in vitro selection of a primary human immunodeficiency virus type 1 isolate. J. Virol. 2007, 81:3757.
    • (2007) J. Virol. , vol.81 , pp. 3757
    • Shibata, J.1    Yoshimura, K.2    Honda, A.3    Koito, A.4    Murakami, T.5    Matsushita, S.6
  • 69
    • 0026089184 scopus 로고
    • Macrophage and T cell-line tropisms of HIV-1 are determined by specific regions of the envelope gp120 gene
    • Shioda T., Levy J.A., Cheng-Mayer C. Macrophage and T cell-line tropisms of HIV-1 are determined by specific regions of the envelope gp120 gene. Nature 1991, 349:167.
    • (1991) Nature , vol.349 , pp. 167
    • Shioda, T.1    Levy, J.A.2    Cheng-Mayer, C.3
  • 70
    • 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., Cheng-Mayer C. 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. 1998, 72:7840.
    • (1998) J. Virol. , vol.72 , pp. 7840
    • Stamatatos, L.1    Cheng-Mayer, C.2
  • 71
    • 0032169683 scopus 로고    scopus 로고
    • Effect of major deletions in the V1 and V2 loops of a macrophage-tropic HIV type 1 isolate on viral envelope structure, cell entry, and replication
    • Stamatatos L., Wiskerchen M., Cheng-Mayer C. Effect of major deletions in the V1 and V2 loops of a macrophage-tropic HIV type 1 isolate on viral envelope structure, cell entry, and replication. AIDS Res. Hum. Retroviruses 1998, 14:1129.
    • (1998) AIDS Res. Hum. Retroviruses , vol.14 , pp. 1129
    • Stamatatos, L.1    Wiskerchen, M.2    Cheng-Mayer, C.3
  • 72
    • 69149083668 scopus 로고    scopus 로고
    • Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine?
    • Stamatatos L., Morris L., Burton D.R., Mascola J.R. Neutralizing antibodies generated during natural HIV-1 infection: good news for an HIV-1 vaccine?. Nat. Med. 2009, 15:866.
    • (2009) Nat. Med. , vol.15 , pp. 866
    • Stamatatos, L.1    Morris, L.2    Burton, D.R.3    Mascola, J.R.4
  • 73
    • 0027204667 scopus 로고
    • Effect of amino acid changes in the V1/V2 region of the human immunodeficiency virus type 1 gp120 glycoprotein on subunit association, syncytium formation, and recognition by a neutralizing antibody
    • Sullivan N., Thali M., Furman C., Ho D.D., Sodroski J. Effect of amino acid changes in the V1/V2 region of the human immunodeficiency virus type 1 gp120 glycoprotein on subunit association, syncytium formation, and recognition by a neutralizing antibody. J. Virol. 1993, 67:3674.
    • (1993) J. Virol. , vol.67 , pp. 3674
    • Sullivan, N.1    Thali, M.2    Furman, C.3    Ho, D.D.4    Sodroski, J.5
  • 74
    • 0028866919 scopus 로고
    • Human immunodeficiency virus envelope V1 and V2 regions influence replication efficiency in macrophages by affecting virus spread
    • Toohey K., Wehrly K., Nishio J., Perryman S., Chesebro B. Human immunodeficiency virus envelope V1 and V2 regions influence replication efficiency in macrophages by affecting virus spread. Virology 1995, 213:70.
    • (1995) Virology , vol.213 , pp. 70
    • Toohey, K.1    Wehrly, K.2    Nishio, J.3    Perryman, S.4    Chesebro, B.5
  • 75
    • 0022352075 scopus 로고
    • Characterization of gp41 as the transmembrane protein coded by the HTLV-III/LAV envelope gene
    • Veronese F., Devico A., Copeland T., Oroszlan S., Gallo R., Sarngadharan M. Characterization of gp41 as the transmembrane protein coded by the HTLV-III/LAV envelope gene. Science 1985, 229:1402.
    • (1985) Science , vol.229 , pp. 1402
    • Veronese, F.1    Devico, A.2    Copeland, T.3    Oroszlan, S.4    Gallo, R.5    Sarngadharan, M.6
  • 81
    • 33748881797 scopus 로고    scopus 로고
    • N-Glycans in the gp120 V1/V2 domain of the HIV-1 strain NL4-3 are indispensable for viral infectivity and resistance against antibody neutralization
    • Wolk T., Schreiber M. N-Glycans in the gp120 V1/V2 domain of the HIV-1 strain NL4-3 are indispensable for viral infectivity and resistance against antibody neutralization. Med. Microbiol. Immunol. 2006, 195:165.
    • (2006) Med. Microbiol. Immunol. , vol.195 , pp. 165
    • Wolk, T.1    Schreiber, M.2
  • 82
    • 70350320690 scopus 로고    scopus 로고
    • Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment
    • Wu X., Zhou T., O'Dell S., Wyatt R.T., Kwong P.D., Mascola J.R. Mechanism of human immunodeficiency virus type 1 resistance to monoclonal antibody B12 that effectively targets the site of CD4 attachment. J. Virol. 2009, 83:10892.
    • (2009) J. Virol. , vol.83 , pp. 10892
    • Wu, X.1    Zhou, T.2    O'Dell, S.3    Wyatt, R.T.4    Kwong, P.D.5    Mascola, J.R.6
  • 83
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens
    • Wyatt R., Sodroski J. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 1998, 280:1884.
    • (1998) Science , vol.280 , pp. 1884
    • Wyatt, R.1    Sodroski, J.2
  • 84
    • 0027194743 scopus 로고
    • Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions
    • Wyatt R., Sullivan N., Thali M., Repke H., Ho D., Robinson J., Posner M., Sodroski J. Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions. J. Virol. 1993, 67:4557.
    • (1993) J. Virol. , vol.67 , pp. 4557
    • Wyatt, R.1    Sullivan, N.2    Thali, M.3    Repke, H.4    Ho, D.5    Robinson, J.6    Posner, M.7    Sodroski, J.8
  • 85
    • 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. 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. 1995, 69:5723.
    • (1995) J. Virol. , vol.69 , pp. 5723
    • Wyatt, R.1    Moore, J.2    Accola, M.3    Desjardin, E.4    Robinson, J.5    Sodroski, J.6
  • 86
    • 1842432386 scopus 로고    scopus 로고
    • Selective modification of variable loops alters tropism and enhances immunogenicity of human immunodeficiency virus type 1 envelope
    • Yang Z.Y., Chakrabarti B.K., Xu L., Welcher B., Kong W.P., Leung K., Panet A., Mascola J.R., Nabel G.J. Selective modification of variable loops alters tropism and enhances immunogenicity of human immunodeficiency virus type 1 envelope. J. Virol. 2004, 78:4029.
    • (2004) J. Virol. , vol.78 , pp. 4029
    • Yang, Z.Y.1    Chakrabarti, B.K.2    Xu, L.3    Welcher, B.4    Kong, W.P.5    Leung, K.6    Panet, A.7    Mascola, J.R.8    Nabel, G.J.9
  • 87
    • 14744269583 scopus 로고    scopus 로고
    • Stoichiometry of antibody neutralization of Human Immunodeficiency Virus type 1
    • Yang X., Kurteva S., Lee S., Sodroski J. Stoichiometry of antibody neutralization of Human Immunodeficiency Virus type 1. J. Virol. 2005, 79:3500.
    • (2005) J. Virol. , vol.79 , pp. 3500
    • Yang, X.1    Kurteva, S.2    Lee, S.3    Sodroski, J.4
  • 88
    • 25144500649 scopus 로고    scopus 로고
    • Stoichiometry of envelope glycoprotein trimers in the entry of Human Immunodeficiency Virus type 1
    • Yang X., Kurteva S., Ren X., Lee S., Sodroski J. Stoichiometry of envelope glycoprotein trimers in the entry of Human Immunodeficiency Virus type 1. J. Virol. 2005, 79:12132.
    • (2005) J. Virol. , vol.79 , pp. 12132
    • Yang, X.1    Kurteva, S.2    Ren, X.3    Lee, S.4    Sodroski, J.5
  • 89
    • 33646185493 scopus 로고    scopus 로고
    • Subunit stoichiometry of human immunodeficiency virus type 1 envelope glycoprotein trimers during virus entry into host cells
    • Yang X., Kurteva S., Ren X., Lee S., Sodroski J. Subunit stoichiometry of human immunodeficiency virus type 1 envelope glycoprotein trimers during virus entry into host cells. J. Virol. 2006, 80:4388.
    • (2006) J. Virol. , vol.80 , pp. 4388
    • Yang, X.1    Kurteva, S.2    Ren, X.3    Lee, S.4    Sodroski, J.5
  • 90
    • 33750743141 scopus 로고    scopus 로고
    • Antibody binding is a dominant determinant of the efficiency of human immunodeficiency virus type 1 neutralization
    • Yang X., Lipchina I., Cocklin S., Chaiken I., Sodroski J. Antibody binding is a dominant determinant of the efficiency of human immunodeficiency virus type 1 neutralization. J. Virol. 2006, 80:11404. 10.1128/JVI.01102-06.
    • (2006) J. Virol. , vol.80 , pp. 11404
    • Yang, X.1    Lipchina, I.2    Cocklin, S.3    Chaiken, I.4    Sodroski, J.5


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