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Volumn 8, Issue 8, 2013, Pages

HIV-1 Envelope Glycoprotein Variable Loops Are Indispensable for Envelope Structural Integrity and Virus Entry

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 160; GLYCOPROTEIN GP 41; VIRUS ENVELOPE PROTEIN;

EID: 84881006882     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0069789     Document Type: Article
Times cited : (18)

References (25)
  • 1
    • 78651237643 scopus 로고    scopus 로고
    • HIV-1 envelope subregion length variation during disease progression
    • Curlin ME, Zioni R, Hawes SE, Liu Y, Deng W, et al. (2010) HIV-1 envelope subregion length variation during disease progression. PLoS Pathog 6: e1001228.
    • (2010) PLoS Pathog , vol.6
    • Curlin, M.E.1    Zioni, R.2    Hawes, S.E.3    Liu, Y.4    Deng, W.5
  • 2
    • 38149080706 scopus 로고    scopus 로고
    • Independent evolution of hypervariable regions of HIV-1 gp120: V4 as a swarm of N-Linked glycosylation variants
    • Castro E, Belair M, Rizzardi GP, Bart PA, Pantaleo G, et al. (2008) Independent evolution of hypervariable regions of HIV-1 gp120: V4 as a swarm of N-Linked glycosylation variants. AIDS Res Hum Retroviruses 24: 106-113.
    • (2008) AIDS Res Hum Retroviruses , vol.24 , pp. 106-113
    • Castro, E.1    Belair, M.2    Rizzardi, G.P.3    Bart, P.A.4    Pantaleo, G.5
  • 3
    • 80054690690 scopus 로고    scopus 로고
    • Impact of mutations outside the V3 region on coreceptor tropism phenotypically assessed in patients infected with HIV-1 subtype B
    • Monno L, Saracino A, Scudeller L, Punzi G, Brindicci G, et al. (2011) Impact of mutations outside the V3 region on coreceptor tropism phenotypically assessed in patients infected with HIV-1 subtype B. Antimicrob Agents Chemother. 55: 5078-5084.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 5078-5084
    • Monno, L.1    Saracino, A.2    Scudeller, L.3    Punzi, G.4    Brindicci, G.5
  • 4
    • 79960405099 scopus 로고    scopus 로고
    • Longer V1V2 region with increased number of potential N-linked glycosylation sites in the HIV-1 envelope glycoprotein protects against HIV-specific neutralizing antibodies
    • van Gils MJ, Bunnik EM, Boeser-Nunnink BD, Burger JA, Terlouw-Klein M, et al. (2011) Longer V1V2 region with increased number of potential N-linked glycosylation sites in the HIV-1 envelope glycoprotein protects against HIV-specific neutralizing antibodies. J Virol 85: 6986-6995.
    • (2011) J Virol , vol.85 , pp. 6986-6995
    • van Gils, M.J.1    Bunnik, E.M.2    Boeser-Nunnink, B.D.3    Burger, J.A.4    Terlouw-Klein, M.5
  • 5
    • 77956425857 scopus 로고    scopus 로고
    • Adaptation of HIV-1 envelope gp120 to humoral immunity at a population level
    • Bunnik EM, Euler Z, Welkers MR, Boeser-Nunnink BD, Grijsen ML, et al. (2010) Adaptation of HIV-1 envelope gp120 to humoral immunity at a population level. Nat Med 16: 995-997.
    • (2010) Nat Med , vol.16 , pp. 995-997
    • Bunnik, E.M.1    Euler, Z.2    Welkers, M.R.3    Boeser-Nunnink, B.D.4    Grijsen, M.L.5
  • 6
    • 0037456827 scopus 로고    scopus 로고
    • Antibody neutralization and escape by HIV-1
    • Wei X, Decker JM, Wang S, Hui H, Kappes JC, et al. (2003) Antibody neutralization and escape by HIV-1. Nature 422: 307-312.
    • (2003) Nature , vol.422 , pp. 307-312
    • Wei, X.1    Decker, J.M.2    Wang, S.3    Hui, H.4    Kappes, J.C.5
  • 7
    • 38849090714 scopus 로고    scopus 로고
    • The c3-v4 region is a major target of autologous neutralizing antibodies in human immunodeficiency virus type 1 subtype C infection
    • Moore PL, Gray ES, Choge IA, Ranchobe N, Mlisana K, et al. (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.
    • (2008) J Virol , vol.82 , pp. 1860-1869
    • Moore, P.L.1    Gray, E.S.2    Choge, I.A.3    Ranchobe, N.4    Mlisana, K.5
  • 8
    • 34249789875 scopus 로고    scopus 로고
    • Unique mutational patterns in the envelope alpha 2 amphipathic helix and acquisition of length in gp120 hypervariable domains are associated with resistance to autologous neutralization of subtype C human immunodeficiency virus type 1
    • Rong R, Gnanakaran S, Decker JM, Bibollet-Ruche F, Taylor J, et al. (2007) Unique mutational patterns in the envelope alpha 2 amphipathic helix and acquisition of length in gp120 hypervariable domains are associated with resistance to autologous neutralization of subtype C human immunodeficiency virus type 1. J Virol 81: 5658-5668.
    • (2007) J Virol , vol.81 , pp. 5658-5668
    • Rong, R.1    Gnanakaran, S.2    Decker, J.M.3    Bibollet-Ruche, F.4    Taylor, J.5
  • 9
    • 70349695689 scopus 로고    scopus 로고
    • Escape from autologous neutralizing antibodies in acute/early subtype C HIV-1 infection requires multiple pathways
    • Rong R, Li B, Lynch RM, Haaland RE, Murphy MK, et al. (2009) Escape from autologous neutralizing antibodies in acute/early subtype C HIV-1 infection requires multiple pathways. PLoS Pathog 5: e1000594.
    • (2009) PLoS Pathog , vol.5
    • Rong, R.1    Li, B.2    Lynch, R.M.3    Haaland, R.E.4    Murphy, M.K.5
  • 10
    • 33846552274 scopus 로고    scopus 로고
    • Role of V1V2 and other human immunodeficiency virus type 1 envelope domains in resistance to autologous neutralization during clade C infection
    • Rong R, Bibollet-Ruche F, Mulenga J, Allen S, Blackwell JL, et al. (2007) Role of V1V2 and other human immunodeficiency virus type 1 envelope domains in resistance to autologous neutralization during clade C infection. J Virol 81: 1350-1359.
    • (2007) J Virol , vol.81 , pp. 1350-1359
    • Rong, R.1    Bibollet-Ruche, F.2    Mulenga, J.3    Allen, S.4    Blackwell, J.L.5
  • 11
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou T, Georgiev I, Wu X, Yang ZY, Dai K, et al. (2010) Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01. Science 329: 811-817.
    • (2010) Science , vol.329 , pp. 811-817
    • Zhou, T.1    Georgiev, I.2    Wu, X.3    Yang, Z.Y.4    Dai, K.5
  • 12
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    • McLellan JS, Pancera M, Carrico C, Gorman J, Julien JP, et al. (2011) Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 480: 336-343.
    • (2011) Nature , vol.480 , pp. 336-343
    • McLellan, J.S.1    Pancera, M.2    Carrico, C.3    Gorman, J.4    Julien, J.P.5
  • 13
    • 82255179322 scopus 로고    scopus 로고
    • A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield
    • Pejchal R, Doores KJ, Walker LM, Khayat R, Huang PS, et al. (2011) A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield. Science 334: 1097-1103.
    • (2011) Science , vol.334 , pp. 1097-1103
    • Pejchal, R.1    Doores, K.J.2    Walker, L.M.3    Khayat, R.4    Huang, P.S.5
  • 14
    • 12344264596 scopus 로고    scopus 로고
    • Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage
    • Pancera M, Wyatt R, (2005) Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage. Virology 332: 145-156.
    • (2005) Virology , vol.332 , pp. 145-156
    • Pancera, M.1    Wyatt, R.2
  • 16
    • 67049156802 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV-1 antibodies disrupt a hinge-related function of gp41 at the membrane interface
    • Song L, Sun ZY, Coleman KE, Zwick MB, Gach JS, et al. (2009) Broadly neutralizing anti-HIV-1 antibodies disrupt a hinge-related function of gp41 at the membrane interface. Proc Natl Acad Sci U S A 106: 9057-9062.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 9057-9062
    • Song, L.1    Sun, Z.Y.2    Coleman, K.E.3    Zwick, M.B.4    Gach, J.S.5
  • 17
    • 84866493348 scopus 로고    scopus 로고
    • Broad and potent neutralization of HIV-1 by a gp41-specific human antibody
    • Huang J, Ofek G, Laub L, Louder MK, Doria-Rose NA, et al. (2012) Broad and potent neutralization of HIV-1 by a gp41-specific human antibody. Nature 491: 406-412.
    • (2012) Nature , vol.491 , pp. 406-412
    • Huang, J.1    Ofek, G.2    Laub, L.3    Louder, M.K.4    Doria-Rose, N.A.5
  • 18
    • 84866061123 scopus 로고    scopus 로고
    • Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer
    • Mao Y, Wang L, Gu C, Herschhorn A, Xiang SH, et al. (2012) Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer. Nat Struct Mol Biol 19: 893-899.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 893-899
    • Mao, Y.1    Wang, L.2    Gu, C.3    Herschhorn, A.4    Xiang, S.H.5
  • 19
    • 80052287270 scopus 로고    scopus 로고
    • Mechanism of Neutralization by the Broadly Neutralizing HIV-1 Monoclonal Antibody VRC01
    • Li Y, O'Dell S, Walker LM, Wu X, Guenaga J, et al. (2011) Mechanism of Neutralization by the Broadly Neutralizing HIV-1 Monoclonal Antibody VRC01. J Virol 85: 8954-8967.
    • (2011) J Virol , vol.85 , pp. 8954-8967
    • Li, Y.1    O'Dell, S.2    Walker, L.M.3    Wu, X.4    Guenaga, J.5
  • 20
    • 84871653353 scopus 로고    scopus 로고
    • HIV-1 V3 loop crown epitope-focused mimotope selection by patient serum from random phage display libraries: Implications for the epitope structural features
    • Gazarian KG, Palacios-Rodriguez Y, Gazarian TG, Huerta L, (2013) HIV-1 V3 loop crown epitope-focused mimotope selection by patient serum from random phage display libraries: Implications for the epitope structural features. Mol Immunol 54: 148-156.
    • (2013) Mol Immunol , vol.54 , pp. 148-156
    • Gazarian, K.G.1    Palacios-Rodriguez, Y.2    Gazarian, T.G.3    Huerta, L.4
  • 22
    • 33744933182 scopus 로고    scopus 로고
    • Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity
    • Stanfield RL, Gorny MK, Zolla-Pazner S, Wilson IA, (2006) Crystal structures of human immunodeficiency virus type 1 (HIV-1) neutralizing antibody 2219 in complex with three different V3 peptides reveal a new binding mode for HIV-1 cross-reactivity. J Virol 80: 6093-6105.
    • (2006) J Virol , vol.80 , pp. 6093-6105
    • Stanfield, R.L.1    Gorny, M.K.2    Zolla-Pazner, S.3    Wilson, I.A.4
  • 23
    • 0034467955 scopus 로고    scopus 로고
    • Mutational analysis of conserved domains within the cytoplasmic tail of gp41 from human immunodeficiency virus type 1: effects on glycoprotein incorporation and infectivity
    • Piller SC, Dubay JW, Derdeyn CA, Hunter E, (2000) Mutational analysis of conserved domains within the cytoplasmic tail of gp41 from human immunodeficiency virus type 1: effects on glycoprotein incorporation and infectivity. J Virol 74: 11717-11723.
    • (2000) J Virol , vol.74 , pp. 11717-11723
    • Piller, S.C.1    Dubay, J.W.2    Derdeyn, C.A.3    Hunter, E.4
  • 24
    • 80051737642 scopus 로고    scopus 로고
    • HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation
    • Checkley MA, Luttge BG, Freed EO, (2011) HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation. J Mol Biol 410: 582-608.
    • (2011) J Mol Biol , vol.410 , pp. 582-608
    • Checkley, M.A.1    Luttge, B.G.2    Freed, E.O.3
  • 25
    • 0029655514 scopus 로고    scopus 로고
    • Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions
    • Freed EO, Martin MA, (1996) Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions. J Virol 70: 341-351.
    • (1996) J Virol , vol.70 , pp. 341-351
    • Freed, E.O.1    Martin, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.