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Volumn 109, Issue 15, 2012, Pages 5663-5668

Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops

(18)  Kwon, Young Do a   Finzi, Andrés b   Wu, Xueling a   Dogo Isonagie, Cajetan d   Lee, Lawrence K e   Moore, Lucas R f   Schmidt, Stephen D a   Stuckey, Jonathan a   Yang, Yongping a   Zhou, Tongqing a   Zhu, Jiang a   Vicic, David A f,g   Debnath, Asim K h   Shapiro, Lawrence a,i   Bewley, Carole A d   Mascola, John R a   Sodroski, Joseph G b,c   Kwong, Peter D a  


Author keywords

Conformational equilibrium; Viral evasion; X ray crystallography

Indexed keywords

CD4 ANTIGEN; GLYCOPROTEIN GP 120;

EID: 84859561617     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1112391109     Document Type: Article
Times cited : (210)

References (46)
  • 1
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • DOI 10.1146/annurev.biochem.70.1.777
    • Eckert DM, Kim PS (2001) Mechanisms of viral membrane fusion and its inhibition. Annu Rev Biochem 70:777-810. (Pubitemid 32662225)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 2
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • DOI 10.1038/nrm1076
    • Colman PM, Lawrence MC (2003) The structural biology of type I viral membrane fusion. Nat Rev Mol Cell Biol 4:309-319. (Pubitemid 36383957)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 3
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • DOI 10.1126/science.280.5371.1884
    • Wyatt R, Sodroski J (1998) The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens. Science 280:1884-1888. (Pubitemid 28299385)
    • (1998) Science , vol.280 , Issue.5371 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 4
    • 0032529071 scopus 로고    scopus 로고
    • HIV gp120: Double lock strategy foils host defences
    • Sattentau QJ (1998) HIV gp120: Double lock strategy foils host defences. Structure 6: 945-949.
    • (1998) Structure , vol.6 , pp. 945-949
    • Sattentau, Q.J.1
  • 5
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease
    • DOI 10.1146/annurev.immunol.17.1.657
    • Berger EA, Murphy PM, Farber JM (1999) Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease. Annu Rev Immunol 17:657-700. (Pubitemid 29241137)
    • (1999) Annual Review of Immunology , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 7
    • 78650426126 scopus 로고    scopus 로고
    • Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure
    • Wu SR, et al. (2010) Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure. Proc Natl Acad Sci USA 107:18844-18849.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 18844-18849
    • Wu, S.R.1
  • 8
    • 78651241895 scopus 로고    scopus 로고
    • Molecular architectures of trimeric SIV and HIV-1 envelope glycoproteins on intact viruses: Strain-dependent variation in quaternary structure
    • White TA, et al. (2010) Molecular architectures of trimeric SIV and HIV-1 envelope glycoproteins on intact viruses: Strain-dependent variation in quaternary structure. PLoS Pathog 6:e1001249.
    • (2010) PLoS Pathog , vol.6
    • White, T.A.1
  • 9
    • 79952368717 scopus 로고    scopus 로고
    • Structural comparison of HIV-1 envelope spikes with and without the V1/V2 loop
    • Hu G, Liu J, Taylor KA, Roux KH (2011) Structural comparison of HIV-1 envelope spikes with and without the V1/V2 loop. J Virol 85:2741-2750.
    • (2011) J Virol , vol.85 , pp. 2741-2750
    • Hu, G.1    Liu, J.2    Taylor, K.A.3    Roux, K.H.4
  • 10
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, Kim PS (1997) Core structure of gp41 from the HIV envelope glycoprotein. Cell 89:263-273. (Pubitemid 27199898)
    • (1997) Cell , vol.89 , Issue.2 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 11
    • 0030962291 scopus 로고    scopus 로고
    • Atomic structure of the ectodomain from HIV-1 gp41
    • DOI 10.1038/387426a0
    • WeissenhornW, Dessen A, Harrison SC, Skehel JJ, Wiley DC (1997) Atomic structure of the ectodomain from HIV-1 gp41. Nature 387:426-430. (Pubitemid 27227210)
    • (1997) Nature , vol.387 , Issue.6631 , pp. 426-430
    • Weissenhorn, W.1    Dessen, A.2    Harrison, S.C.3    Skehel, J.J.4    Wiley, D.C.5
  • 12
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp 120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • DOI 10.1038/31405
    • Kwong PD, et al. (1998) Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393:648-659. (Pubitemid 28289647)
    • (1998) Nature , vol.393 , Issue.6686 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 13
    • 0034482696 scopus 로고    scopus 로고
    • Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates
    • DOI 10.1016/S0969-2126(00)00547-5, PII S0969212600005475
    • Kwong PD, et al. (2000) Structures of HIV-1 gp120 envelope glycoproteins from laboratory- adapted and primary isolates. Structure 8:1329-1339. (Pubitemid 32149759)
    • (2000) Structure , vol.8 , Issue.12 , pp. 1329-1339
    • Kwong, P.D.1    Wyatt, R.2    Majeed, S.3    Robinson, J.4    Sweet, R.W.5    Sodroski, J.6    Hendrickson, W.A.7
  • 14
    • 27744597054 scopus 로고    scopus 로고
    • Structure of a V3-containing HIV-1 gp120 core
    • Huang CC, et al. (2005) Structure of a V3-containing HIV-1 gp120 core. Science 310: 1025-1028.
    • (2005) Science , vol.310 , pp. 1025-1028
    • Huang, C.C.1
  • 15
    • 34848868199 scopus 로고    scopus 로고
    • Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4
    • Huang CC, et al. (2007) Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4. Science 317:1930-1934.
    • (2007) Science , vol.317 , pp. 1930-1934
    • Huang, C.C.1
  • 16
    • 75749133275 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility
    • Pancera M, et al. (2010) Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility. Proc Natl Acad Sci USA 107:1166-1171.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 1166-1171
    • Pancera, M.1
  • 17
    • 13844302894 scopus 로고    scopus 로고
    • Structure of an unliganded simian immunodeficiency virus gp120 core
    • DOI 10.1038/nature03327
    • Chen B, et al. (2005) Structure of an unliganded simian immunodeficiency virus gp120 core. Nature 433:834-841. (Pubitemid 40314887)
    • (2005) Nature , vol.433 , Issue.7028 , pp. 834-841
    • Chen, B.1    Vogan, E.M.2    Gong, H.3    Skehel, J.J.4    Wiley, D.C.5    Harrison, S.C.6
  • 18
    • 0033548254 scopus 로고    scopus 로고
    • Probability analysis of variational crystallization and its application to gp120, the exterior envelope glycoprotein of type 1 human immunodeficiency virus (HIV-1)
    • Kwong PD, et al. (1999) Probability analysis of variational crystallization and its application to gp120, the exterior envelope glycoprotein of type 1 human immunodeficiency virus (HIV-1). J Biol Chem 274:4115-4123.
    • (1999) J Biol Chem , vol.274 , pp. 4115-4123
    • Kwong, P.D.1
  • 20
    • 70450182950 scopus 로고    scopus 로고
    • Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120
    • Chen L, et al. (2009) Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120. Science 326:1123-1127.
    • (2009) Science , vol.326 , pp. 1123-1127
    • Chen, L.1
  • 21
    • 77954943648 scopus 로고    scopus 로고
    • Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01
    • Zhou T, 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
  • 23
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, et al. (2009) Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326:285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1
  • 24
    • 67249085575 scopus 로고    scopus 로고
    • Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site
    • Dey B, et al. (2009) Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site. PLoS Pathog 5:e1000445.
    • (2009) PLoS Pathog , vol.5
    • Dey, B.1
  • 25
    • 13844267637 scopus 로고    scopus 로고
    • Determining the structure of an unliganded and fully glycosylated SIV gp120 envelope glycoprotein
    • DOI 10.1016/j.str.2004.12.004
    • Chen B, et al. (2005) Determining the structure of an unliganded and fully glycosylated SIV gp120 envelope glycoprotein. Structure 13:197-211. (Pubitemid 40247697)
    • (2005) Structure , vol.13 , Issue.2 , pp. 197-211
    • Chen, B.1    Vogan, E.M.2    Gong, H.3    Skehel, J.J.4    Wiley, D.C.5    Harrison, S.C.6
  • 26
    • 33745767712 scopus 로고    scopus 로고
    • Characterization of the multiple conformationai states of free monomeric and trimeric human immunodeficiency virus envelope glycoproteins after fixation by cross-linker
    • DOI 10.1128/JVI.00118-06
    • Yuan W, Bazick J, Sodroski J (2006) Characterization of the multiple conformational states of free monomeric and trimeric human immunodeficiency virus envelope glycoproteins after fixation by cross-linker. J Virol 80:6725-6737. (Pubitemid 44025172)
    • (2006) Journal of Virology , vol.80 , Issue.14 , pp. 6725-6737
    • Yuan, W.1    Bazick, J.2    Sodroski, J.3
  • 27
    • 77956819789 scopus 로고    scopus 로고
    • Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/deuterium exchange
    • Kong L, et al. (2010) Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/deuterium exchange. J Virol 84: 10311-10321.
    • (2010) J Virol , vol.84 , pp. 10311-10321
    • Kong, L.1
  • 29
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu X, et al. (2010) Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 329:856-861.
    • (2010) Science , vol.329 , pp. 856-861
    • Wu, X.1
  • 30
    • 0036776445 scopus 로고    scopus 로고
    • Mutagenic stabilization and/or disruption of a CD4-bound state reveals distinct conformations of the human immunodeficiency virus type 1 gp120 envelope glycoprotein
    • Xiang SH, et al. (2002) Mutagenic stabilization and/or disruption of a CD4-bound state reveals distinct conformations of the human immunodeficiency virus type 1 gp120 envelope glycoprotein. J Virol 76:9888-9899.
    • (2002) J Virol , vol.76 , pp. 9888-9899
    • Xiang, S.H.1
  • 31
    • 23844440296 scopus 로고    scopus 로고
    • Identification of N-phenyl-N′-(2,2,6,6-tetramethyl-piperidin-4-yl)- oxalamides as a new class of HIV-1 entry inhibitors that prevent gp120 binding to CD4
    • DOI 10.1016/j.virol.2005.06.008, PII S0042682205003363
    • Zhao Q, et al. (2005) Identification of N-phenyl-N′-(2,2,6,6- tetramethyl-piperidin-4-yl)- oxalamides as a new class of HIV-1 entry inhibitors that prevent gp120 binding to CD4. Virology 339:213-225. (Pubitemid 41169789)
    • (2005) Virology , vol.339 , Issue.2 , pp. 213-225
    • Zhao, Q.1    Ma, L.2    Jiang, S.3    Lu, H.4    Liu, S.5    He, Y.6    Strick, N.7    Neamati, N.8    Debnath, A.K.9
  • 32
    • 55249083812 scopus 로고    scopus 로고
    • Small-molecule CD4 mimics interact with a highly conserved pocket on HIV-1 gp120
    • Madani N, et al. (2008) Small-molecule CD4 mimics interact with a highly conserved pocket on HIV-1 gp120. Structure 16:1689-1701.
    • (2008) Structure , vol.16 , pp. 1689-1701
    • Madani, N.1
  • 34
    • 0035131175 scopus 로고    scopus 로고
    • Increased neutralization sensitivity of CD4-independent human immunodeficiency virus variants
    • DOI 10.1128/JVI.75.5.2041-2050.2001
    • Kolchinsky P, Kiprilov E, Sodroski J (2001) Increased neutralization sensitivity of CD4- independent human immunodeficiency virus variants. J Virol 75:2041-2050. (Pubitemid 32147543)
    • (2001) Journal of Virology , vol.75 , Issue.5 , pp. 2041-2050
    • Kolchinsky, P.1    Kiprilov, E.2    Sodroski, J.3
  • 35
    • 0027194743 scopus 로고
    • Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions
    • Wyatt R, et al. (1993) Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions. J Virol 67:4557-4565. (Pubitemid 23215934)
    • (1993) Journal of Virology , vol.67 , Issue.8 , pp. 4557-4565
    • Wyatt, R.1    Sullivan, N.2    Thali, M.3    Repke, H.4    Ho, D.5    Robinson, J.6    Posner, M.7    Sodroski, J.8
  • 36
    • 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, et al. (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. (Pubitemid 27492434)
    • (1997) Journal of Virology , vol.71 , Issue.12 , pp. 9808-9812
    • Cao, J.1    Sullivan, N.2    Desjardin, E.3    Parolin, C.4    Robinson, J.5    Wyatt, R.6    Sodroski, J.7
  • 37
    • 69249202492 scopus 로고    scopus 로고
    • Transitions to and from the CD4-bound conformation are modulated by a single-residue change in the human immunodeficiency virus type 1 gp120 inner domain
    • Kassa A, et al. (2009) Transitions to and from the CD4-bound conformation are modulated by a single-residue change in the human immunodeficiency virus type 1 gp120 inner domain. J Virol 83:8364-8378.
    • (2009) J Virol , vol.83 , pp. 8364-8378
    • Kassa, A.1
  • 38
    • 77949401834 scopus 로고    scopus 로고
    • A V3 loop-dependent gp120 element disrupted by CD4 binding stabilizes the human immunodeficiency virus envelope glycoprotein trimer
    • Xiang SH, et al. (2010) A V3 loop-dependent gp120 element disrupted by CD4 binding stabilizes the human immunodeficiency virus envelope glycoprotein trimer. J Virol 84:3147-3161.
    • (2010) J Virol , vol.84 , pp. 3147-3161
    • Xiang, S.H.1
  • 40
    • 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 SM, et al. (2010) 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 84:11200-11209.
    • (2010) J Virol , vol.84 , pp. 11200-11209
    • O'Rourke, S.M.1
  • 41
    • 79551700244 scopus 로고    scopus 로고
    • A conserved determinant in the V1 loop of HIV-1 modulates the V3 loop to prime low CD4 use and macrophage infection
    • Musich T, et al. (2011) A conserved determinant in the V1 loop of HIV-1 modulates the V3 loop to prime low CD4 use and macrophage infection. J Virol 85:2397-2405.
    • (2011) J Virol , vol.85 , pp. 2397-2405
    • Musich, T.1
  • 42
    • 33644782704 scopus 로고    scopus 로고
    • Sequential CD134-CXCR4 interactions in feline immunodeficiency virus (FIV): Soluble CD134 activates FIV Env for CXCR4-dependent entry and reveals a cryptic neutralization epitope
    • DOI 10.1128/JVI.80.6.3088-3091.2006
    • de Parseval A, Grant CK, Sastry KJ, Elder JH (2006) Sequential CD134-CXCR4 interactions in feline immunodeficiency virus (FIV): Soluble CD134 activates FIV Env for CXCR4-dependent entry and reveals a cryptic neutralization epitope. J Virol 80:3088-3091. (Pubitemid 43346405)
    • (2006) Journal of Virology , vol.80 , Issue.6 , pp. 3088-3091
    • De Parseval, A.1    Grant, C.K.2    Sastry, K.J.3    Elder, J.H.4
  • 44
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 46
    • 73949127978 scopus 로고    scopus 로고
    • Tiered categorization of a diverse panel of HIV-1 Env pseudoviruses for assessment of neutralizing antibodies
    • Seaman MS, et al. (2010) Tiered categorization of a diverse panel of HIV-1 Env pseudoviruses for assessment of neutralizing antibodies. J Virol 84:1439-1452.
    • (2010) J Virol , vol.84 , pp. 1439-1452
    • Seaman, M.S.1


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