메뉴 건너뛰기




Volumn 90, Issue 19, 2016, Pages 8395-8409

A highly conserved gp120 inner domain residue modulates Env conformation and trimer stability

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; GLYCOPROTEIN GP 120; GP120 PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; PROTEIN BINDING;

EID: 84990243334     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01068-16     Document Type: Article
Times cited : (13)

References (50)
  • 1
    • 0026069632 scopus 로고
    • Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein
    • Helseth E, Olshevsky U, Furman C, Sodroski J. 1991. Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein. J Virol 65: 2119-2123
    • (1991) J Virol , vol.65 , pp. 2119-2123
    • Helseth, E.1    Olshevsky, U.2    Furman, C.3    Sodroski, J.4
  • 2
    • 0021751840 scopus 로고
    • The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus
    • Dalgleish AG, Beverley PC, Clapham PR, Crawford DH, Greaves MF, Weiss RA. 1984. The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature 312:763-767. http://dx.doi.org/10.1038/312763a0
    • (1984) Nature , vol.312 , pp. 763-767
    • Dalgleish, A.G.1    Beverley, P.C.2    Clapham, P.R.3    Crawford, D.H.4    Greaves, M.F.5    Weiss, R.A.6
  • 4
    • 0030018156 scopus 로고    scopus 로고
    • CC CKR5: a RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1
    • Alkhatib G, Combadiere C, Broder CC, Feng Y, Kennedy PE, Murphy PM, Berger EA. 1996. CC CKR5: a RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1. Science 272: 1955-1958. http://dx.doi.org/10.1126/science.272.5270.1955
    • (1996) Science , vol.272 , pp. 1955-1958
    • Alkhatib, G.1    Combadiere, C.2    Broder, C.C.3    Feng, Y.4    Kennedy, P.E.5    Murphy, P.M.6    Berger, E.A.7
  • 7
    • 0030604727 scopus 로고    scopus 로고
    • A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors
    • Doranz BJ, Rucker J, Yi Y, Smyth RJ, Samson M, Peiper SC, Parmentier M, Collman RG, Doms RW. 1996. A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors. Cell 85:1149-1158. http://dx.doi.org/10.1016/S0092-8674(00)81314-8
    • (1996) Cell , vol.85 , pp. 1149-1158
    • Doranz, B.J.1    Rucker, J.2    Yi, Y.3    Smyth, R.J.4    Samson, M.5    Peiper, S.C.6    Parmentier, M.7    Collman, R.G.8    Doms, R.W.9
  • 9
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng Y, Broder CC, Kennedy PE, Berger EA. 1996. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 272:872-877. http://dx.doi.org/10.1126/science.272.5263.872
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 12
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M, Blacklow SC, Kim PS. 1995. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat Struct Biol 2:1075-1082. http://dx.doi.org/10.1038/nsb1295-1075
    • (1995) Nat Struct Biol , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 13
    • 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. http://dx.doi.org/10.1016/S0092-8674(00)80205-6
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 15
    • 77749329921 scopus 로고    scopus 로고
    • Topological layers in the HIV-1 gp120 inner domain regulate gp41 interaction and CD4-triggered conformational transitions
    • Finzi A, Xiang SH, Pacheco B, Wang L, Haight J, Kassa A, Danek B, Pancera M, Kwong PD, Sodroski J. 2010. Topological layers in the HIV-1 gp120 inner domain regulate gp41 interaction and CD4-triggered conformational transitions. Mol Cell 37:656-667. http://dx.doi.org/10.1016/j.molcel.2010.02.012
    • (2010) Mol Cell , vol.37 , pp. 656-667
    • Finzi, A.1    Xiang, S.H.2    Pacheco, B.3    Wang, L.4    Haight, J.5    Kassa, A.6    Danek, B.7    Pancera, M.8    Kwong, P.D.9    Sodroski, J.10
  • 16
    • 84874738557 scopus 로고    scopus 로고
    • The highly conserved layer-3 component of the HIV-1 gp120 inner domain is critical for CD4-required conformational transitions
    • Desormeaux A, Coutu M, Medjahed H, Pacheco B, Herschhorn A, Gu C, Xiang SH, Mao Y, Sodroski J, Finzi A. 2013. The highly conserved layer-3 component of the HIV-1 gp120 inner domain is critical for CD4-required conformational transitions. J Virol 87:2549-2562. http://dx.doi.org/10.1128/JVI.03104-12
    • (2013) J Virol , vol.87 , pp. 2549-2562
    • Desormeaux, A.1    Coutu, M.2    Medjahed, H.3    Pacheco, B.4    Herschhorn, A.5    Gu, C.6    Xiang, S.H.7    Mao, Y.8    Sodroski, J.9    Finzi, A.10
  • 17
    • 84919429656 scopus 로고    scopus 로고
    • The HIV-1 gp120 CD4-bound conformation is preferentially targeted by ADCC-mediating antibodies in sera from HIV-1-infected individuals
    • Veillette M, Coutu M, Richard J, Batraville LA, Dagher O, Bernard N, Tremblay C, Kaufmann DE, Roger M, Finzi A. 2014. The HIV-1 gp120 CD4-bound conformation is preferentially targeted by ADCC-mediating antibodies in sera from HIV-1-infected individuals. J Virol 89:545-551. http://dx.doi.org/10.1128/JVI.02868-14
    • (2014) J Virol , vol.89 , pp. 545-551
    • Veillette, M.1    Coutu, M.2    Richard, J.3    Batraville, L.A.4    Dagher, O.5    Bernard, N.6    Tremblay, C.7    Kaufmann, D.E.8    Roger, M.9    Finzi, A.10
  • 21
    • 66149136375 scopus 로고    scopus 로고
    • Identification of a human immunodeficiency virus (HIV-1) envelope glycoprotein variant resistant to cold inactivation
    • Kassa A, Finzi A, Pancera M, Courter JR, Smith AB, III, Sodroski J. 2009. Identification of a human immunodeficiency virus (HIV-1) envelope glycoprotein variant resistant to cold inactivation. J Virol 83:4476-4488
    • (2009) J Virol , vol.83 , pp. 4476-4488
    • Kassa, A.1    Finzi, A.2    Pancera, M.3    Courter, J.R.4    Smith I.I.I, A.B.5    Sodroski, J.6
  • 23
    • 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, Finzi A, Pacheco B, Alexander K, Yuan W, Rizzuto C, Huang CC, Kwong PD, Sodroski J. 2010. A V3 loop-dependent gp120 element disrupted by CD4 binding stabilizes the human immunodeficiency virus envelope glycoprotein trimer. J Virol 84:3147-3161. http://dx.doi.org/10.1128/JVI.02587-09
    • (2010) J Virol , vol.84 , pp. 3147-3161
    • Xiang, S.H.1    Finzi, A.2    Pacheco, B.3    Alexander, K.4    Yuan, W.5    Rizzuto, C.6    Huang, C.C.7    Kwong, P.D.8    Sodroski, J.9
  • 24
    • 84866153322 scopus 로고    scopus 로고
    • Lineage-specific differences between human and simian immunodeficiency virus regulation of gp120 trimer association and CD4 binding
    • Finzi A, Pacheco B, Xiang SH, Pancera M, Herschhorn A, Wang L, Zeng X, Desormeaux A, Kwong PD, Sodroski J. 2012. Lineage-specific differences between human and simian immunodeficiency virus regulation of gp120 trimer association and CD4 binding. J Virol 86:8974-8986. http://dx.doi.org/10.1128/JVI.01076-12
    • (2012) J Virol , vol.86 , pp. 8974-8986
    • Finzi, A.1    Pacheco, B.2    Xiang, S.H.3    Pancera, M.4    Herschhorn, A.5    Wang, L.6    Zeng, X.7    Desormeaux, A.8    Kwong, P.D.9    Sodroski, J.10
  • 25
    • 84875516588 scopus 로고    scopus 로고
    • The HIV-1 gp120 major variable regions modulate cold inactivation
    • Medjahed H, Pacheco B, Desormeaux A, Sodroski J, Finzi A. 2013. The HIV-1 gp120 major variable regions modulate cold inactivation. J Virol 87:4103-4111. http://dx.doi.org/10.1128/JVI.03124-12
    • (2013) J Virol , vol.87 , pp. 4103-4111
    • Medjahed, H.1    Pacheco, B.2    Desormeaux, A.3    Sodroski, J.4    Finzi, A.5
  • 26
    • 0033766295 scopus 로고    scopus 로고
    • Importance of membrane fusion mediated by human immunodeficiency virus envelope glycoproteins for lysis of primary CD4-positive T cells
    • LaBonte JA, Patel T, Hofmann W, Sodroski J. 2000. Importance of membrane fusion mediated by human immunodeficiency virus envelope glycoproteins for lysis of primary CD4-positive T cells. J Virol 74:10690-10698 http://dx.doi.org/10.1128/JVI.74.22.10690-10698.2000
    • (2000) J Virol , vol.74 , pp. 10690-10698
    • LaBonte, J.A.1    Patel, T.2    Hofmann, W.3    Sodroski, J.4
  • 27
    • 0031954686 scopus 로고    scopus 로고
    • Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1
    • Platt EJ, Wehrly K, Kuhmann SE, Chesebro B, Kabat D. 1998. Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1. J Virol 72:2855-2864
    • (1998) J Virol , vol.72 , pp. 2855-2864
    • Platt, E.J.1    Wehrly, K.2    Kuhmann, S.E.3    Chesebro, B.4    Kabat, D.5
  • 28
    • 0001720445 scopus 로고    scopus 로고
    • Numbering positions in HIV relative to HXB2CG
    • 3, Los Alamos National Laboratory, Los Alamos, NM
    • Korber B, Foley BT, Kuiken C, Pillai SK, Sodroski JG. 1998. Numbering positions in HIV relative to HXB2CG, p 102-111, vol III. In Human retroviruses and AIDS, vol III. Los Alamos National Laboratory, Los Alamos, NM
    • (1998) Human retroviruses and AIDS , vol.3 , pp. 102-111
    • Korber, B.1    Foley, B.T.2    Kuiken, C.3    Pillai, S.K.4    Sodroski, J.G.5
  • 29
    • 0019406057 scopus 로고
    • Characterization of the reverse transcriptase from a new retrovirus (HTLV) produced by a human cutaneous T-cell lymphoma cell line
    • Rho HM, Poiesz B, Ruscetti FW, Gallo RC. 1981. Characterization of the reverse transcriptase from a new retrovirus (HTLV) produced by a human cutaneous T-cell lymphoma cell line. Virology 112:355-360. http://dx.doi.org/10.1016/0042-6822(81)90642-5
    • (1981) Virology , vol.112 , pp. 355-360
    • Rho, H.M.1    Poiesz, B.2    Ruscetti, F.W.3    Gallo, R.C.4
  • 30
    • 84924985686 scopus 로고    scopus 로고
    • HIV-1 gp120 dimers decrease the overall affinity of gp120 preparations for CD4-induced ligands
    • Coutu M, Finzi A. 2015. HIV-1 gp120 dimers decrease the overall affinity of gp120 preparations for CD4-induced ligands. J Virol Methods 215-216: 37-44
    • (2015) J Virol Methods , vol.215-216 , pp. 37-44
    • Coutu, M.1    Finzi, A.2
  • 31
    • 77955093635 scopus 로고    scopus 로고
    • Conformational characterization of aberrant disulfide-linked HIV-1 gp120 dimers secreted from overexpressing cells
    • Finzi A, Pacheco B, Zeng X, Kwon YD, Kwong PD, Sodroski J. 2010. Conformational characterization of aberrant disulfide-linked HIV-1 gp120 dimers secreted from overexpressing cells. J Virol Methods 168: 155-161. http://dx.doi.org/10.1016/j.jviromet.2010.05.008
    • (2010) J Virol Methods , vol.168 , pp. 155-161
    • Finzi, A.1    Pacheco, B.2    Zeng, X.3    Kwon, Y.D.4    Kwong, P.D.5    Sodroski, J.6
  • 32
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors
    • Johnsson B, Lofas S, Lindquist G. 1991. Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal Biochem 198:268-277. http://dx.doi.org/10.1016/0003-2697(91)90424-R
    • (1991) Anal Biochem , vol.198 , pp. 268-277
    • Johnsson, B.1    Lofas, S.2    Lindquist, G.3
  • 34
    • 84878880620 scopus 로고    scopus 로고
    • Structural basis for highly effective HIV-1 neutralization by CD4-mimetic miniproteins revealed by 1.5 A cocrystal structure of gp120 and M48U1
    • Acharya P, Luongo TS, Louder MK, McKee K, Yang Y, Kwon YD, Mascola JR, Kessler P, Martin L, Kwong PD. 2013. Structural basis for highly effective HIV-1 neutralization by CD4-mimetic miniproteins revealed by 1.5 A cocrystal structure of gp120 and M48U1. Structure 21: 1018-1029. http://dx.doi.org/10.1016/j.str.2013.04.015
    • (2013) Structure , vol.21 , pp. 1018-1029
    • Acharya, P.1    Luongo, T.S.2    Louder, M.K.3    McKee, K.4    Yang, Y.5    Kwon, Y.D.6    Mascola, J.R.7    Kessler, P.8    Martin, L.9    Kwong, P.D.10
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, Carter CW, Jr. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2    Carter, C.W.3
  • 37
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ. 2007. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D Biol Crystallogr 63:32-41. http://dx.doi.org/10.1107/S0907444906045975
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 38
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50:760-763. http://dx.doi.org/10.1107/S0907444994003112
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 39
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53:240-255. http://dx.doi.org/10.1107/S0907444996012255
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 41
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60:2126-2132. http://dx.doi.org/10.1107/S0907444904019158
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 42
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley WC, White SH. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat Struct Biol 3:842-848. http://dx.doi.org/10.1038/nsb1096-842
    • (1996) Nat Struct Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 44
    • 0030043169 scopus 로고    scopus 로고
    • Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein
    • Moore JP, Sodroski J. 1996. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J Virol 70:1863-1872
    • (1996) J Virol , vol.70 , pp. 1863-1872
    • Moore, J.P.1    Sodroski, J.2
  • 47
    • 0042389489 scopus 로고    scopus 로고
    • Role of the gp120 inner domain beta-sandwich in the interaction between the human immunodeficiency virus envelope glycoprotein subunits
    • Yang X, Mahony E, Holm GH, Kassa A, Sodroski J. 2003. Role of the gp120 inner domain beta-sandwich in the interaction between the human immunodeficiency virus envelope glycoprotein subunits. Virology 313: 117-125. http://dx.doi.org/10.1016/S0042-6822(03)00273-3
    • (2003) Virology , vol.313 , pp. 117-125
    • Yang, X.1    Mahony, E.2    Holm, G.H.3    Kassa, A.4    Sodroski, J.5
  • 48
    • 84961231130 scopus 로고    scopus 로고
    • Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer
    • Lee JH, Ozorowski G, Ward AB. 2016. Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer. Science 351:1043-1048. http://dx.doi.org/10.1126/science.aad2450
    • (2016) Science , vol.351 , pp. 1043-1048
    • Lee, J.H.1    Ozorowski, G.2    Ward, A.B.3
  • 50
    • 0026597444 scopus 로고
    • Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger AT. 1992. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355:472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.