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Volumn 111, Issue 52, 2014, Pages 18542-18547

Stable, uncleaved HIV-1 envelope glycoprotein gp140 forms a tightly folded trimer with a native-like structure

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; FURIN; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 140; GLYCOPROTEIN GP 41; SOLUBLE CD4 ANTIGEN; GP140 ENVELOPE PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; VIRUS ENVELOPE PROTEIN;

EID: 84923154103     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1422269112     Document Type: Article
Times cited : (56)

References (44)
  • 1
    • 26944466459 scopus 로고    scopus 로고
    • Mechanism of membrane fusion by viral envelope proteins
    • Harrison SC (2005) Mechanism of membrane fusion by viral envelope proteins. Adv Virus Res 64:231-261.
    • (2005) Adv Virus Res , vol.64 , pp. 231-261
    • Harrison, S.C.1
  • 2
    • 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(2):263-273.
    • (1997) Cell , vol.89 , Issue.2 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 4
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan DC, Kim PS (1998) HIV entry and its inhibition. Cell 93(5):681-684.
    • (1998) Cell , vol.93 , Issue.5 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 5
    • 0038187684 scopus 로고    scopus 로고
    • Novel therapies based on mechanisms of HIV-1 cell entry
    • Kilby JM, Eron JJ (2003) Novel therapies based on mechanisms of HIV-1 cell entry. N Engl J Med 348(22):2228-2238.
    • (2003) N Engl J Med , vol.348 , Issue.22 , pp. 2228-2238
    • Kilby, J.M.1    Eron, J.J.2
  • 6
    • 41649090223 scopus 로고    scopus 로고
    • A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies
    • Frey G, et al. (2008) A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies. Proc Natl Acad Sci USA 105(10):3739-3744.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.10 , pp. 3739-3744
    • Frey, G.1
  • 7
    • 73949133588 scopus 로고    scopus 로고
    • Role of HIV membrane in neutralization by two broadly neutralizing antibodies
    • Alam SM, et al. (2009) Role of HIV membrane in neutralization by two broadly neutralizing antibodies. Proc Natl Acad Sci USA 106(48):20234-20239.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.48 , pp. 20234-20239
    • Alam, S.M.1
  • 8
    • 84891680667 scopus 로고    scopus 로고
    • Mechanism of HIV-1 neutralization by antibodies targeting a membrane-proximal region of gp41
    • Chen J, et al. (2014) Mechanism of HIV-1 neutralization by antibodies targeting a membrane-proximal region of gp41. J Virol 88(2):1249-1258.
    • (2014) J Virol , vol.88 , Issue.2 , pp. 1249-1258
    • Chen, J.1
  • 9
    • 84883796903 scopus 로고    scopus 로고
    • Antibodies in HIV-1 vaccine development and therapy
    • Klein F, et al. (2013) Antibodies in HIV-1 vaccine development and therapy. Science 341(6151):1199-1204.
    • (2013) Science , vol.341 , Issue.6151 , pp. 1199-1204
    • Klein, F.1
  • 10
    • 84883187027 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies and the search for an HIV-1 vaccine: The end of the beginning
    • Kwong PD, Mascola JR, Nabel GJ (2013) Broadly neutralizing antibodies and the search for an HIV-1 vaccine: The end of the beginning. Nat Rev Immunol 13(9):693-701.
    • (2013) Nat Rev Immunol , vol.13 , Issue.9 , pp. 693-701
    • Kwong, P.D.1    Mascola, J.R.2    Nabel, G.J.3
  • 11
    • 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 JM, et al. (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(2):627-643.
    • (2000) J Virol , vol.74 , Issue.2 , pp. 627-643
    • Binley, J.M.1
  • 12
    • 33847293391 scopus 로고    scopus 로고
    • Specific amino acids in the N-terminus of the gp41 ectodomain contribute to the stabilization of a soluble, cleaved gp140 envelope glycoprotein from human immunodeficiency virus type 1
    • Dey AK, David KB, Klasse PJ, Moore JP (2007) Specific amino acids in the N-terminus of the gp41 ectodomain contribute to the stabilization of a soluble, cleaved gp140 envelope glycoprotein from human immunodeficiency virus type 1. Virology 360(1):199-208.
    • (2007) Virology , vol.360 , Issue.1 , pp. 199-208
    • Dey, A.K.1    David, K.B.2    Klasse, P.J.3    Moore, J.P.4
  • 13
    • 84884678235 scopus 로고    scopus 로고
    • A next-generation cleaved, soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not nonneutralizing antibodies
    • Sanders RW, et al. (2013) A next-generation cleaved, soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not nonneutralizing antibodies. PLoS Pathog 9(9):e1003618.
    • (2013) PLoS Pathog , vol.9 , Issue.9 , pp. e1003618
    • Sanders, R.W.1
  • 14
    • 84887307095 scopus 로고    scopus 로고
    • Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation
    • Ringe RP, et al. (2013) Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation. Proc Natl Acad Sci USA 110(45):18256-18261.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.45 , pp. 18256-18261
    • Ringe, R.P.1
  • 15
    • 84890858459 scopus 로고    scopus 로고
    • Crystal structure of a soluble cleaved HIV-1 envelope trimer
    • Julien JP, et al. (2013) Crystal structure of a soluble cleaved HIV-1 envelope trimer. Science 342(6165):1477-1483.
    • (2013) Science , vol.342 , Issue.6165 , pp. 1477-1483
    • Julien, J.P.1
  • 16
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • Lyumkis D, et al. (2013) Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science 342(6165):1484-1490.
    • (2013) Science , vol.342 , Issue.6165 , pp. 1484-1490
    • Lyumkis, D.1
  • 17
    • 46449100666 scopus 로고    scopus 로고
    • Viral membrane fusion
    • Harrison SC (2008) Viral membrane fusion. Nat Struct Mol Biol 15(7):690-698.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.7 , pp. 690-698
    • Harrison, S.C.1
  • 18
    • 84904127504 scopus 로고    scopus 로고
    • CD4-induced activation in a soluble HIV-1 Env trimer
    • Guttman M, et al. (2014) CD4-induced activation in a soluble HIV-1 Env trimer. Structure 22(7):974-984.
    • (2014) Structure , vol.22 , Issue.7 , pp. 974-984
    • Guttman, M.1
  • 19
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding
    • Sattentau QJ, Moore JP (1991) Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding. J ExpMed 174(2):407-415.
    • (1991) J ExpMed , vol.174 , Issue.2 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 20
    • 0027488547 scopus 로고
    • Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding
    • Sattentau QJ, Moore JP, Vignaux F, Traincard F, Poignard P (1993) Conformational changes induced in the envelope glycoproteins of the human and simian immunodeficiency viruses by soluble receptor binding. J Virol 67(12):7383-7393.
    • (1993) J Virol , vol.67 , Issue.12 , pp. 7383-7393
    • Sattentau, Q.J.1    Moore, J.P.2    Vignaux, F.3    Traincard, F.4    Poignard, P.5
  • 21
    • 0034255034 scopus 로고    scopus 로고
    • Energetics of the HIV gp120-CD4 binding reaction
    • Myszka DG, et al. (2000) Energetics of the HIV gp120-CD4 binding reaction. Proc Natl Acad Sci USA 97(16):9026-9031.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.16 , pp. 9026-9031
    • Myszka, D.G.1
  • 22
    • 13844302894 scopus 로고    scopus 로고
    • Structure of an unliganded simian immunodeficiency virus gp120 core
    • Chen B, et al. (2005) Structure of an unliganded simian immunodeficiency virus gp120 core. Nature 433(7028):834-841.
    • (2005) Nature , vol.433 , Issue.7028 , pp. 834-841
    • Chen, B.1
  • 23
    • 84864365540 scopus 로고    scopus 로고
    • HIV-1 envelope trimer elicits more potent neutralizing antibody responses than monomeric gp120
    • Kovacs JM, et al. (2012) HIV-1 envelope trimer elicits more potent neutralizing antibody responses than monomeric gp120. Proc Natl Acad Sci USA 109(30):12111-12116.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.30 , pp. 12111-12116
    • Kovacs, J.M.1
  • 24
    • 84875034460 scopus 로고    scopus 로고
    • Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9
    • Julien JP, et al. (2013) Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9. Proc Natl Acad Sci USA 110(11):4351-4356.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.11 , pp. 4351-4356
    • Julien, J.P.1
  • 25
    • 78650833474 scopus 로고    scopus 로고
    • Comparative magnitude of cross-strain conservation of HIV variable loop neutralization epitopes
    • Swetnam J, Shmelkov E, Zolla-Pazner S, Cardozo T (2010) Comparative magnitude of cross-strain conservation of HIV variable loop neutralization epitopes. PLoS ONE 5(12):e15994.
    • (2010) PLoS ONE , vol.5 , Issue.12 , pp. e15994
    • Swetnam, J.1    Shmelkov, E.2    Zolla-Pazner, S.3    Cardozo, T.4
  • 26
    • 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, et al. (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(10):5205-5215.
    • (2004) J Virol , vol.78 , Issue.10 , pp. 5205-5215
    • Pinter, A.1
  • 27
    • 54949111659 scopus 로고    scopus 로고
    • Neutralizing activity of antibodies to the V3 loop region of HIV-1 gp120 relative to their epitope fine specificity
    • Pantophlet R, Wrin T, Cavacini LA, Robinson JE, Burton DR (2008) Neutralizing activity of antibodies to the V3 loop region of HIV-1 gp120 relative to their epitope fine specificity. Virology 381(2):251-260.
    • (2008) Virology , vol.381 , Issue.2 , pp. 251-260
    • Pantophlet, R.1    Wrin, T.2    Cavacini, L.A.3    Robinson, J.E.4    Burton, D.R.5
  • 28
    • 78649861760 scopus 로고    scopus 로고
    • Distinct conformational states of HIV-1 gp41 are recognized by neutralizing and non-neutralizing antibodies
    • Frey G, et al. (2010) Distinct conformational states of HIV-1 gp41 are recognized by neutralizing and non-neutralizing antibodies. Nat Struct Mol Biol 17(12):1486-1491.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.12 , pp. 1486-1491
    • Frey, G.1
  • 29
    • 0031985314 scopus 로고    scopus 로고
    • Spontaneous mutations in the env gene of the human immunodeficiency virus type 1 NDK isolate are associated with a CD4-independent entry phenotype
    • Dumonceaux J, et al. (1998) Spontaneous mutations in the env gene of the human immunodeficiency virus type 1 NDK isolate are associated with a CD4-independent entry phenotype. J Virol 72(1):512-519.
    • (1998) J Virol , vol.72 , Issue.1 , pp. 512-519
    • Dumonceaux, J.1
  • 30
    • 84908379850 scopus 로고    scopus 로고
    • Characterization and Immunogenicity of a Novel Mosaic M HIV-1:Gp140
    • Nkolola JP, et al. (2014) Characterization and Immunogenicity of a Novel Mosaic M HIV-1:gp140. J Virol 88(17):9538-9552.
    • (2014) J Virol , vol.88 , Issue.17 , pp. 9538-9552
    • Nkolola, J.P.1
  • 31
    • 84883308389 scopus 로고    scopus 로고
    • Influences on trimerization and aggregation of soluble, cleaved HIV-1 SOSIP envelope glycoprotein
    • Klasse PJ, et al. (2013) Influences on trimerization and aggregation of soluble, cleaved HIV-1 SOSIP envelope glycoprotein. J Virol 87(17):9873-9885.
    • (2013) J Virol , vol.87 , Issue.17 , pp. 9873-9885
    • Klasse, P.J.1
  • 32
    • 84890859441 scopus 로고    scopus 로고
    • Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer
    • Lyumkis D, et al. (2013) Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer. Science 342(6165):1484-1490.
    • (2013) Science , vol.342 , Issue.6165 , pp. 1484-1490
    • Lyumkis, D.1
  • 33
    • 84909640954 scopus 로고    scopus 로고
    • Structure and immune recognition of trimeric pre-fusion HIV-1 Env
    • Pancera M, et al. (2014) Structure and immune recognition of trimeric pre-fusion HIV-1 Env. Nature 514(7523):455-461.
    • (2014) Nature , vol.514 , Issue.7523 , pp. 455-461
    • Pancera, M.1
  • 34
    • 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(1):145-156.
    • (2005) Virology , vol.332 , Issue.1 , pp. 145-156
    • Pancera, M.1    Wyatt, R.2
  • 35
    • 18844470928 scopus 로고    scopus 로고
    • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
    • Chen J, et al. (1998) Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95(3):409-417.
    • (1998) Cell , vol.95 , Issue.3 , pp. 409-417
    • Chen, J.1
  • 36
    • 0037018921 scopus 로고    scopus 로고
    • Conserved structures exposed in HIV-1 envelope glycoproteins stabilized by flexible linkers as potent entry inhibitors and potential immunogens
    • Chow YH, et al. (2002) Conserved structures exposed in HIV-1 envelope glycoproteins stabilized by flexible linkers as potent entry inhibitors and potential immunogens. Biochemistry 41(22):7176-7182.
    • (2002) Biochemistry , vol.41 , Issue.22 , pp. 7176-7182
    • Chow, Y.H.1
  • 37
    • 84886888823 scopus 로고    scopus 로고
    • A functional interaction between gp41 and gp120 is observed for monomeric but not oligomeric, uncleaved HIV-1 Env gp140
    • Guttman M, Lee KK (2013) A functional interaction between gp41 and gp120 is observed for monomeric but not oligomeric, uncleaved HIV-1 Env gp140. J Virol 87(21):11462-11475.
    • (2013) J Virol , vol.87 , Issue.21 , pp. 11462-11475
    • Guttman, M.1    Lee, K.K.2
  • 38
    • 84864603281 scopus 로고    scopus 로고
    • Structural mechanism of trimeric HIV-1 envelope glycoprotein activation
    • Tran EE, et al. (2012) Structural mechanism of trimeric HIV-1 envelope glycoprotein activation. PLoS Pathog 8(7):e1002797.
    • (2012) PLoS Pathog , vol.8 , Issue.7 , pp. e1002797
    • Tran, E.E.1
  • 39
    • 0027168953 scopus 로고
    • Adaptation of two primary human immunodeficiency virus type 1 isolates to growth in transformed T cell lines correlates with alterations in the responses of their envelope glycoproteins to soluble CD4
    • Moore JP, et al. (1993) Adaptation of two primary human immunodeficiency virus type 1 isolates to growth in transformed T cell lines correlates with alterations in the responses of their envelope glycoproteins to soluble CD4. AIDS Res Hum Retroviruses 9(6):529-539.
    • (1993) AIDS Res Hum Retroviruses , vol.9 , Issue.6 , pp. 529-539
    • Moore, J.P.1
  • 40
    • 0026601827 scopus 로고
    • Virions of primary human immunodeficiency virus type 1 isolates resistant to soluble CD4 (sCD4) neutralization differ in sCD4 binding and glycoprotein gp120 retention from sCD4-sensitive isolates
    • Moore JP, McKeating JA, Huang YX, Ashkenazi A, Ho DD (1992) Virions of primary human immunodeficiency virus type 1 isolates resistant to soluble CD4 (sCD4) neutralization differ in sCD4 binding and glycoprotein gp120 retention from sCD4-sensitive isolates. J Virol 66(1):235-243.
    • (1992) J Virol , vol.66 , Issue.1 , pp. 235-243
    • Moore, J.P.1    McKeating, J.A.2    Huang, Y.X.3    Ashkenazi, A.4    Ho, D.D.5
  • 41
    • 0032990223 scopus 로고    scopus 로고
    • Stable exposure of the coreceptor-binding site in a CD4-independent HIV-1 envelope protein
    • Hoffman TL, et al. (1999) Stable exposure of the coreceptor-binding site in a CD4-independent HIV-1 envelope protein. Proc Natl Acad Sci USA 96(11):6359-6364.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.11 , pp. 6359-6364
    • Hoffman, T.L.1
  • 42
    • 29444439322 scopus 로고    scopus 로고
    • Single particle reconstructions of the transferrin-transferrin receptor complex obtained with different specimen preparation techniques
    • Cheng Y, et al. (2006) Single particle reconstructions of the transferrin-transferrin receptor complex obtained with different specimen preparation techniques. J Mol Biol 355(5):1048-1065.
    • (2006) J Mol Biol , vol.355 , Issue.5 , pp. 1048-1065
    • Cheng, Y.1
  • 43
    • 84901499773 scopus 로고    scopus 로고
    • Stable 293 T and CHO cell lines expressing cleaved, stable HIV-1 envelope glycoprotein trimers for structural and vaccine studies
    • Chung NP, et al. (2014) Stable 293 T and CHO cell lines expressing cleaved, stable HIV-1 envelope glycoprotein trimers for structural and vaccine studies. Retrovirology 11(1):33.
    • (2014) Retrovirology , vol.11 , Issue.1 , pp. 33
    • Chung, N.P.1
  • 44
    • 84921564277 scopus 로고    scopus 로고
    • Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single particle electron microscopy
    • Murin CD, et al. (2014) Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single particle electron microscopy. J Virol 88(17):10177-10188.
    • (2014) J Virol , vol.88 , Issue.17 , pp. 10177-10188
    • Murin, C.D.1


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