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Volumn 287, Issue 41, 2012, Pages 34558-34568

The M-T hook structure is critical for design of HIV-1 fusion inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-HIV ACTIVITY; BINDING AFFINITIES; BUNDLE FORMATION; CELL FUSIONS; FUSION INHIBITORS; HIGH RESOLUTION CRYSTAL STRUCTURE; KEY DETERMINANTS; N-TERMINALS; VIRUS ENTRY;

EID: 84867242967     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.390393     Document Type: Article
Times cited : (53)

References (45)
  • 1
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • DOI 10.1146/annurev.biochem.70.1.777
    • Eckert, D. M., and Kim, P. S. (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, P. M., and Lawrence, M. C. (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
  • 5
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., Fass, D., Berger, J. M., and Kim, P. S. (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
  • 7
    • 0030962291 scopus 로고    scopus 로고
    • Atomic structure of the ectodomain from HIV-1 gp41
    • DOI 10.1038/387426a0
    • Weissenhorn, W., Dessen, A., Harrison, S. C., Skehel, J. J., and Wiley, D. C. (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
  • 9
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • DOI 10.1016/S0092-8674(00)81430-0
    • Chan, D. C., and Kim, P. S. (1998) HIV entry and its inhibition. Cell 93, 681-684 (Pubitemid 28257575)
    • (1998) Cell , vol.93 , Issue.5 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 14
    • 79960463354 scopus 로고    scopus 로고
    • Multifaceted action of Fuzeon as virus-cell membrane fusion inhibitor
    • Ashkenazi, A., Wexler-Cohen, Y., and Shai, Y. (2011) Multifaceted action of Fuzeon as virus-cell membrane fusion inhibitor. Biochim. Biophys. Acta 1808, 2352-2358
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2352-2358
    • Ashkenazi, A.1    Wexler-Cohen, Y.2    Shai, Y.3
  • 15
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus types 1 resistance to gp41- derived inhibitory peptides
    • Rimsky, L. T., Shugars, D. C., and Matthews, T. J. (1998) Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J. Virol. 72, 986-993 (Pubitemid 28116876)
    • (1998) Journal of Virology , vol.72 , Issue.2 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 16
    • 0036090585 scopus 로고    scopus 로고
    • Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy
    • DOI 10.1128/AAC.46.6.1896-1905.2002
    • Wei, X., Decker, J. M., Liu, H., Zhang, Z., Arani, R. B., Kilby, J. M., Saag, M. S., Wu, X., Shaw, G. M., and Kappes, J. C. (2002) Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy. Antimicrob. Agents Chemother. 46, 1896-1905 (Pubitemid 34535213)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.6 , pp. 1896-1905
    • Wei, X.1    Decker, J.M.2    Liu, H.3    Zhang, Z.4    Arani, R.B.5    Kilby, J.M.6    Saag, M.S.7    Wu, X.8    Shaw, G.M.9    Kappes, J.C.10
  • 17
    • 4444375658 scopus 로고    scopus 로고
    • Resistance to enfuvirtide, the first HIV fusion inhibitor
    • DOI 10.1093/jac/dkh330
    • Greenberg, M. L., and Cammack, N. (2004) Resistance to enfuvirtide, the first HIV fusion inhibitor. J. Antimicrob. Chemother. 54, 333-340 (Pubitemid 39177450)
    • (2004) Journal of Antimicrobial Chemotherapy , vol.54 , Issue.2 , pp. 333-340
    • Greenberg, M.L.1    Cammack, N.2
  • 19
    • 79955701366 scopus 로고    scopus 로고
    • Inhibition of HIV-1 by fusion inhibitors
    • Eggink, D., Berkhout, B., and Sanders, R. W. (2010) Inhibition of HIV-1 by fusion inhibitors. Curr. Pharm. Des. 16, 3716-3728
    • (2010) Curr. Pharm. Des. , vol.16 , pp. 3716-3728
    • Eggink, D.1    Berkhout, B.2    Sanders, R.W.3
  • 20
    • 77950199930 scopus 로고    scopus 로고
    • Peptide-based inhibitors of the HIV envelope protein and other class i viral fusion proteins
    • Steffen, I., and Pöhlmann, S. (2010) Peptide-based inhibitors of the HIV envelope protein and other class I viral fusion proteins. Curr. Pharm. Des. 16, 1143-1158
    • (2010) Curr. Pharm. Des. , vol.16 , pp. 1143-1158
    • Steffen, I.1    Pöhlmann, S.2
  • 21
    • 84857363079 scopus 로고    scopus 로고
    • Is there a future for antiviral fusion inhibitors?
    • Berkhout, B., Eggink, D., and Sanders, R. W. (2012) Is there a future for antiviral fusion inhibitors? Curr. Opin. Virol. 2, 50-59
    • (2012) Curr. Opin. Virol. , vol.2 , pp. 50-59
    • Berkhout, B.1    Eggink, D.2    Sanders, R.W.3
  • 22
    • 45749112585 scopus 로고    scopus 로고
    • Identification of a critical motif for the human immunodeficiency virus type 1 (HIV-1) gp41 core structure: Implications for designing novel anti-HIV fusion inhibitors
    • DOI 10.1128/JVI.00319-08
    • He, Y., Cheng, J., Li, J., Qi, Z., Lu, H., Dong, M., Jiang, S., and Dai, Q. (2008) Identification of a critical motif for the human immunodeficiency virus type 1 (HIV-1) gp41 core structure. Implications for designing novel anti-HIV fusion inhibitors. J. Virol. 82, 6349-6358 (Pubitemid 351875113)
    • (2008) Journal of Virology , vol.82 , Issue.13 , pp. 6349-6358
    • He, Y.1    Cheng, J.2    Li, J.3    Qi, Z.4    Lu, H.5    Dong, M.6    Jiang, S.7    Dai, Q.8
  • 25
    • 84862001877 scopus 로고    scopus 로고
    • Discovery of critical residues for viral entry and inhibition through structural insight of HIV-1 fusion inhibitor CP621-652
    • Chong, H., Yao, X., Qiu, Z., Qin, B., Han, R., Waltersperger, S., Wang, M., Cui, S., and He, Y. (2012) Discovery of critical residues for viral entry and inhibition through structural insight of HIV-1 fusion inhibitor CP621-652. J. Biol. Chem. 287, 20281-20289
    • (2012) J. Biol. Chem. , vol.287 , pp. 20281-20289
    • Chong, H.1    Yao, X.2    Qiu, Z.3    Qin, B.4    Han, R.5    Waltersperger, S.6    Wang, M.7    Cui, S.8    He, Y.9
  • 26
    • 33646903467 scopus 로고    scopus 로고
    • Structurally altered peptides reveal an important role for N-terminal heptad repeat binding and stability in the inhibitory action of HIV-1 peptide DP178
    • DOI 10.1074/jbc.M512475200
    • Wexler-Cohen, Y., Johnson, B. T., Puri, A., Blumenthal, R., and Shai, Y. (2006) Structurally altered peptides reveal an important role for N-terminal heptad repeat binding and stability in the inhibitory action of HIV-1 peptide DP178. J. Biol. Chem. 281, 9005-9010 (Pubitemid 43864612)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9005-9010
    • Wexler-Cohen, Y.1    Johnson, B.T.2    Puri, A.3    Blumenthal, R.4    Shai, Y.5
  • 27
    • 34548481743 scopus 로고    scopus 로고
    • 574 in the cavity of HIV-1 Gp41 coiled-coil domain is critical for six-helix bundle stability and virus entry
    • DOI 10.1074/jbc.M703781200
    • He, Y., Liu, S., Jing, W., Lu, H., Cai, D., Chin, D. J., Debnath, A. K., Kirchhoff, F., and Jiang, S. (2007) Conserved residue Lys-574 in the cavity of HIV-1 Gp41 coiled-coil domain is critical for six-helix bundle stability and virus entry. J. Biol. Chem. 282, 25631-25639 (Pubitemid 47372795)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.35 , pp. 25631-25639
    • He, Y.1    Liu, S.2    Jing, W.3    Lu, H.4    Cai, D.5    Darin, J.C.6    Debnath, A.K.7    Kirchhoff, F.8    Jiang, S.9
  • 28
    • 55549105768 scopus 로고    scopus 로고
    • Conserved salt bridge between the N- and C-terminal heptad repeat regions of the human immunodeficiency virus type 1 gp41 core structure is critical for virus entry and inhibition
    • He, Y., Liu, S., Li, J., Lu, H., Qi, Z., Liu, Z., Debnath, A. K., and Jiang, S. (2008) Conserved salt bridge between the N- and C-terminal heptad repeat regions of the human immunodeficiency virus type 1 gp41 core structure is critical for virus entry and inhibition. J. Virol. 82, 11129-11139
    • (2008) J. Virol. , vol.82 , pp. 11129-11139
    • He, Y.1    Liu, S.2    Li, J.3    Lu, H.4    Qi, Z.5    Liu, Z.6    Debnath, A.K.7    Jiang, S.8
  • 29
    • 58149522849 scopus 로고    scopus 로고
    • Identification of critical antibody-binding sites in the HIV-1 gp41 six-helix bundle core as potential targets for HIV-1 fusion inhibitors
    • Li, J., Chen, X., Huang, J., Jiang, S., and Chen, Y. H. (2009) Identification of critical antibody-binding sites in the HIV-1 gp41 six-helix bundle core as potential targets for HIV-1 fusion inhibitors. Immunobiology 214, 51-60
    • (2009) Immunobiology , vol.214 , pp. 51-60
    • Li, J.1    Chen, X.2    Huang, J.3    Jiang, S.4    Chen, Y.H.5
  • 30
    • 0031743949 scopus 로고    scopus 로고
    • A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein
    • Jiang, S., Lin, K., and Lu, M. (1998) A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol. 72, 10213-10217 (Pubitemid 28520893)
    • (1998) Journal of Virology , vol.72 , Issue.12 , pp. 10213-10217
    • Jiang, S.1    Lin, K.2    Lu, M.3
  • 31
    • 77954059555 scopus 로고    scopus 로고
    • Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions
    • Buzon, V., Natrajan, G., Schibli, D., Campelo, F., Kozlov, M. M., and Weissenhorn, W. (2010) Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions. PLoS Pathog. 6, e1000880
    • (2010) PLoS Pathog. , vol.6
    • Buzon, V.1    Natrajan, G.2    Schibli, D.3    Campelo, F.4    Kozlov, M.M.5    Weissenhorn, W.6
  • 35
    • 0031798443 scopus 로고    scopus 로고
    • Mutational analysis of residues in the coiled-coil domain of human immunodeficiency virus type 1 transmembrane protein gp41
    • Weng, Y., and Weiss, C. D. (1998) Mutational analysis of residues in the coiled-coil domain of human immunodeficiency virus type 1 transmembrane protein gp41. J. Virol. 72, 9676-9682 (Pubitemid 28520831)
    • (1998) Journal of Virology , vol.72 , Issue.12 , pp. 9676-9682
    • Weng, Y.1    Weiss, C.D.2
  • 36
    • 0034701058 scopus 로고    scopus 로고
    • Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides
    • DOI 10.1021/bi9921687
    • Shu, W., Liu, J., Ji, H., Radigen, L., Jiang, S., and Lu, M. (2000) Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides. Biochemistry 39, 1634-1642 (Pubitemid 30108955)
    • (2000) Biochemistry , vol.39 , Issue.7 , pp. 1634-1642
    • Shu, W.1    Liu, J.2    Ji, H.3    Radigen, L.4    Jiang, S.5    Lu, M.6
  • 37
    • 0034023726 scopus 로고    scopus 로고
    • Structure-function studies of the self-assembly domain of the human immunodeficiency virus type 1 transmembrane protein gp41
    • DOI 10.1128/JVI.74.11.5368-5372.2000
    • Weng, Y., Yang, Z., and Weiss, C. D. (2000) Structure-function studies of the self-assembly domain of the human immunodeficiency virus type 1 transmembrane protein gp41. J. Virol. 74, 5368-5372 (Pubitemid 30313881)
    • (2000) Journal of Virology , vol.74 , Issue.11 , pp. 5368-5372
    • Weng, Y.1    Yang, Z.2    Weiss, C.D.3
  • 38
    • 0034759947 scopus 로고    scopus 로고
    • Structural and functional analysis of interhelical interactions in the human immunodeficiency virus type 1 gp41 envelope glycoprotein by alanine-scanning mutagenesis
    • DOI 10.1128/JVI.75.22.11146-11156.2001
    • Lu, M., Stoller, M. O., Wang, S., Liu, J., Fagan, M. B., and Nunberg, J. H. (2001) Structural and functional analysis of interhelical interactions in the human immunodeficiency virus type 1 gp41 envelope glycoprotein by alanine-scanning mutagenesis. J. Virol. 75, 11146-11156 (Pubitemid 33031581)
    • (2001) Journal of Virology , vol.75 , Issue.22 , pp. 11146-11156
    • Lu, M.1    Stoller, M.O.2    Wang, S.3    Liu, J.4    Fagan, M.B.5    Nunberg, J.H.6
  • 39
    • 33746838814 scopus 로고    scopus 로고
    • Characterization of the HIV N-terminal fusion peptide-containing region in context of key gp41 fusion conformations
    • DOI 10.1074/jbc.M603135200
    • Sackett, K., Wexler-Cohen, Y., and Shai, Y. (2006) Characterization of the HIV N-terminal fusion peptide-containing region in context of key gp41 fusion conformations. J. Biol. Chem. 281, 21755-21762 (Pubitemid 44181879)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.31 , pp. 21755-21762
    • Sackett, K.1    Wexler-Cohen, Y.2    Shai, Y.3
  • 40
    • 24944493173 scopus 로고    scopus 로고
    • Conformational changes in HIV-1 gp41 in the course of HIV-1 envelope glycoprotein-mediated fusion and inactivation
    • DOI 10.1021/bi051092d
    • Dimitrov, A. S., Louis, J. M., Bewley, C. A., Clore, G. M., and Blumenthal, R. (2005) Conformational changes in HIV-1 gp41 in the course of HIV-1 envelope glycoprotein-mediated fusion and inactivation. Biochemistry 44, 12471-12479 (Pubitemid 41324338)
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12471-12479
    • Dimitrov, A.S.1    Louis, J.M.2    Bewley, C.A.3    Clore, G.M.4    Blumenthal, R.5
  • 41
    • 84863116316 scopus 로고    scopus 로고
    • Broad antiviral activity and crystal structure of HIV-1 fusion inhibitor Sifuvirtide
    • Yao, X., Chong, H., Zhang, C., Waltersperger, S., Wang, M., Cui, S., and He, Y. (2012) Broad antiviral activity and crystal structure of HIV-1 fusion inhibitor Sifuvirtide. J. Biol. Chem. 287, 6788-6796
    • (2012) J. Biol. Chem. , vol.287 , pp. 6788-6796
    • Yao, X.1    Chong, H.2    Zhang, C.3    Waltersperger, S.4    Wang, M.5    Cui, S.6    He, Y.7
  • 45
    • 80055013474 scopus 로고    scopus 로고
    • Resistance of human immunodeficiency virus type 1 to a third-generation fusion inhibitor requires multiple mutations in gp41 and is accompanied by a dramatic loss of gp41 function
    • Eggink, D., Bontjer, I., Langedijk, J. P., Berkhout, B., and Sanders, R. W. (2011) Resistance of human immunodeficiency virus type 1 to a third-generation fusion inhibitor requires multiple mutations in gp41 and is accompanied by a dramatic loss of gp41 function. J. Virol. 85, 10785-10797
    • (2011) J. Virol. , vol.85 , pp. 10785-10797
    • Eggink, D.1    Bontjer, I.2    Langedijk, J.P.3    Berkhout, B.4    Sanders, R.W.5


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