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Volumn 78, Issue 4, 2004, Pages 2131-2136

Distribution of Hydrophobic Residues Is Crucial for the Fusogenic Properties of the Ebola Virus GP2 Fusion Peptide

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS FUSION PROTEIN;

EID: 0842282793     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.4.2131-2136.2004     Document Type: Article
Times cited : (28)

References (35)
  • 1
    • 37049106853 scopus 로고
    • Peptide synthesis. II. Procedures for solid-phase synthesis by N- fluorenylmethoxycarbonylamino-acids on polyamide supports: Synthesis of substance P and of acyl carrier protein 65-74 decapeptide
    • Atherton, E., C. J. Logan, and R. C. Sheppard. 1981. Peptide synthesis. II. Procedures for solid-phase synthesis by N- fluorenylmethoxycarbonylamino-acids on polyamide supports: synthesis of substance P and of acyl carrier protein 65-74 decapeptide. J. Chem. Soc. Perkin Trans. I 1:538.
    • (1981) J. Chem. Soc. Perkin Trans. I , vol.1 , pp. 538
    • Atherton, E.1    Logan, C.J.2    Sheppard, R.C.3
  • 2
    • 0040952847 scopus 로고    scopus 로고
    • Oblique membrane insertion of viral fusion peptide probed by neutron diffraction
    • Bradshaw, J. P., M. J. Darkes, T. A. Harroun, J. Katsaras, and R. M. Epand. 2000. Oblique membrane insertion of viral fusion peptide probed by neutron diffraction. Biochemistry 39:6581-6585.
    • (2000) Biochemistry , vol.39 , pp. 6581-6585
    • Bradshaw, J.P.1    Darkes, M.J.2    Harroun, T.A.3    Katsaras, J.4    Epand, R.M.5
  • 3
    • 0025936242 scopus 로고
    • Differentiation of lipid-associating helices by use of three-dimensional molecular hydrophobicity potential calculations
    • Brasseur, R. 1991. Differentiation of lipid-associating helices by use of three-dimensional molecular hydrophobicity potential calculations. J. Biol. Chem. 266:16120-16127.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16120-16127
    • Brasseur, R.1
  • 5
    • 0034091871 scopus 로고    scopus 로고
    • Tilted peptides: A motif for membrane destabilization (hypothesis)
    • Brasseur, R. 2000. Tilted peptides: a motif for membrane destabilization (hypothesis). Mol. Membr. Biol. 17:31-40.
    • (2000) Mol. Membr. Biol. , vol.17 , pp. 31-40
    • Brasseur, R.1
  • 6
    • 0026693513 scopus 로고
    • Molecular modeling of the amphipathic helices of the plasma apolipoproteins
    • Brasseur, R., L. Lins, B. Vanloo, J. M. Ruysschaert, and M. Rosseneu. 1992. Molecular modeling of the amphipathic helices of the plasma apolipoproteins. Proteins 13:246-257.
    • (1992) Proteins , vol.13 , pp. 246-257
    • Brasseur, R.1    Lins, L.2    Vanloo, B.3    Ruysschaert, J.M.4    Rosseneu, M.5
  • 8
    • 0033947260 scopus 로고    scopus 로고
    • The central proline of an internal viral fusion peptide serves two important roles
    • Delos, S. E., J. M. Gilbert, and J. M. White. 2000. The central proline of an internal viral fusion peptide serves two important roles. J. Virol. 74:1686-1693.
    • (2000) J. Virol. , vol.74 , pp. 1686-1693
    • Delos, S.E.1    Gilbert, J.M.2    White, J.M.3
  • 10
    • 0032032107 scopus 로고    scopus 로고
    • IMPALA: A simple restraint field to simulate the biological membrane in molecular structure studies
    • Ducarme, P., M. Rahman, and R. Brasseur. 1998. IMPALA: a simple restraint field to simulate the biological membrane in molecular structure studies. Proteins 30:357-371.
    • (1998) Proteins , vol.30 , pp. 357-371
    • Ducarme, P.1    Rahman, M.2    Brasseur, R.3
  • 11
    • 0021890825 scopus 로고
    • 2+-induced fusion and destabilization of liposomes
    • 2+-induced fusion and destabilization of liposomes. Biochemistry 24:3099-3106.
    • (1985) Biochemistry , vol.24 , pp. 3099-3106
    • Ellens, H.1    Bentz, J.2    Szoka, F.C.3
  • 12
    • 0038487375 scopus 로고    scopus 로고
    • Fusion peptides and the mechanism of viral fusion
    • Epand, R. M. 2003. Fusion peptides and the mechanism of viral fusion, Biochim. Biophys. Acta 1614:116-121.
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 116-121
    • Epand, R.M.1
  • 13
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyze amino acid sequences
    • Gaboriaud, C., V. Bissery, T. Benchetrit, and J. P. Mornon. 1987. Hydrophobic cluster analysis: an efficient new way to compare and analyze amino acid sequences. FEBS Lett. 224:149-155.
    • (1987) FEBS Lett. , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 14
    • 0030591276 scopus 로고    scopus 로고
    • Similar structural models of the transmembrane proteins of Ebola virus and avian sarcoma viruses
    • Gallaher, W. R. 1996. Similar structural models of the transmembrane proteins of Ebola virus and avian sarcoma viruses. Cell 85:477-478.
    • (1996) Cell , vol.85 , pp. 477-478
    • Gallaher, W.R.1
  • 16
    • 0034892952 scopus 로고    scopus 로고
    • Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin
    • Han, X., J. H. Bushweller, D. S. Cafiso, and L. K. Tamm. 2001. Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin. Nat. Struct. Biol. 8:715-720.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 715-720
    • Han, X.1    Bushweller, J.H.2    Cafiso, D.S.3    Tamm, L.K.4
  • 17
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure: Characteriza-tion of size, trapped volume and ability to maintain a membrane potential
    • Hope, M. J., M. G. Bally, G. Webb, and P. R. Cullis. 1985. Production of large unilamellar vesicles by a rapid extrusion procedure: characteriza-tion of size, trapped volume and ability to maintain a membrane potential. Biochim. Biophys. Acta 812:55-65.
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 55-65
    • Hope, M.J.1    Bally, M.G.2    Webb, G.3    Cullis, P.R.4
  • 19
    • 0032849336 scopus 로고    scopus 로고
    • Mutational analysis of the putative fusion domain of Ebola virus glycoprotein
    • Ito, H., S. Watanabe, A. Sanchez, M. A. Whitt, and Y. Kawaoka. 1999. Mutational analysis of the putative fusion domain of Ebola virus glycoprotein. J. Virol. 73:8907-8912.
    • (1999) J. Virol. , vol.73 , pp. 8907-8912
    • Ito, H.1    Watanabe, S.2    Sanchez, A.3    Whitt, M.A.4    Kawaoka, Y.5
  • 20
    • 0034889536 scopus 로고    scopus 로고
    • A critical view on conservative mutations
    • Jonson, P. H., and S. B. Petersen. 2001. A critical view on conservative mutations. Protein Eng. 14:397-402.
    • (2001) Protein Eng. , vol.14 , pp. 397-402
    • Jonson, P.H.1    Petersen, S.B.2
  • 21
    • 0020479909 scopus 로고
    • A fluorescence assay to monitor vesicle fusion and lysis
    • Kendall, D. A., and R. C. MacDonald. 1982. A fluorescence assay to monitor vesicle fusion and lysis. J. Biol. Chem. 257:13892-13895.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13892-13895
    • Kendall, D.A.1    MacDonald, R.C.2
  • 22
  • 23
    • 0036019358 scopus 로고    scopus 로고
    • Lipid-interacting properties of the N-terminal domain of human apolipoprotein C-III
    • Lins, L., C. Flore, L. Chapelle, P. J. Talmud, A. Thomas, and R. Brasseur. 2002. Lipid-interacting properties of the N-terminal domain of human apolipoprotein C-III. Protein Eng. 15:513-520.
    • (2002) Protein Eng. , vol.15 , pp. 513-520
    • Lins, L.1    Flore, C.2    Chapelle, L.3    Talmud, P.J.4    Thomas, A.5    Brasseur, R.6
  • 24
    • 0035451179 scopus 로고    scopus 로고
    • Computational study of lipid-destabilizing protein fragments: Towards a comprehensive view of tilted peptides
    • Lins, L., B. Charloteaux, A. Thomas, and R. Brasseur. 2001. Computational study of lipid-destabilizing protein fragments: towards a comprehensive view of tilted peptides. Proteins 44:435-447.
    • (2001) Proteins , vol.44 , pp. 435-447
    • Lins, L.1    Charloteaux, B.2    Thomas, A.3    Brasseur, R.4
  • 25
    • 0033020204 scopus 로고    scopus 로고
    • Core structure of the envelope glycoprotein GP2 from Ebola virus at 1. 9-A resolution
    • Malashkevich, V. N., B. J. Schneider, M. L. McNally, et al. 1999. Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolution. Proc. Natl. Acad. Sci. USA 96:2662-2667.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2662-2667
    • Malashkevich, V.N.1    Schneider, B.J.2    McNally, M.L.3
  • 27
    • 0027955142 scopus 로고
    • Correlation between fusogenicity of synthetic modified peptides corresponding to the NH2-terminal extremity of simian immunodeficiency virus gp32 and their mode of insertion into the lipid bilayer: An infrared spectroscopy study
    • Martin, I., M. C. Dubois, F. Defrise-Quertain, T. Saermark, A. Burny, R. Brasseur, and J. M. Ruysschaert. 1994. Correlation between fusogenicity of synthetic modified peptides corresponding to the NH2-terminal extremity of simian immunodeficiency virus gp32 and their mode of insertion into the lipid bilayer: an infrared spectroscopy study. J. Virol. 68:1139-1148.
    • (1994) J. Virol. , vol.68 , pp. 1139-1148
    • Martin, I.1    Dubois, M.C.2    Defrise-Quertain, F.3    Saermark, T.4    Burny, A.5    Brasseur, R.6    Ruysschaert, J.M.7
  • 29
    • 0033591307 scopus 로고    scopus 로고
    • Are the fusion processes involved in birth, life and death of the cell depending on tilted insertion of peptides into membranes?
    • Peuvot, J., A. Schanck, L. Lins, and R. Brasseur. 1999. Are the fusion processes involved in birth, life and death of the cell depending on tilted insertion of peptides into membranes? J. Theor. Biol. 198:173-181.
    • (1999) J. Theor. Biol. , vol.198 , pp. 173-181
    • Peuvot, J.1    Schanck, A.2    Lins, L.3    Brasseur, R.4
  • 32
    • 0038093145 scopus 로고    scopus 로고
    • Phosphatidylinositol-dependent membrane fusion induced by a putative fusogenic sequence of Ebola virus
    • Ruiz-Arguello, M. B., F. M. Goni, F. B. Pereira, and J. L. Nieva. 1998. Phosphatidylinositol-dependent membrane fusion induced by a putative fusogenic sequence of Ebola virus. J. Virol. 72:1775-1781.
    • (1998) J. Virol. , vol.72 , pp. 1775-1781
    • Ruiz-Arguello, M.B.1    Goni, F.M.2    Pereira, F.B.3    Nieva, J.L.4
  • 33
    • 0037472744 scopus 로고    scopus 로고
    • Calcium-dependent conformational changes of membrane-bound Ebola virus fusion peptide drive vesicle fusion
    • Suarez, T., M. J. Gomara, F. M. Goni, I. Mingarro, A. Muga, E. Perez-Paya, and J. L. Nieva. 2003. Calcium-dependent conformational changes of membrane-bound Ebola virus fusion peptide drive vesicle fusion. FEBS Lett. 535:23-28.
    • (2003) FEBS Lett. , vol.535 , pp. 23-28
    • Suarez, T.1    Gomara, M.J.2    Goni, F.M.3    Mingarro, I.4    Muga, A.5    Perez-Paya, E.6    Nieva, J.L.7
  • 34
    • 0029977378 scopus 로고    scopus 로고
    • Prediction of signal peptide functional properties: A study of the orientation and angle of insertion of yeast invertase mutants and human apolipoprotein B signal peptide variants
    • Talmud, P., L. Lins, and R. Brasseur. 1996. Prediction of signal peptide functional properties: a study of the orientation and angle of insertion of yeast invertase mutants and human apolipoprotein B signal peptide variants. Protein Eng. 9:317-321.
    • (1996) Protein Eng. , vol.9 , pp. 317-321
    • Talmud, P.1    Lins, L.2    Brasseur, R.3
  • 35
    • 0026505142 scopus 로고
    • Fusogenic segments of bovine leukemia virus and simian immunodeficiency virus are interchangeable and mediate fusion by means of oblique insertion in the lipid bilayer of their target cells
    • Voneche, V., D. Portetelle, R. Kettmann, L. Willems, K. Limbach, E. Paoletti, J. M. Ruysschaert, A. Burny, and R. Brasseur. 1992. Fusogenic segments of bovine leukemia virus and simian immunodeficiency virus are interchangeable and mediate fusion by means of oblique insertion in the lipid bilayer of their target cells. Proc. Natl. Acad. Sci. USA 89:3810-3814.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3810-3814
    • Voneche, V.1    Portetelle, D.2    Kettmann, R.3    Willems, L.4    Limbach, K.5    Paoletti, E.6    Ruysschaert, J.M.7    Burny, A.8    Brasseur, R.9


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