메뉴 건너뛰기




Volumn 430, Issue 7003, 2004, Pages 1053-1058

Structural rearrangements in the membrane penetration protein of a non-enveloped virus

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CELLS; CRYSTAL STRUCTURE; CYTOLOGY; IMAGE RECONSTRUCTION; VIRUSES;

EID: 4344695186     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02836     Document Type: Article
Times cited : (191)

References (30)
  • 2
    • 0034968905 scopus 로고    scopus 로고
    • Trypsin cleavage stabilizes the rotavirus VP4 spike
    • Crawford, S. E. et al. Trypsin cleavage stabilizes the rotavirus VP4 spike. J. Virol. 75, 6052-6061 (2001).
    • (2001) J. Virol. , vol.75 , pp. 6052-6061
    • Crawford, S.E.1
  • 3
    • 0023716861 scopus 로고
    • Studies on the structure of the influenza virus haemagglutinin at the pH of membrane fusion
    • Ruigrok, R. W. et al. Studies on the structure of the influenza virus haemagglutinin at the pH of membrane fusion. J. Gen. Virol. 69, 2785-2795 (1988).
    • (1988) J. Gen. Virol. , vol.69 , pp. 2785-2795
    • Ruigrok, R.W.1
  • 4
    • 0029878665 scopus 로고    scopus 로고
    • The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide
    • Weissenhorn, W. et al. The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide. EMBO J. 15, 1507-1514 (1996).
    • (1996) EMBO J. , vol.15 , pp. 1507-1514
    • Weissenhorn, W.1
  • 5
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis, Y., Ogata, S., Clements, D. & Harrison, S.C. Structure of the dengue virus envelope protein after membrane fusion. Nature 427, 313-319 (2004).
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 6
    • 1642540249 scopus 로고    scopus 로고
    • Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus
    • Gibbons, D. L. et al. Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature 427, 320-325 (2004).
    • (2004) Nature , vol.427 , pp. 320-325
    • Gibbons, D.L.1
  • 7
    • 0036500085 scopus 로고    scopus 로고
    • The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site
    • Dormitzer, P. R., Sun, Z.-Y. J., Wagner, G. & Harrison, S. C. The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site. EMBO J. 21, 885-897 (2002).
    • (2002) EMBO J. , vol.21 , pp. 885-897
    • Dormitzer, P.R.1    Sun, Z.-Y.J.2    Wagner, G.3    Harrison, S.C.4
  • 8
    • 0023838918 scopus 로고
    • The rhesus rotavirus gene encoding protein VP3: Location of amino acids involved in homologous and heterologous rotavirus neutralization and identification of a putative fusion region
    • Mackow, E. R. et al. The rhesus rotavirus gene encoding protein VP3: location of amino acids involved in homologous and heterologous rotavirus neutralization and identification of a putative fusion region. Proc. Natl Acad. Sci. USA 85, 645-649 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 645-649
    • Mackow, E.R.1
  • 9
    • 0033937215 scopus 로고    scopus 로고
    • Selective membrane permeabilization by the rotavirus VP5* protein is abrogated by mutations in an internal hydrophobic domain
    • Dowling, W., Denisova, E., LaMonica, R. & Mackow, E. R. Selective membrane permeabilization by the rotavirus VP5* protein is abrogated by mutations in an internal hydrophobic domain. J. Virol. 74, 636-376 (2000).
    • (2000) J. Virol. , vol.74 , pp. 636-376
    • Dowling, W.1    Denisova, E.2    LaMonica, R.3    Mackow, E.R.4
  • 10
    • 0141458927 scopus 로고    scopus 로고
    • Integrin-using rotaviruses bind α2β1 integrin α2 I domain via VP4 DGE sequence and recognize αXβ2 and αVβ3 by using VP7 during cell entry
    • Graham, K. L. et al. Integrin-using rotaviruses bind α2β1 integrin α2 I domain via VP4 DGE sequence and recognize αXβ2 and αVβ3 by using VP7 during cell entry. J. Virol. 77, 9969-9978 (2003).
    • (2003) J. Virol. , vol.77 , pp. 9969-9978
    • Graham, K.L.1
  • 11
    • 0025900084 scopus 로고
    • Antibodies to the trypsin cleavage peptide VP8 neutralize rotavirus by inhibiting binding of virions to target cells in culture
    • Ruggeri, F. M. & Greenberg, H. B. Antibodies to the trypsin cleavage peptide VP8 neutralize rotavirus by inhibiting binding of virions to target cells in culture. J. Virol. 65, 2211-2219 (1991).
    • (1991) J. Virol. , vol.65 , pp. 2211-2219
    • Ruggeri, F.M.1    Greenberg, H.B.2
  • 12
    • 0022460714 scopus 로고
    • Passive protection against rotavirus-induced diarrhea by monoclonal antibodies to surface proteins vp3 and vp7
    • Offit, P. A., Shaw, R. D. & Greenberg, H. B. Passive protection against rotavirus-induced diarrhea by monoclonal antibodies to surface proteins vp3 and vp7. J. Virol. 58, 700-703 (1986).
    • (1986) J. Virol. , vol.58 , pp. 700-703
    • Offit, P.A.1    Shaw, R.D.2    Greenberg, H.B.3
  • 13
    • 0034902747 scopus 로고    scopus 로고
    • Proteolysis of monomeric recombinant rotavirus VP4 yields an oligomeric VP5* core
    • Dormitzer, P. R., Greenberg, H. B. & Harrison, S. C. Proteolysis of monomeric recombinant rotavirus VP4 yields an oligomeric VP5* core. J. Virol. 75, 7339-7350 (2001).
    • (2001) J. Virol. , vol.75 , pp. 7339-7350
    • Dormitzer, P.R.1    Greenberg, H.B.2    Harrison, S.C.3
  • 14
    • 0029793570 scopus 로고    scopus 로고
    • Trypsin activation pathway of rotavirus infectivity
    • Arias, C. F., Romero, P., Alvarez, V. & Lopez, S. Trypsin activation pathway of rotavirus infectivity. J. Virol. 70, 5832-5839 (1996).
    • (1996) J. Virol. , vol.70 , pp. 5832-5839
    • Arias, C.F.1    Romero, P.2    Alvarez, V.3    Lopez, S.4
  • 15
    • 0031901344 scopus 로고    scopus 로고
    • Cleavage of rhesus rotavirus VP4 after arginine 247 is essential for rotavirus-like particle-induced fusion from without
    • Gilbert, J. M. & Greenberg, H. B. Cleavage of rhesus rotavirus VP4 after arginine 247 is essential for rotavirus-like particle-induced fusion from without. J. Virol. 72, 5323-5327 (1998).
    • (1998) J. Virol. , vol.72 , pp. 5323-5327
    • Gilbert, J.M.1    Greenberg, H.B.2
  • 16
    • 0035861996 scopus 로고    scopus 로고
    • Localization of membrane permeabilization and receptor binding sites on the VP4 hemagglutinin of rotavirus: Implications for cell entry
    • Tihova, M., Dryden, K. A., Bellamy, A. R., Greenberg, H. B. & Yeager, M. Localization of membrane permeabilization and receptor binding sites on the VP4 hemagglutinin of rotavirus: implications for cell entry. J. Mol. Biol. 314, 985-992 (2001).
    • (2001) J. Mol. Biol. , vol.314 , pp. 985-992
    • Tihova, M.1    Dryden, K.A.2    Bellamy, A.R.3    Greenberg, H.B.4    Yeager, M.5
  • 17
    • 0023820279 scopus 로고
    • Identification of cross-reactive and serotype 2-specific neutralization epitopes on VP3 of human rotavirus
    • Taniguchi, K. et al. Identification of cross-reactive and serotype 2-specific neutralization epitopes on VP3 of human rotavirus. J. Virol. 62, 2421-2426 (1988).
    • (1988) J. Virol. , vol.62 , pp. 2421-2426
    • Taniguchi, K.1
  • 18
    • 0027220677 scopus 로고
    • Three-dimensional visualization of the rotavirus hemagglutinin structure
    • Shaw, A. L. et al. Three-dimensional visualization of the rotavirus hemagglutinin structure. Cell 74, 693-701 (1993).
    • (1993) Cell , vol.74 , pp. 693-701
    • Shaw, A.L.1
  • 19
    • 0028205688 scopus 로고
    • Three-dimensional structure of the rotavirus haemagglutinin VP4 by cryo-electron microscopy and difference map analysis
    • Yeager, M., Berriman, J. A., Baker, T. S. & Bellamy, A. R. Three-dimensional structure of the rotavirus haemagglutinin VP4 by cryo-electron microscopy and difference map analysis. EMBO J. 13, 1011-1018 (1994).
    • (1994) EMBO J. , vol.13 , pp. 1011-1018
    • Yeager, M.1    Berriman, J.A.2    Baker, T.S.3    Bellamy, A.R.4
  • 20
    • 0037169362 scopus 로고    scopus 로고
    • Structure of the reovirus membrane-penetration protein, μ1, in a complex with its protector protein, σ3
    • Liemann, S., Chandran, K., Baker, T. S., Nibert, M. L. & Harrison, S. C. Structure of the reovirus membrane-penetration protein, μ1, in a complex with its protector protein, σ3. Cell 108, 283-295 (2002).
    • (2002) Cell , vol.108 , pp. 283-295
    • Liemann, S.1    Chandran, K.2    Baker, T.S.3    Nibert, M.L.4    Harrison, S.C.5
  • 21
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • Weeks, C. M. & Miller, R. The design and implementation of SnB v2.0. J. Appl. Crystallogr. 32, 120-124 (1999).
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 22
    • 0037779022 scopus 로고    scopus 로고
    • A statistic for local intensity differences: Robustness to anisotropy and pseudo-centering and utility for detecting twinning
    • Padilla, J. E. & Yeates, T. O. A statistic for local intensity differences: robustness to anisotropy and pseudo-centering and utility for detecting twinning. Acta Crystallogr. D 59, 1124-1130 (2003).
    • (2003) Acta Crystallogr. D , vol.59 , pp. 1124-1130
    • Padilla, J.E.1    Yeates, T.O.2
  • 23
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther, R. A. Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Phil. Trans. R. Soc. Lond. B 261, 221-230 (1971).
    • (1971) Phil. Trans. R. Soc. Lond. B , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 24
    • 0029916491 scopus 로고    scopus 로고
    • Automated software package for icosahedral virus reconstruction
    • Lawton, J. A. & Prasad, B. V. V. Automated software package for icosahedral virus reconstruction. J. Struct. Biol. 116, 209-215 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 209-215
    • Lawton, J.A.1    Prasad, B.V.V.2
  • 25
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., Baldwin, P. R. & Chiu, W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (1999).
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 26
    • 0032780181 scopus 로고    scopus 로고
    • Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers, W., Milligan, R. A. & McCammon, J. A. Situs: A package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125, 185-195 (1999).
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 27
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 28
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, J.1
  • 29
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from interfacial and thermodynamic properties of hydrocarbons. Prot. Struct. Funct. Genet. 11, 281-296 (1991).
    • (1991) Prot. Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 30
    • 0025371944 scopus 로고
    • Three-dimensional structure of rhesus rotavirus by cryoelectron microscopy and image reconstruction
    • Yeager, M., Dryden, K. A., Olson, N. H., Greenberg, H. B. & Baker, T. S. Three-dimensional structure of rhesus rotavirus by cryoelectron microscopy and image reconstruction. J. Cell Biol. 110, 2133-2144 (1990).
    • (1990) J. Cell Biol. , vol.110 , pp. 2133-2144
    • Yeager, M.1    Dryden, K.A.2    Olson, N.H.3    Greenberg, H.B.4    Baker, T.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.