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Volumn 85, Issue 18, 2011, Pages 9327-9333

The structure of barmah forest virus as revealed by cryo-electron microscopy at a 6-angstrom resolution has detailed transmembrane protein architecture and interactions

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS PROTEIN E1; VIRUS PROTEIN E2; VIRUS PROTEIN E3;

EID: 80052503042     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05015-11     Document Type: Article
Times cited : (49)

References (40)
  • 1
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar, D. L., and A. Klug. 1962. Physical principles in the construction of regular viruses. Cold Spring Harb. Symp. Quant. Biol. 27:1-24.
    • (1962) Cold Spring Harb. Symp. Quant. Biol. , vol.27 , pp. 1-24
    • Caspar, D.L.1    Klug, A.2
  • 2
    • 61449123986 scopus 로고    scopus 로고
    • Palmitoylation of membrane proteins (review)
    • Charollais, J., and F. G. Van Der Goot. 2009. Palmitoylation of membrane proteins (review). Mol. Membr. Biol. 26:55-66.
    • (2009) Mol. Membr. Biol. , vol.26 , pp. 55-66
    • Charollais, J.1    Van Der Goot, F.G.2
  • 3
    • 0030890291 scopus 로고    scopus 로고
    • Structure of Semliki Forest virus core protein
    • Choi, H. K., G. Lu, S. Lee, G. Wengler, and M. G. Rossmann. 1997. Structure of Semliki Forest virus core protein. Proteins 27:345-359.
    • (1997) Proteins , vol.27 , pp. 345-359
    • Choi, H.K.1    Lu, G.2    Lee, S.3    Wengler, G.4    Rossmann, M.G.5
  • 5
    • 0021321085 scopus 로고
    • Characterization of Barmah forest virus: an alphavirus with some unusual properties
    • Dalgarno, L., et al. 1984. Characterization of Barmah forest virus: an alphavirus with some unusual properties. Virology 133:416-426.
    • (1984) Virology , vol.133 , pp. 416-426
    • Dalgarno, L.1
  • 7
    • 0025913578 scopus 로고
    • Site-directed mutations in Sindbis virus E2 glycoprotein's cytoplasmic domain and the 6K protein lead to similar defects in virus assembly and budding
    • Gaedigk-Nitschko, K., and M. J. Schlesinger. 1991. Site-directed mutations in Sindbis virus E2 glycoprotein's cytoplasmic domain and the 6K protein lead to similar defects in virus assembly and budding. Virology 183:206-214.
    • (1991) Virology , vol.183 , pp. 206-214
    • Gaedigk-Nitschko, K.1    Schlesinger, M.J.2
  • 8
    • 1642540249 scopus 로고    scopus 로고
    • Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus
    • Gibbons, D. L., et al. 2004. Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature 427:320-325.
    • (2004) Nature , vol.427 , pp. 320-325
    • Gibbons, D.L.1
  • 9
    • 0033994741 scopus 로고    scopus 로고
    • A single deletion in the membrane-proximal region of the Sindbis virus glycoprotein E2 endodomain blocks virus assembly
    • Hernandez, R., H. Lee, C. Nelson, and D. T. Brown. 2000. A single deletion in the membrane-proximal region of the Sindbis virus glycoprotein E2 endodomain blocks virus assembly. J. Virol. 74:4220-4228.
    • (2000) J. Virol. , vol.74 , pp. 4220-4228
    • Hernandez, R.1    Lee, H.2    Nelson, C.3    Brown, D.T.4
  • 11
    • 77957923201 scopus 로고    scopus 로고
    • The first human epitope map of the alphaviral E1 and E2 proteins reveals a new E2 epitope with significant virus neutralizing activity
    • Hunt, A. R., S. Frederickson, T. Maruyama, J. T. Roehrig, and C. D. Blair. 2010. The first human epitope map of the alphaviral E1 and E2 proteins reveals a new E2 epitope with significant virus neutralizing activity. PLoS Negl. Trop. Dis. 4:e739.
    • (2010) PLoS Negl. Trop. Dis. , vol.4
    • Hunt, A.R.1    Frederickson, S.2    Maruyama, T.3    Roehrig, J.T.4    Blair, C.D.5
  • 12
    • 43049145015 scopus 로고    scopus 로고
    • Ross River virus and Barmah Forest virus infections: a review of history, ecology, and predictive models, with implications for tropical northern Australia
    • Jacups, S. P., P. I. Whelan, and B. J. Currie. 2008. Ross River virus and Barmah Forest virus infections: a review of history, ecology, and predictive models, with implications for tropical northern Australia. Vector Borne Zoonotic Dis. 8:283-297.
    • (2008) Vector Borne Zoonotic Dis , vol.8 , pp. 283-297
    • Jacups, S.P.1    Whelan, P.I.2    Currie, B.J.3
  • 13
    • 77649180251 scopus 로고    scopus 로고
    • A novel approximation method of CTF amplitude correction for 3D single particle reconstruction
    • Jiang, L., Z. Liu, D. Georgieva, M. E. Kuil, and J. P. Abrahams. 2010. A novel approximation method of CTF amplitude correction for 3D single particle reconstruction. Ultramicroscopy 110:350-358.
    • (2010) Ultramicroscopy , vol.110 , pp. 350-358
    • Jiang, L.1    Liu, Z.2    Georgieva, D.3    Kuil, M.E.4    Abrahams, J.P.5
  • 14
    • 0025348447 scopus 로고
    • Variants of Venezuelan equine encephalitis virus that resist neutralization define a domain of the E2 glycoprotein
    • Johnson, B. J., J. R. Brubaker, J. T. Roehrig, and D. W. Trent. 1990. Variants of Venezuelan equine encephalitis virus that resist neutralization define a domain of the E2 glycoprotein. Virology 177:676-683.
    • (1990) Virology , vol.177 , pp. 676-683
    • Johnson, B.J.1    Brubaker, J.R.2    Roehrig, J.T.3    Trent, D.W.4
  • 15
    • 70349199877 scopus 로고    scopus 로고
    • A structural and functional perspective of alphavirus replication and assembly
    • Jose, J., J. E. Snyder, and R. J. Kuhn. 2009. A structural and functional perspective of alphavirus replication and assembly. Future Microbiol. 4:837-856.
    • (2009) Future Microbiol , vol.4 , pp. 837-856
    • Jose, J.1    Snyder, J.E.2    Kuhn, R.J.3
  • 16
    • 0033787642 scopus 로고    scopus 로고
    • Local average intensity-based method for identifying spherical particles in electron micrographs
    • Kivioja, T., J. Ravantti, A. Verkhovsky, E. Ukkonen, and D. Bamford. 2000. Local average intensity-based method for identifying spherical particles in electron micrographs. J. Struct. Biol. 131:126-134.
    • (2000) J. Struct. Biol. , vol.131 , pp. 126-134
    • Kivioja, T.1    Ravantti, J.2    Verkhovsky, A.3    Ukkonen, E.4    Bamford, D.5
  • 17
    • 75849161566 scopus 로고    scopus 로고
    • Site-specific attachment of palmitate or stearate to cytoplasmic versus transmembrane cysteines is a common feature of viral spike proteins
    • Kordyukova, L. V., M. V. Serebryakova, L. A. Baratova, and M. Veit. 2010. Site-specific attachment of palmitate or stearate to cytoplasmic versus transmembrane cysteines is a common feature of viral spike proteins. Virology 398:49-56.
    • (2010) Virology , vol.398 , pp. 49-56
    • Kordyukova, L.V.1    Serebryakova, M.V.2    Baratova, L.A.3    Veit, M.4
  • 18
    • 0031579243 scopus 로고    scopus 로고
    • Nucleotide sequence of the Barmah Forest virus genome
    • Lee, E., et al. 1997. Nucleotide sequence of the Barmah Forest virus genome. Virology 227:509-514.
    • (1997) Virology , vol.227 , pp. 509-514
    • Lee, E.1
  • 19
    • 78649891889 scopus 로고    scopus 로고
    • Structural changes of envelope proteins during alphavirus fusion
    • Li, L., J. Jose, Y. Xiang, R. J. Kuhn, and M. G. Rossmann. 2010. Structural changes of envelope proteins during alphavirus fusion. Nature 468:705-708.
    • (2010) Nature , vol.468 , pp. 705-708
    • Li, L.1    Jose, J.2    Xiang, Y.3    Kuhn, R.J.4    Rossmann, M.G.5
  • 20
    • 34548643898 scopus 로고    scopus 로고
    • Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-path Simulated Annealing optimization algorithm
    • Liu, X., W. Jiang, J. Jakana, and W. Chiu. 2007. Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-path Simulated Annealing optimization algorithm. J. Struct. Biol. 160:11-27.
    • (2007) J. Struct. Biol. , vol.160 , pp. 11-27
    • Liu, X.1    Jiang, W.2    Jakana, J.3    Chiu, W.4
  • 21
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., P. R. Baldwin, and W. Chiu. 1999. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128:82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 23
    • 0020308625 scopus 로고
    • Viruses recovered from mosquitoes and wildlife serum collected in the Murray Valley of Southeastern Australia, February 1974, during an epidemic of encephalitis
    • Marshall, I. D., G. M. Woodroofe, and S. Hirsch. 1982. Viruses recovered from mosquitoes and wildlife serum collected in the Murray Valley of Southeastern Australia, February 1974, during an epidemic of encephalitis. Aust. J. Exp. Biol. Med. Sci. 60:457-470.
    • (1982) Aust. J. Exp. Biol. Med. Sci. , vol.60 , pp. 457-470
    • Marshall, I.D.1    Woodroofe, G.M.2    Hirsch, S.3
  • 24
    • 33644815756 scopus 로고    scopus 로고
    • Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses
    • Mukhopadhyay, S., et al. 2006. Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses. Structure 14:63-73.
    • (2006) Structure , vol.14 , pp. 63-73
    • Mukhopadhyay, S.1
  • 25
    • 0030450955 scopus 로고    scopus 로고
    • Glycoproteins E2 of the Venezuelan and eastern equine encephalomyelitis viruses contain multiple cross-reactive epitopes
    • Pereboev, A. V., I. A. Razumov, V. A. Svyatchenko, and V. B. Loktev. 1996. Glycoproteins E2 of the Venezuelan and eastern equine encephalomyelitis viruses contain multiple cross-reactive epitopes. Arch. Virol. 141:2191-2205.
    • (1996) Arch. Virol. , vol.141 , pp. 2191-2205
    • Pereboev, A.V.1    Razumov, I.A.2    Svyatchenko, V.A.3    Loktev, V.B.4
  • 26
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Pettersen, E. F., et al. 2004. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25:1605-1612.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 27
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • Phillips, J. C., et al. 2005. Scalable molecular dynamics with NAMD. J. Comput. Chem. 26:1781-1802.
    • (2005) J. Comput. Chem. , vol.26 , pp. 1781-1802
    • Phillips, J.C.1
  • 28
    • 0034795886 scopus 로고    scopus 로고
    • Evolutionary relationships and systematics of the alphaviruses
    • Powers, A. M., et al. 2001. Evolutionary relationships and systematics of the alphaviruses. J. Virol. 75:10118-10131.
    • (2001) J. Virol. , vol.75 , pp. 10118-10131
    • Powers, A.M.1
  • 29
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • Rey, F. A., F. X. Heinz, C. Mandl, C. Kunz, and S. C. Harrison. 1995. The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 375:291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 30
    • 33644799064 scopus 로고    scopus 로고
    • Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus
    • Roussel, A., J. Lescar, M. C. Vaney, G. Wengler, and F. A. Rey. 2006. Structure and interactions at the viral surface of the envelope protein E1 of Semliki Forest virus. Structure 14:75-86.
    • (2006) Structure , vol.14 , pp. 75-86
    • Roussel, A.1    Lescar, J.2    Vaney, M.C.3    Wengler, G.4    Rey, F.A.5
  • 31
    • 0024263339 scopus 로고
    • Chemical identification of cysteine as palmitoylation site in a transmembrane protein (Semliki Forest virus E1)
    • Schmidt, M., M. F. Schmidt, and R. Rott. 1988. Chemical identification of cysteine as palmitoylation site in a transmembrane protein (Semliki Forest virus E1). J. Biol. Chem. 263:18635-18639.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18635-18639
    • Schmidt, M.1    Schmidt, M.F.2    Rott, R.3
  • 32
    • 33845291163 scopus 로고    scopus 로고
    • Ab initio resolution measurement for single particle structures
    • Sousa, D., and N. Grigorieff. 2007. Ab initio resolution measurement for single particle structures. J. Struct. Biol. 157:201-210.
    • (2007) J. Struct. Biol. , vol.157 , pp. 201-210
    • Sousa, D.1    Grigorieff, N.2
  • 33
    • 0025945880 scopus 로고
    • Identification of antigenically important domains in the glycoproteins of Sindbis virus by analysis of antibody escape variants
    • Strauss, E. G., D. S. Stec, A. L. Schmaljohn, and J. H. Strauss. 1991. Identification of antigenically important domains in the glycoproteins of Sindbis virus by analysis of antibody escape variants. J. Virol. 65:4654-4664.
    • (1991) J. Virol. , vol.65 , pp. 4654-4664
    • Strauss, E.G.1    Stec, D.S.2    Schmaljohn, A.L.3    Strauss, J.H.4
  • 34
    • 70349267547 scopus 로고    scopus 로고
    • Molecular dynamics flexible fitting: a practical guide to combine cryo-electron microscopy and X-ray crystallography
    • Trabuco, L. G., E. Villa, E. Schreiner, C. B. Harrison, and K. Schulten. 2009. Molecular dynamics flexible fitting: a practical guide to combine cryo-electron microscopy and X-ray crystallography. Methods 49:174-180.
    • (2009) Methods , vol.49 , pp. 174-180
    • Trabuco, L.G.1    Villa, E.2    Schreiner, E.3    Harrison, C.B.4    Schulten, K.5
  • 35
    • 34249313614 scopus 로고    scopus 로고
    • U.S. Department of Health and Human Services. 5th ed. U.S. Government Printing Office, Washington, DC
    • U.S. Department of Health and Human Services. 2007. Biosafety in microbiological and biomedical laboratories, 5th ed. U.S. Government Printing Office, Washington, DC.
    • (2007) Biosafety in microbiological and biomedical laboratories
  • 36
    • 78649817910 scopus 로고    scopus 로고
    • Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography
    • Voss, J. E., et al. 2010. Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography. Nature 468:709-712.
    • (2010) Nature , vol.468 , pp. 709-712
    • Voss, J.E.1
  • 37
    • 0023858978 scopus 로고
    • Location of a major antigenic site involved in Ross River virus neutralization
    • Vrati, S., C. A. Fernon, L. Dalgarno, and R. C. Weir. 1988. Location of a major antigenic site involved in Ross River virus neutralization. Virology 162:346-353.
    • (1988) Virology , vol.162 , pp. 346-353
    • Vrati, S.1    Fernon, C.A.2    Dalgarno, L.3    Weir, R.C.4
  • 38
    • 33644608432 scopus 로고    scopus 로고
    • Role of a conserved tripeptide in the endodomain of Sindbis virus glycoprotein E2 in virus assembly and function
    • West, J., and D. T. Brown. 2006. Role of a conserved tripeptide in the endodomain of Sindbis virus glycoprotein E2 in virus assembly and function. J. Gen. Virol. 87:657-664.
    • (2006) J. Gen. Virol. , vol.87 , pp. 657-664
    • West, J.1    Brown, D.T.2
  • 39
    • 33646198240 scopus 로고    scopus 로고
    • Mutations in the endodomain of Sindbis virus glycoprotein E2 define sequences critical for virus assembly
    • West, J., R. Hernandez, D. Ferreira, and D. T. Brown. 2006. Mutations in the endodomain of Sindbis virus glycoprotein E2 define sequences critical for virus assembly. J. Virol. 80:4458-4468.
    • (2006) J. Virol. , vol.80 , pp. 4458-4468
    • West, J.1    Hernandez, R.2    Ferreira, D.3    Brown, D.T.4
  • 40
    • 0036827856 scopus 로고    scopus 로고
    • Placement of the structural proteins in Sindbis virus
    • Zhang, W., et al. 2002. Placement of the structural proteins in Sindbis virus. J. Virol. 76:11645-11658.
    • (2002) J. Virol. , vol.76 , pp. 11645-11658
    • Zhang, W.1


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