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Volumn 13, Issue 1, 2005, Pages 17-28

The structure and function of the outer coat protein VP9 of Banna virus

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; GENE PRODUCT; GLYCOPROTEIN GP 41; NEUTRALIZING ANTIBODY; OUTER CAPSID PROTEIN; PROTEIN VP8; PROTEIN VP9; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; VIRUS PROTEIN;

EID: 19944426595     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2004.10.017     Document Type: Article
Times cited : (32)

References (60)
  • 1
    • 0028815675 scopus 로고
    • Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH
    • S.L. Allison, J. Schalich, K. Stiasny, C.W. Mandl, C. Kunz, and F.X. Heinz Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH J. Virol. 69 1995 695 700
    • (1995) J. Virol. , vol.69 , pp. 695-700
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 2
    • 0034117552 scopus 로고    scopus 로고
    • Complete sequence determination and genetic analysis of Banna virus and Kadipiro virus: Proposal for assignment to a new genus (Seadornavirus) within the family Reoviridae
    • H. Attoui, F. Billoir, P. Biagini, P. de Micco, and X. de Lamballerie Complete sequence determination and genetic analysis of Banna virus and Kadipiro virus: proposal for assignment to a new genus (Seadornavirus) within the family Reoviridae J. Gen. Virol. 81 2000 1507 1515
    • (2000) J. Gen. Virol. , vol.81 , pp. 1507-1515
    • Attoui, H.1    Billoir, F.2    Biagini, P.3    De Micco, P.4    De Lamballerie, X.5
  • 4
    • 0032712359 scopus 로고    scopus 로고
    • Adding the third dimension to virus life cycles: Three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs
    • T.S. Baker, N.H. Olson, and S.D. Fuller Adding the third dimension to virus life cycles: three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs Microbiol. Mol. Biol. Rev. 63 1999 862 922
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 862-922
    • Baker, T.S.1    Olson, N.H.2    Fuller, S.D.3
  • 7
    • 0027255286 scopus 로고
    • Coltiviruses isolated from mosquitoes collected in Indonesia
    • S.E. Brown, M. Gorman, R.B. Tesh, and D.L. Knudson Coltiviruses isolated from mosquitoes collected in Indonesia Virology 196 1993 363 367
    • (1993) Virology , vol.196 , pp. 363-367
    • Brown, S.E.1    Gorman, M.2    Tesh, R.B.3    Knudson, D.L.4
  • 10
    • 0027992057 scopus 로고
    • Purification and properties of virus particles, infectious subviral particles, cores and VP7 crystals of African horsesickness virus serotype 9
    • J.N. Burroughs, R.S. O'Hara, C.J. Smale, C. Hamblin, A. Walton, R. Armstrong, and P.P.C. Mertens Purification and properties of virus particles, infectious subviral particles, cores and VP7 crystals of African horsesickness virus serotype 9 J. Gen. Virol. 75 1994 1849 1857
    • (1994) J. Gen. Virol. , vol.75 , pp. 1849-1857
    • Burroughs, J.N.1    O'Hara, R.S.2    Smale, C.J.3    Hamblin, C.4    Walton, A.5    Armstrong, R.6    Mertens, P.P.C.7
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 12
    • 0032899595 scopus 로고    scopus 로고
    • In vitro recoating of reovirus cores with baculovirus-expressed outer capsid proteins Mu1 and Sigma3
    • K. Chandran, S.B. Walker, Y. Chen, C.M. Contreras, L.A. Schiff, T.S. Baker, and M.L. Nibert In vitro recoating of reovirus cores with baculovirus-expressed outer capsid proteins Mu1 and Sigma3 J. Virol. 73 1999 3941 3950
    • (1999) J. Virol. , vol.73 , pp. 3941-3950
    • Chandran, K.1    Walker, S.B.2    Chen, Y.3    Contreras, C.M.4    Schiff, L.A.5    Baker, T.S.6    Nibert, M.L.7
  • 13
    • 0035036348 scopus 로고    scopus 로고
    • Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein
    • K. Chandran, X. Zhang, N.H. Olson, S.B. Walker, J.D. Chappell, T.S. Dermody, T.S. Baker, and M.L. Nibert Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein J. Virol. 75 2001 5335 5342
    • (2001) J. Virol. , vol.75 , pp. 5335-5342
    • Chandran, K.1    Zhang, X.2    Olson, N.H.3    Walker, S.B.4    Chappell, J.D.5    Dermody, T.S.6    Baker, T.S.7    Nibert, M.L.8
  • 14
    • 0030982689 scopus 로고    scopus 로고
    • Solubilized and cleaved VP7, the outer glycoprotein of rotavirus, induces permeabilization of cell membrane vesicles
    • A. Charpilienne, M.J. Abad, F. Michelangeli, F. Alvarado, M. Vasseur, J. Cohen, and M.C. Ruiz Solubilized and cleaved VP7, the outer glycoprotein of rotavirus, induces permeabilization of cell membrane vesicles J. Gen. Virol. 78 1997 1367 1371
    • (1997) J. Gen. Virol. , vol.78 , pp. 1367-1371
    • Charpilienne, A.1    Abad, M.J.2    Michelangeli, F.3    Alvarado, F.4    Vasseur, M.5    Cohen, J.6    Ruiz, M.C.7
  • 15
    • 0029678921 scopus 로고    scopus 로고
    • Arbovirus survey in China in recent ten years
    • B. Chen, and S. Tao Arbovirus survey in China in recent ten years Chin. Med. J. (Engl.) 109 1996 13 15
    • (1996) Chin. Med. J. (Engl.) , vol.109 , pp. 13-15
    • Chen, B.1    Tao, S.2
  • 17
    • 0034715826 scopus 로고    scopus 로고
    • Purified recombinant rotavirus VP7 forms soluble, calcium-dependent trimers
    • P.R. Dormitzer, H.B. Greenberg, and S.C. Harrison Purified recombinant rotavirus VP7 forms soluble, calcium-dependent trimers Virology 277 2000 420 428
    • (2000) Virology , vol.277 , pp. 420-428
    • Dormitzer, P.R.1    Greenberg, H.B.2    Harrison, S.C.3
  • 18
    • 0036500085 scopus 로고    scopus 로고
    • The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site
    • P.R. Dormitzer, Z.Y. Sun, G. Wagner, and S.C. Harrison The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site EMBO J. 21 2002 885 897
    • (2002) EMBO J. , vol.21 , pp. 885-897
    • Dormitzer, P.R.1    Sun, Z.Y.2    Wagner, G.3    Harrison, S.C.4
  • 20
    • 0033937215 scopus 로고    scopus 로고
    • Selective membrane permeabilization by the rotavirus VP5* protein is abrogated by mutations in an internal hydrophobic domain
    • W. Dowling, E. Denisova, R. LaMonica, and E.R. Mackow Selective membrane permeabilization by the rotavirus VP5* protein is abrogated by mutations in an internal hydrophobic domain J. Virol. 74 2000 6368 6376
    • (2000) J. Virol. , vol.74 , pp. 6368-6376
    • Dowling, W.1    Denisova, E.2    Lamonica, R.3    MacKow, E.R.4
  • 21
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • R.M. Esnouf Further additions to MolScript version 1.4, including reading and contouring of electron-density maps Acta Crystallogr. D Biol. Crystallogr. 55 1999 938 940
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 22
    • 0001581287 scopus 로고    scopus 로고
    • Rotaviruses and their replication
    • D.M. Knipe P.M. Howley Lippincott Williams and Wilkins Philadelphia
    • M.K. Estes Rotaviruses and their replication D.M. Knipe P.M. Howley Fields Virology 2001 Lippincott Williams and Wilkins Philadelphia 1747 1785
    • (2001) Fields Virology , pp. 1747-1785
    • Estes, M.K.1
  • 23
    • 1242319267 scopus 로고    scopus 로고
    • A capsid protein of nonenveloped Bluetongue virus exhibits membrane fusion activity
    • M. Forzan, C. Wirblich, and P. Roy A capsid protein of nonenveloped Bluetongue virus exhibits membrane fusion activity Proc. Natl. Acad. Sci. USA 101 2004 2100 2105
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2100-2105
    • Forzan, M.1    Wirblich, C.2    Roy, P.3
  • 25
    • 0842325991 scopus 로고    scopus 로고
    • Discrete domains within the rotavirus VP5* direct peripheral membrane association and membrane permeability
    • N.E. Golantsova, E.E. Gorbunova, and E.R. Mackow Discrete domains within the rotavirus VP5* direct peripheral membrane association and membrane permeability J. Virol. 78 2004 2037 2044
    • (2004) J. Virol. , vol.78 , pp. 2037-2044
    • Golantsova, N.E.1    Gorbunova, E.E.2    MacKow, E.R.3
  • 26
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • P. Gouet, E. Courcelle, D.I. Stuart, and F. Metoz ESPript: analysis of multiple sequence alignments in PostScript Bioinformatics 15 1999 305 308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 27
    • 0034284847 scopus 로고    scopus 로고
    • Oligomerization and cell-binding properties of the avian reovirus cell-attachment protein sigmaC
    • A. Grande, E. Rodriguez, C. Costas, E. Everitt, and J. Benavente Oligomerization and cell-binding properties of the avian reovirus cell-attachment protein sigmaC Virology 274 2000 367 377
    • (2000) Virology , vol.274 , pp. 367-377
    • Grande, A.1    Rodriguez, E.2    Costas, C.3    Everitt, E.4    Benavente, J.5
  • 29
    • 0034892675 scopus 로고    scopus 로고
    • Expression and functional characterization of bluetongue virus vp2 protein: Role in cell entry
    • S.H. Hassan, and P. Roy Expression and functional characterization of bluetongue virus vp2 protein: role in cell entry J. Virol. 75 1999 8356 8367
    • (1999) J. Virol. , vol.75 , pp. 8356-8367
    • Hassan, S.H.1    Roy, P.2
  • 30
    • 0034892675 scopus 로고    scopus 로고
    • Expression and functional characterization of bluetongue virus vp5 protein: Role in cellular permeabilization
    • S.H. Hassan, C. Wirblich, M. Forzan, and P. Roy Expression and functional characterization of bluetongue virus vp5 protein: role in cellular permeabilization Virology 75 2001 8356 8367
    • (2001) Virology , vol.75 , pp. 8356-8367
    • Hassan, S.H.1    Wirblich, C.2    Forzan, M.3    Roy, P.4
  • 32
    • 0345196599 scopus 로고    scopus 로고
    • Reovirus virion-like particles obtained by recoating infectiuos subvirion particles with baculovirus-expressed sigma3 protein: An approach for analysing sigma3 functions during virus entry
    • J. Jane-Valbuena, M.L. Nibert, S.M. Spencer, S.B. Walker, T.S. Baker, Y. Chen, V.E. Centonze, and L.A. Schiff Reovirus virion-like particles obtained by recoating infectiuos subvirion particles with baculovirus-expressed sigma3 protein: an approach for analysing sigma3 functions during virus entry J. Virol. 73 1999 2963 2973
    • (1999) J. Virol. , vol.73 , pp. 2963-2973
    • Jane-Valbuena, J.1    Nibert, M.L.2    Spencer, S.M.3    Walker, S.B.4    Baker, T.S.5    Chen, Y.6    Centonze, V.E.7    Schiff, L.A.8
  • 33
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • J. Janin, S. Miller, and C. Chothia Surface, subunit interfaces and interior of oligomeric proteins J. Mol. Biol. 204 1988 155 164
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 34
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 1991 110 119
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 35
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 37
    • 11844284745 scopus 로고
    • First isolation of 8 strains of new orbivirus (Banna) from patients with innominate fever in Xinjiang
    • Q.P. Li First isolation of 8 strains of new orbivirus (Banna) from patients with innominate fever in Xinjiang Endemic Dis. Bull. 7 1992 77 82
    • (1992) Endemic Dis. Bull. , vol.7 , pp. 77-82
    • Li, Q.P.1
  • 38
    • 0027257854 scopus 로고
    • Binding to sialic acids is not an essential step for the entry of animal rotaviruses to epithelial cells in culture
    • E. Mendez, C.F. Arias, and S. Lopez Binding to sialic acids is not an essential step for the entry of animal rotaviruses to epithelial cells in culture J. Virol. 67 1993 5253 5259
    • (1993) J. Virol. , vol.67 , pp. 5253-5259
    • Mendez, E.1    Arias, C.F.2    Lopez, S.3
  • 39
    • 1542328804 scopus 로고    scopus 로고
    • The dsRNA viruses
    • P.P.C. Mertens The dsRNA viruses Virus Res. 101 2004 3 13
    • (2004) Virus Res. , vol.101 , pp. 3-13
    • Mertens, P.P.C.1
  • 43
    • 0014284002 scopus 로고
    • Colorado tick fever virus: An electron microscopy study
    • F.A. Murphy, P.H. Coleman, A.K. Harrison, and W.G. Gary Colorado tick fever virus: an electron microscopy study Virology 35 1968 28 40
    • (1968) Virology , vol.35 , pp. 28-40
    • Murphy, F.A.1    Coleman, P.H.2    Harrison, A.K.3    Gary, W.G.4
  • 44
    • 0001123624 scopus 로고    scopus 로고
    • Reoviruses and their replication
    • D.M. Knipe P.M. Howley Lippincott Williams and Wilkins New York
    • M.L. Nibert, and L.A. Schiff Reoviruses and their replication D.M. Knipe P.M. Howley Fields Virology 2001 Lippincott Williams and Wilkins New York 1679 1728
    • (2001) Fields Virology , pp. 1679-1728
    • Nibert, M.L.1    Schiff, L.A.2
  • 45
    • 0029058860 scopus 로고
    • Infectious subvirion particles of reovirus type 3 dearing exhibit a loss in infectivity and contain a cleaved s1 protein
    • M.L. Nibert, J.D. Chappell, and T.S. Dermody Infectious subvirion particles of reovirus type 3 dearing exhibit a loss in infectivity and contain a cleaved s1 protein J. Virol. 69 1995 5057 5067
    • (1995) J. Virol. , vol.69 , pp. 5057-5067
    • Nibert, M.L.1    Chappell, J.D.2    Dermody, T.S.3
  • 46
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • A. Nicholls, K.A. Sharp, and B. Honig Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons Proteins 11 1991 281 296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 47
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 48
    • 0025178591 scopus 로고
    • Localization of VP4 neutralization sites in rotavirus by three-dimensional cryo-electron microscopy
    • B.V. Prasad, J.W. Burns, E. Marietta, M.K. Estes, and W. Chiu Localization of VP4 neutralization sites in rotavirus by three-dimensional cryo-electron microscopy Nature 343 1990 476 479
    • (1990) Nature , vol.343 , pp. 476-479
    • Prasad, B.V.1    Burns, J.W.2    Marietta, E.3    Estes, M.K.4    Chiu, W.5
  • 49
    • 0025900084 scopus 로고
    • Antibodies to the trypsin cleavage peptide VP8 neutralize rotavirus by inhibiting binding of virions to target cells in culture
    • F.M. Ruggeri, and H.B. Greenberg Antibodies to the trypsin cleavage peptide VP8 neutralize rotavirus by inhibiting binding of virions to target cells in culture J. Virol. 65 1991 2211 2219
    • (1991) J. Virol. , vol.65 , pp. 2211-2219
    • Ruggeri, F.M.1    Greenberg, H.B.2
  • 50
    • 0030778980 scopus 로고    scopus 로고
    • Structure of broadhaven virus by cryoelectron microscopy: Correlation of structural and antigenic properties of broadhaven virus and bluetongue virus outer capsid proteins
    • G. Schoehn, S.R. Moss, P.A. Nuttall, and E.A. Hewat Structure of broadhaven virus by cryoelectron microscopy: correlation of structural and antigenic properties of broadhaven virus and bluetongue virus outer capsid proteins Virology 235 1997 191 200
    • (1997) Virology , vol.235 , pp. 191-200
    • Schoehn, G.1    Moss, S.R.2    Nuttall, P.A.3    Hewat, E.A.4
  • 51
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • J.J. Skehel, and D.C. Wiley Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin Annu. Rev. Biochem. 69 2000 531 569
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 52
    • 0018792428 scopus 로고
    • Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 Å
    • D.I. Stuart, M. Levine, H. Muirhead, and D.K. Stammers Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 Å J. Mol. Biol. 134 1979 109 142
    • (1979) J. Mol. Biol. , vol.134 , pp. 109-142
    • Stuart, D.I.1    Levine, M.2    Muirhead, H.3    Stammers, D.K.4
  • 53
    • 0027186211 scopus 로고
    • Electron microscopic evidence for budding process-independent assembly of double-shelled rotavirus particles during passage through endoplasmic reticulum membranes
    • H. Suzuki, T. Konno, and Y. Numazaki Electron microscopic evidence for budding process-independent assembly of double-shelled rotavirus particles during passage through endoplasmic reticulum membranes J. Gen. Virol. 74 1993 2015 2018
    • (1993) J. Gen. Virol. , vol.74 , pp. 2015-2018
    • Suzuki, H.1    Konno, T.2    Numazaki, Y.3
  • 55
    • 0038793604 scopus 로고    scopus 로고
    • Improving macromolecular atomic models at moderate resolution by automated iterative model building, statistical density modification and refinement
    • T.C. Terwilliger Improving macromolecular atomic models at moderate resolution by automated iterative model building, statistical density modification and refinement Acta Crystallogr. D Biol. Crystallogr. 59 2003 1174 1182
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 1174-1182
    • Terwilliger, T.C.1
  • 57
    • 0037391746 scopus 로고    scopus 로고
    • A procedure for setting up high-throughput, nanolitre crystallisation experiments. I. Protocol design and validation
    • T.S. Walter, J. Diprose, J. Brown, M. Pickford, R.J. Owens, D.I. Stuart, and K. Harlos A procedure for setting up high-throughput, nanolitre crystallisation experiments. I. Protocol design and validation J. Appl. Crystallogr. 36 2003 308 314
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 308-314
    • Walter, T.S.1    Diprose, J.2    Brown, J.3    Pickford, M.4    Owens, R.J.5    Stuart, D.I.6    Harlos, K.7
  • 58
    • 0003413082 scopus 로고
    • New orbiviruses isolated from patients with unknown fever and encephalitis in Yunnan province
    • P. Xu, Y. Wang, J. Zuo, J. Lin, and P. Xu New orbiviruses isolated from patients with unknown fever and encephalitis in Yunnan province Chin. J. Virol. 6 1990 27 33
    • (1990) Chin. J. Virol. , vol.6 , pp. 27-33
    • Xu, P.1    Wang, Y.2    Zuo, J.3    Lin, J.4    Xu, P.5
  • 60
    • 0030802761 scopus 로고    scopus 로고
    • Details of the arrangement of the outer capsid of rice dwarf phytoreovirus, as visualized by two-dimensional crystallography
    • P. Zhu, A.M. Hemmings, K. Iwasaki, Y. Fujiyoshi, B. Zhong, J. Yan, M. Isogai, and T. Omura Details of the arrangement of the outer capsid of rice dwarf phytoreovirus, as visualized by two-dimensional crystallography J. Virol. 71 1997 8899 8901
    • (1997) J. Virol. , vol.71 , pp. 8899-8901
    • Zhu, P.1    Hemmings, A.M.2    Iwasaki, K.3    Fujiyoshi, Y.4    Zhong, B.5    Yan, J.6    Isogai, M.7    Omura, T.8


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