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Volumn 107, Issue 14, 2010, Pages 6292-6297

Bluetongue virus coat protein VP2 contains sialic acid-binding domains, and VP5 resembles enveloped virus fusion proteins

Author keywords

Cryo electron microscopy; dsRNA virus structure; Membrane penetration protein; Sialic acid binding protein

Indexed keywords

AMINO ACID; COAT PROTEIN; DOUBLE STRANDED RNA; PROTEIN VP2; SIALIC ACID; SUGAR; VIRUS FUSION PROTEIN;

EID: 77950907290     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0913403107     Document Type: Article
Times cited : (97)

References (43)
  • 3
    • 58449099320 scopus 로고    scopus 로고
    • Prospects for improved bluetongue vaccines
    • Roy P, Boyce M, Noad R (2009) Prospects for improved bluetongue vaccines. Nat Rev Microbiol 7:120-128.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 120-128
    • Roy, P.1    Boyce, M.2    Noad, R.3
  • 4
    • 0024978523 scopus 로고
    • Expression of largest RNA segment and synthesis of VP1 protein of bluetongue virus in insect cells by recombinant baculovirus: Association of VP1 protein with RNA polymerase activity
    • Urakawa T, Ritter DG, Roy P (1989) Expression of largest RNA segment and synthesis of VP1 protein of bluetongue virus in insect cells by recombinant baculovirus: Association of VP1 protein with RNA polymerase activity. Nucleic Acids Res 17:7395-7401.
    • (1989) Nucleic Acids Res , vol.17 , pp. 7395-7401
    • Urakawa, T.1    Ritter, D.G.2    Roy, P.3
  • 5
    • 1842329184 scopus 로고    scopus 로고
    • Bluetongue virus VP6 protein binds ATP and exhibits an RNA-dependent ATPase function and a helicase activity that catalyze the unwinding of double-stranded RNA substrates
    • Stauber N, et al. (1997) Bluetongue virus VP6 protein binds ATP and exhibits an RNA-dependent ATPase function and a helicase activity that catalyze the unwinding of double-stranded RNA substrates. J Virol 71:7220-7226. (Pubitemid 27391656)
    • (1997) Journal of Virology , vol.71 , Issue.10 , pp. 7220-7226
    • Stauber, N.1    Martinez-Costas, J.2    Sutton, G.3    Monastyrskaya, K.4    Roy, P.5
  • 7
    • 50549097204 scopus 로고    scopus 로고
    • Bluetongue virus: Dissection of the polymerase complex
    • Roy P (2008) Bluetongue virus: Dissection of the polymerase complex. J Gen Virol 89:1789-1804.
    • (2008) J Gen Virol , vol.89 , pp. 1789-1804
    • Roy, P.1
  • 8
    • 0032189765 scopus 로고    scopus 로고
    • The atomic structure of the bluetongue virus core
    • Grimes JM, et al. (1998) The atomic structure of the bluetongue virus core. Nature 395:470-478.
    • (1998) Nature , vol.395 , pp. 470-478
    • Grimes, J.M.1
  • 9
    • 2942703320 scopus 로고    scopus 로고
    • Interactions between the inner and outer capsids of bluetongue virus
    • Nason EL, et al. (2004) Interactions between the inner and outer capsids of bluetongue virus. J Virol 78:8059-8067.
    • (2004) J Virol , vol.78 , pp. 8059-8067
    • Nason, E.L.1
  • 10
    • 55249086106 scopus 로고    scopus 로고
    • Bluetongue virus outer capsid protein VP5 interacts with membrane lipid rafts via a SNARE domain
    • DOI 10.1128/JVI.01274-08
    • Bhattacharya B, Roy P (2008) Bluetongue virus outer capsid protein VP5 interacts with membrane lipid rafts via a SNARE domain. J Virol 82:10600-10612. (Pubitemid 352691148)
    • (2008) Journal of Virology , vol.82 , Issue.21 , pp. 10600-10612
    • Bhattacharya, B.1    Roy, P.2
  • 12
    • 0032780181 scopus 로고    scopus 로고
    • Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
    • DOI 10.1006/jsbi.1998.4080
    • Wriggers W, Milligan RA, McCammon JA (1999) Situs: A package for docking crystal structures into low-resolution maps from electron microscopy. J Struct Biol 125:185-195. (Pubitemid 29402603)
    • (1999) Journal of Structural Biology , vol.125 , Issue.2-3 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 13
    • 0032710383 scopus 로고    scopus 로고
    • Expression and functional characterization of bluetongue virus VP2 protein: Role in cell entry
    • Hassan SS, Roy P (1999) Expression and functional characterization of bluetongue virus VP2 protein: Role in cell entry. J Virol 73:9832-9842.
    • (1999) J Virol , vol.73 , pp. 9832-9842
    • Hassan, S.S.1    Roy, P.2
  • 14
    • 0036500085 scopus 로고    scopus 로고
    • The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site
    • DOI 10.1093/emboj/21.5.885
    • Dormitzer PR, Sun ZY, Wagner G, Harrison SC (2002) The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site. EMBO J 21:885-897. (Pubitemid 34206162)
    • (2002) EMBO Journal , vol.21 , Issue.5 , pp. 885-897
    • Dormitzer, P.R.1    Sun, Z.-Y.J.2    Wagner, G.3    Harrison, S.C.4
  • 15
    • 0024853528 scopus 로고
    • The site of bluetongue virus attachment to glycophorins from a number of animal erythrocytes
    • Eaton BT, Crameri GS (1989) The site of bluetongue virus attachment to glycophorins from a number of animal erythrocytes. J Gen Virol 70(12):3347-3353.
    • (1989) J Gen Virol , vol.70 , Issue.12 , pp. 3347-3353
    • Eaton, B.T.1    Crameri, G.S.2
  • 16
    • 0015541815 scopus 로고
    • The purification, composition and specificity of wheat-germ agglutinin
    • Allen AK, Neuberger A, Sharon N (1973) The purification, composition and specificity of wheat-germ agglutinin. Biochem J 131:155-162.
    • (1973) Biochem J , vol.131 , pp. 155-162
    • Allen, A.K.1    Neuberger, A.2    Sharon, N.3
  • 17
    • 0037169362 scopus 로고    scopus 로고
    • Structure of the reovirus membrane-penetration protein, Mu1, in a complex with its protector protein, Sigma3
    • DOI 10.1016/S0092-8674(02)00612-8
    • Liemann S, et al. (2002) Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3. Cell 108:283-295. (Pubitemid 34161147)
    • (2002) Cell , vol.108 , Issue.2 , pp. 283-295
    • Liemann, S.1    Chandran, K.2    Baker, T.S.3    Nibert, M.L.4    Harrison, S.C.5
  • 18
  • 19
    • 23144444979 scopus 로고    scopus 로고
    • Protein structure prediction servers at University College London
    • Bryson K, et al. (2005) Protein structure prediction servers at University College London. Nucleic Acids Res 33:W36-38.
    • (2005) Nucleic Acids Res , vol.33
    • Bryson, K.1
  • 20
    • 0034814786 scopus 로고    scopus 로고
    • Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus
    • Zhou ZH, et al. (2001) Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus. Nat Struct Biol 8:868-873.
    • (2001) Nat Struct Biol , vol.8 , pp. 868-873
    • Zhou, Z.H.1
  • 22
    • 44849089725 scopus 로고    scopus 로고
    • Functional mapping of bluetongue virus proteins and their interactions with host proteins during virus replication
    • Roy P (2008) Functional mapping of bluetongue virus proteins and their interactions with host proteins during virus replication. Cell Biochem Biophys 50:143-157.
    • (2008) Cell Biochem Biophys , vol.50 , pp. 143-157
    • Roy, P.1
  • 23
    • 0034892675 scopus 로고    scopus 로고
    • Expression and functional characterization of bluetongue virus VP5 protein: Role in cellular permeabilization
    • DOI 10.1128/JVI.75.18.8356-8367.2001
    • Hassan SH, Wirblich C, Forzan M, Roy P (2001) Expression and functional characterization of bluetongue virus VP5 protein: Role in cellular permeabilization. J Virol 75:8356-8367. (Pubitemid 32768940)
    • (2001) Journal of Virology , vol.75 , Issue.18 , pp. 8356-8367
    • Hassan, S.H.1    Wirblich, C.2    Forzan, M.3    Roy, P.4
  • 26
    • 0026799307 scopus 로고
    • Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: Analysis by proton nuclear magnetic resonance spectroscopy and x-ray crystallography
    • Sauter NK, et al. (1992) Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: Analysis by proton nuclear magnetic resonance spectroscopy and x-ray crystallography. Biochemistry 31:9609-9621.
    • (1992) Biochemistry , vol.31 , pp. 9609-9621
    • Sauter, N.K.1
  • 27
    • 33846959065 scopus 로고    scopus 로고
    • Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G
    • DOI 10.1126/science.1135710
    • Roche S, Rey FA, Gaudin Y, Bressanelli S (2007) Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G. Science 315:843-848. (Pubitemid 46255836)
    • (2007) Science , vol.315 , Issue.5813 , pp. 843-848
    • Roche, S.1    Rey, F.A.2    Gaudin, Y.3    Bressanelli, S.4
  • 29
    • 4344695186 scopus 로고    scopus 로고
    • Structural rearrangements in the membrane penetration protein of a non-enveloped virus
    • Dormitzer PR, Nason EB, Prasad BV, Harrison SC (2004) Structural rearrangements in the membrane penetration protein of a non-enveloped virus. Nature 430:1053-1058.
    • (2004) Nature , vol.430 , pp. 1053-1058
    • Dormitzer, P.R.1    Nason, E.B.2    Prasad, B.V.3    Harrison, S.C.4
  • 30
    • 34447502257 scopus 로고    scopus 로고
    • Cell entry by enveloped viruses: Redox considerations for HIV and SARS-coronavirus
    • DOI 10.1089/ars.2007.1639
    • Fenouillet E, Barbouche R, Jones IM (2007) Cell entry by enveloped viruses: Redox considerations for HIV and SARS-coronavirus. Antioxid Redox Signal 9:1009-1034. (Pubitemid 47080818)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.8 , pp. 1009-1034
    • Fenouillet, E.1    Barbouche, R.2    Jones, I.M.3
  • 31
    • 59749086300 scopus 로고    scopus 로고
    • Early events during BK virus entry and disassembly
    • Jiang M, Abend JR, Tsai B, Imperiale MJ (2009) Early events during BK virus entry and disassembly. J Virol 83:1350-1358.
    • (2009) J Virol , vol.83 , pp. 1350-1358
    • Jiang, M.1    Abend, J.R.2    Tsai, B.3    Imperiale, M.J.4
  • 32
    • 0023121587 scopus 로고
    • Isolation of a capsid protein of bluetongue virus that induces a protective immune response in sheep
    • DOI 10.1016/0042-6822(87)90326-6
    • Huismans H, van der Walt NT, CloeteM, Erasmus BJ (1987) Isolation of a capsid protein of bluetongue virus that induces a protective immune response in sheep. Virology 157:172-179. (Pubitemid 17029995)
    • (1987) Virology , vol.157 , Issue.1 , pp. 172-179
    • Huismans, H.1    Van Der Walt, N.T.2    Cloete, M.3    Erasmus, B.J.4
  • 33
    • 0029154702 scopus 로고
    • Analysis of the cell and erythrocyte binding activities of the dimple and canyon regions of the canine parvovirus capsid
    • Tresnan DB, et al. (1995) Analysis of the cell and erythrocyte binding activities of the dimple and canyon regions of the canine parvovirus capsid. Virology 211:123-132.
    • (1995) Virology , vol.211 , pp. 123-132
    • Tresnan, D.B.1
  • 34
    • 0028135695 scopus 로고
    • Identification of a 40- To 42-kDa attachment polypeptide for canine parvovirus in A72 cells
    • DOI 10.1006/viro.1994.1614
    • Basak S, Turner H, Parr S (1994) Identification of a 40- to 42-kDa attachment polypeptide for canine parvovirus in A72 cells. Virology 205:207-216 (Pubitemid 24360585)
    • (1994) Virology , vol.205 , Issue.1 , pp. 7-16
    • Basak, S.1    Turner, H.2    Parr, S.3
  • 35
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel JJ, Wiley DC (2000) Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin. Annu Rev Biochem 69:531-569.
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 36
    • 50149089970 scopus 로고    scopus 로고
    • Development of reverse genetics systems for bluetongue virus: Recovery of infectious virus from synthetic RNA transcripts
    • Boyce M, Celma CC, Roy P (2008) Development of reverse genetics systems for bluetongue virus: Recovery of infectious virus from synthetic RNA transcripts. J Virol 82:8339-8348.
    • (2008) J Virol , vol.82 , pp. 8339-8348
    • Boyce, M.1    Celma, C.C.2    Roy, P.3
  • 37
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell JA, Grigorieff N (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142:334-347.
    • (2003) J Struct Biol , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 38
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semi-automated software for high resolution single particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semi-automated 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
  • 39
    • 0036420061 scopus 로고    scopus 로고
    • IMIRS: A high-resolution 3D reconstruction package integrated with a relational image database
    • DOI 10.1016/S1047-8477(02)00014-X, PII S104784770200014X
    • Liang Y, Ke EY, Zhou ZH (2002) IMIRS: A high-resolution 3D reconstruction package integrated with a relational image database. J Struct Biol 137:292-304. (Pubitemid 35304474)
    • (2002) Journal of Structural Biology , vol.137 , Issue.3 , pp. 292-304
    • Liang, Y.1    Ke, E.Y.2    Zhou, Z.H.3
  • 40
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: High-resolution refinement of single particle structures
    • DOI 10.1016/j.jsb.2006.05.004, PII S1047847706001699, Software Tools for Macromolecular Microscopy
    • Grigorieff N (2007) FREALIGN: High-resolution refinement of single particle structures. J Struct Biol 157:117-125. (Pubitemid 44880784)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 117-125
    • Grigorieff, N.1
  • 41
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal PB, Henderson R (2003) Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol 333:721-745
    • (2003) J Mol Biol , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 43
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - a visualization system for exploratory research and analysis
    • Pettersen EF, 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


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