메뉴 건너뛰기




Volumn 87, Issue 13, 2013, Pages 7637-7645

Structures of the procapsid and mature virion of enterovirus 71 strain 1095

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; SINGLE STRANDED RNA;

EID: 84880372616     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03519-12     Document Type: Article
Times cited : (36)

References (64)
  • 1
    • 0016257919 scopus 로고
    • An apparently new enterovirus isolated from patients with disease of the central nervous system
    • Schmidt NJ, Lennette EH, Ho HH. 1974. An apparently new enterovirus isolated from patients with disease of the central nervous system. J. Infect. Dis. 129:304-309.
    • (1974) J. Infect. Dis , vol.129 , pp. 304-309
    • Schmidt, N.J.1    Lennette, E.H.2    Ho, H.H.3
  • 2
    • 84880394209 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 5
    • 68549121126 scopus 로고    scopus 로고
    • Emerging viral infections of the central nervous system: part 1
    • Tyler KL. 2009. Emerging viral infections of the central nervous system: part 1. Arch. Neurol. 66:939-948.
    • (2009) Arch. Neurol , vol.66 , pp. 939-948
    • Tyler, K.L.1
  • 6
    • 79956293299 scopus 로고    scopus 로고
    • apping genetic determinants of the cell-culture growth phenotype of enterovirus 71
    • Phuektes P, Chua BH, Sanders S, Bek EJ, Kok CC, Mc-Minn PC. 2011. Mapping genetic determinants of the cell-culture growth phenotype of enterovirus 71. J. Gen. Virol. 92:1380-1390.
    • (2011) J. Gen. Virol , vol.92 , pp. 1380-1390
    • Phuektes, P.1    Chua, B.H.2    Sanders, S.3    Bek, E.J.4    Kok, C.C.5    Mc-Minn, P.C.6
  • 11
    • 80054790178 scopus 로고    scopus 로고
    • Molecular analysis of virulent determinants of enterovirus 71
    • doi:10.1371 /journal.pone.0026237
    • Li R, Zou Q, Chen L, Zhang H, Wang Y. 2011. Molecular analysis of virulent determinants of enterovirus 71. PLoS One 6:e26237. doi:10.1371 /journal.pone.0026237.
    • (2011) PLoS One 6:e26237
    • Li, R.1    Zou, Q.2    Chen, L.3    Zhang, H.4    Wang, Y.5
  • 12
    • 77949394259 scopus 로고    scopus 로고
    • Evolutionary genetics of human enterovirus 71: origin, population dynamics, natural selection, and seasonal periodic- ity of the VP1 gene
    • Tee KK, Lam TT, Chan YF, Bible JM, Kamarulzaman A, Tong CY, Takebe Y, Pybus OG. 2010. Evolutionary genetics of human enterovirus 71: origin, population dynamics, natural selection, and seasonal periodic- ity of the VP1 gene. J. Virol. 84:3339-3350.
    • (2010) J. Virol , vol.84 , pp. 3339-3350
    • Tee, K.K.1    Lam, T.T.2    Chan, Y.F.3    Bible, J.M.4    Kamarulzaman, A.5    Tong, C.Y.6    Takebe, Y.7    Pybus, O.G.8
  • 13
    • 67650491431 scopus 로고    scopus 로고
    • Human P-selectin glycoprotein ligand-1 is a functional receptor for enterovirus 71
    • Nishimura Y, Shimojima M, Tano Y, Miyamura T, Wakita T, Shimizu H. 2009. Human P-selectin glycoprotein ligand-1 is a functional receptor for enterovirus 71. Nat. Med. 15:794-797.
    • (2009) Nat. Med , vol.15 , pp. 794-797
    • Nishimura, Y.1    Shimojima, M.2    Tano, Y.3    Miyamura, T.4    Wakita, T.5    Shimizu, H.6
  • 16
    • 70349659503 scopus 로고    scopus 로고
    • Sialylated glycans as receptor and inhibitor of enterovirus 71 infection to DLD-1 intestinal cells
    • Yang B, Chuang H, Yang KD. 2009. Sialylated glycans as receptor and inhibitor of enterovirus 71 infection to DLD-1 intestinal cells. Virol. J. 6:141.
    • (2009) Virol. J , vol.6 , pp. 141
    • Yang, B.1    Chuang, H.2    Yang, K.D.3
  • 17
    • 80655125503 scopus 로고    scopus 로고
    • Annexin II binds to capsid protein VP1 of enterovirus 71 and enhances viral infectivity
    • Yang SL, Chou YT, Wu CN, Ho MS. 2011. Annexin II binds to capsid protein VP1 of enterovirus 71 and enhances viral infectivity. J. Virol. 85: 11809-11820.
    • (2011) J. Virol , vol.85 , pp. 11809-11820
    • Yang, S.L.1    Chou, Y.T.2    Wu, C.N.3    Ho, M.S.4
  • 18
    • 84871962446 scopus 로고    scopus 로고
    • Enterovirus 71 uses cell surface heparan sulfate glycosaminoglycan as an attachment receptor
    • Tan CW, Poh CL, Sam IC, Chan YF. 2013. Enterovirus 71 uses cell surface heparan sulfate glycosaminoglycan as an attachment receptor. J. Virol. 87:611-620.
    • (2013) J. Virol , vol.87 , pp. 611-620
    • Tan, C.W.1    Poh, C.L.2    Sam, I.C.3    Chan, Y.F.4
  • 20
    • 84869214041 scopus 로고    scopus 로고
    • In vitro assembly of an empty picornavirus capsid follows a dodecahedral path
    • Li C, Wang JC, Taylor MW, Zlotnick A. 2012. In vitro assembly of an empty picornavirus capsid follows a dodecahedral path. J. Virol. 86: 13062-13069.
    • (2012) J. Virol , vol.86 , pp. 13062-13069
    • Li, C.1    Wang, J.C.2    Taylor, M.W.3    Zlotnick, A.4
  • 21
    • 0028152426 scopus 로고
    • Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: structure of the empty capsid assembly intermediate at 2.9 A resolution
    • Basavappa R, Syed R, Flore O, Icenogle JP, Filman DJ, Hogle JM. 1994. Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: structure of the empty capsid assembly intermediate at 2.9 A resolution. Protein Sci. 3:1651-1669.
    • (1994) Protein Sci , vol.3 , pp. 1651-1669
    • Basavappa, R.1    Syed, R.2    Flore, O.3    Icenogle, J.P.4    Filman, D.J.5    Hogle, J.M.6
  • 22
    • 0015688306 scopus 로고
    • Morphogenesis of poliovirus 3. Formation of provirion in cell-free extracts
    • Fernandez-Tomas CB, Guttman N, Baltimore D. 1973. Morphogenesis of poliovirus 3. Formation of provirion in cell-free extracts. J. Virol. 12: 1181-1183.
    • (1973) J. Virol , vol.12 , pp. 1181-1183
    • Fernandez-Tomas, C.B.1    Guttman, N.2    Baltimore, D.3
  • 23
    • 0017695815 scopus 로고
    • Involvement of viral procapsid in the RNA synthesis and maturation of poliovirus
    • Yin FH. 1977. Involvement of viral procapsid in the RNA synthesis and maturation of poliovirus. Virology 82:299-307.
    • (1977) Virology , vol.82 , pp. 299-307
    • Yin, F.H.1
  • 25
    • 0014944992 scopus 로고
    • Further evidence on the for- mation of poliovirus proteins
    • Jacobson MF, Asso J, Baltimore D. 1970. Further evidence on the for- mation of poliovirus proteins. J. Mol. Biol. 49:657-669.
    • (1970) J. Mol. Biol , vol.49 , pp. 657-669
    • Jacobson, M.F.1    Asso, J.2    Baltimore, D.3
  • 26
    • 0027451701 scopus 로고
    • RNA-dependent cleavage of VP0 capsid protein in provirions of hepatitis A virus
    • Bishop NE, Anderson DA. 1993. RNA-dependent cleavage of VP0 capsid protein in provirions of hepatitis A virus. Virology 197:616-623.
    • (1993) Virology , vol.197 , pp. 616-623
    • Bishop, N.E.1    Anderson, D.A.2
  • 27
    • 0025150548 scopus 로고
    • Temperature-sensitive poliovirus mutant fails to cleave VP0 and accumulates provirions
    • Compton SR, Nelsen B, Kirkegaard K. 1990. Temperature-sensitive poliovirus mutant fails to cleave VP0 and accumulates provirions. J. Virol. 64:4067-4075.
    • (1990) J. Virol , vol.64 , pp. 4067-4075
    • Compton, S.R.1    Nelsen, B.2    Kirkegaard, K.3
  • 28
    • 79251515779 scopus 로고    scopus 로고
    • Adaptive mutations in the genomes of enterovirus 71 strains following infection of mouse cells expressing human P-selectin glycoprotein li- gand-1
    • Miyamura K, Nishimura Y, Abo M, Wakita T, Shimizu H. 2011. Adaptive mutations in the genomes of enterovirus 71 strains following infection of mouse cells expressing human P-selectin glycoprotein li- gand-1. J. Gen. Virol. 92:287-291.
    • (2011) J. Gen. Virol , vol.92 , pp. 287-291
    • Miyamura, K.1    Nishimura, Y.2    Abo, M.3    Wakita, T.4    Shimizu, H.5
  • 29
    • 84861310674 scopus 로고    scopus 로고
    • A 3D framework for understanding enterovirus 71
    • Hogle JM. 2012. A 3D framework for understanding enterovirus 71. Nat. Struct. Mol. Biol. 19:367-368.
    • (2012) Nat. Struct. Mol. Biol , vol.19 , pp. 367-368
    • Hogle, J.M.1
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replace- ment
    • Navaza J. 1994. AMoRe: an automated package for molecular replace- ment. Acta Crystallogr. A 50:157-163.
    • (1994) Acta Crystallogr , vol.50 , pp. 157-163
    • Navaza, J.1
  • 34
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL. 1993. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815.
    • (1993) J. Mol. Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 36
    • 0030845915 scopus 로고    scopus 로고
    • Structural studies of poliovirus mutants that overcome receptor defects
    • Wien MW, Curry S, Filman DJ, Hogle JM. 1997. Structural studies of poliovirus mutants that overcome receptor defects. Nat. Struct. Biol. 4:666-674.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 666-674
    • Wien, M.W.1    Curry, S.2    Filman, D.J.3    Hogle, J.M.4
  • 37
    • 0028945209 scopus 로고
    • mplica- tions for viral uncoating from the structure of bovine enterovirus
    • Smyth M, Tate J, Hoey E, Lyons C, Martin S, Stuart D. 1995. Implica- tions for viral uncoating from the structure of bovine enterovirus. Nat. Struct. Biol. 2:224-231.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 224-231
    • Smyth, M.1    Tate, J.2    Hoey, E.3    Lyons, C.4    Martin, S.5    Stuart, D.6
  • 41
    • 0141682116 scopus 로고    scopus 로고
    • tructure of swine vesicular disease virus: mapping of changes occurring during adap-tation of human coxsackie B5 virus to infect swine
    • Verdaguer N, Jimenez-Clavero MA, Fita I, Ley V. 2003. Structure of swine vesicular disease virus: mapping of changes occurring during adap-tation of human coxsackie B5 virus to infect swine. J. Virol. 77:9780-9789.
    • (2003) J. Virol , vol.77 , pp. 9780-9789
    • Verdaguer, N.1    Jimenez-Clavero, M.A.2    Fita, I.3    Ley, V.4
  • 44
    • 84944816485 scopus 로고
    • The use of molecular-replacement phases for the refinement of the human rhinovirus 14 structure
    • Arnold E, Rossmann MG. 1988. The use of molecular-replacement phases for the refinement of the human rhinovirus 14 structure. Acta Crystallogr. A 44:270-282.
    • (1988) Acta Crystallogr A , vol.44 , pp. 270-282
    • Arnold, E.1    Rossmann, M.G.2
  • 49
    • 33845338800 scopus 로고    scopus 로고
    • AUTO3DEM-an automated and high throughput program for image reconstruction of icosahedral parti- cles
    • Yan X, Sinkovits RS, Baker TS. 2007. AUTO3DEM-an automated and high throughput program for image reconstruction of icosahedral parti- cles. J. Struct. Biol. 157:73-82.
    • (2007) J. Struct. Biol , vol.157 , pp. 73-82
    • Yan, X.1    Sinkovits, R.S.2    Baker, T.S.3
  • 51
    • 33845348934 scopus 로고    scopus 로고
    • Ab initio random model method facilitates 3D reconstruction of icosahedral particles
    • Yan X, Dryden KA, Tang J, Baker TS. 2007. Ab initio random model method facilitates 3D reconstruction of icosahedral particles. J. Struct. Biol. 157:211-225.
    • (2007) J. Struct. Biol , vol.157 , pp. 211-225
    • Yan, X.1    Dryden, K.A.2    Tang, J.3    Baker, T.S.4
  • 53
    • 77955358961 scopus 로고    scopus 로고
    • sing Situs for the integration of multi-resolution structures
    • Wriggers W. 2010. Using Situs for the integration of multi-resolution structures. Biophys. Rev. 2:21-27.
    • (2010) Biophys. Rev , vol.2 , pp. 21-27
    • Wriggers, W.1
  • 54
    • 0036297629 scopus 로고    scopus 로고
    • Multi-resolution contour-based fitting of macromolecular structures
    • Chacon P, Wriggers W. 2002. Multi-resolution contour-based fitting of macromolecular structures. J. Mol. Biol. 317:375-384.
    • (2002) J. Mol. Biol , vol.317 , pp. 375-384
    • Chacon, P.1    Wriggers, W.2
  • 55
    • 79955938192 scopus 로고    scopus 로고
    • urification and characterization of enterovirus 71 viral particles produced from Vero cells grown in a serum- free microcarrier bioreactor system
    • doi:10.1371 /journal.pone.0020005
    • Liu CC, Guo MS, Lin FH, Hsiao KN, Chang KH, Chou AH, Wang YC, Chen YC, Yang CS, Chong PC. 2011. Purification and characterization of enterovirus 71 viral particles produced from Vero cells grown in a serum- free microcarrier bioreactor system. PLoS One 6:e20005. doi:10.1371 /journal.pone.0020005.
    • (2011) PLoS One 6:e20005
    • Liu, C.C.1    Guo, M.S.2    Lin, F.H.3    Hsiao, K.N.4    Chang, K.H.5    Chou, A.H.6    Wang, Y.C.7    Chen, Y.C.8    Yang, C.S.9    Chong, P.C.10
  • 56
    • 84874742838 scopus 로고    scopus 로고
    • Functional comparison of SCARB2 and PSGL1 as receptors for enterovirus 71
    • Yamayoshi S, Ohka S, Fujii K, Koike S. 2013. Functional comparison of SCARB2 and PSGL1 as receptors for enterovirus 71. J. Virol. 87:3335-3347.
    • (2013) J. Virol , vol.87 , pp. 3335-3347
    • Yamayoshi, S.1    Ohka, S.2    Fujii, K.3    Koike, S.4
  • 57
    • 0030780581 scopus 로고    scopus 로고
    • Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: the structure of empty capsids of foot-and-mouth disease virus
    • Curry S, Fry E, Blakemore W, Abu-Ghazaleh R, Jackson T, King A, Lea S, Newman J, Stuart D. 1997. Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: the structure of empty capsids of foot-and-mouth disease virus. J. Virol. 71:9743-9752.
    • (1997) J. Virol , vol.71 , pp. 9743-9752
    • Curry, S.1    Fry, E.2    Blakemore, W.3    Abu-Ghazaleh, R.4    Jackson, T.5    King, A.6    Lea, S.7    Newman, J.8    Stuart, D.9
  • 60
    • 84869022974 scopus 로고    scopus 로고
    • ymmetry-related clustering of positive charges is a common mech- anism for heparan sulfate binding in enteroviruses
    • Mc-Leish NJ, Williams CH, Kaloudas D, Roivainen MM, Stanway G. 2012. Symmetry-related clustering of positive charges is a common mech- anism for heparan sulfate binding in enteroviruses. J. Virol. 86:11163-11170.
    • (2012) J. Virol , vol.86 , pp. 11163-11170
    • Mc-Leish, N.J.1    Williams, C.H.2    Kaloudas, D.3    Roivainen, M.M.4    Stanway, G.5
  • 61
    • 0014432751 scopus 로고
    • Morphogenesis of poliovirus. I. Asso- ciation of the viral RNA with coat protein
    • Jacobson MF, Baltimore D. 1968. Morphogenesis of poliovirus. I. Asso- ciation of the viral RNA with coat protein. J. Mol. Biol. 33:369-378.
    • (1968) J. Mol. Biol , vol.33 , pp. 369-378
    • Jacobson, M.F.1    Baltimore, D.2
  • 62
    • 0015379878 scopus 로고
    • Study of some stages of poliovirus morphogenesis in MiO cells
    • Ghendon Y, Yakobson E, Mikhejeva A. 1972. Study of some stages of poliovirus morphogenesis in MiO cells. J. Virol. 10:261-266.
    • (1972) J. Virol , vol.10 , pp. 261-266
    • Ghendon, Y.1    Yakobson, E.2    Mikhejeva, A.3
  • 63
    • 0019512309 scopus 로고
    • Poliovirus morphogenesis. I. Identification of 80S dissociable particles and evidence for the artifactual production of procapsids
    • Marongiu ME, Pani A, Corrias MV, Sau M, La Colla P. 1981. Poliovirus morphogenesis. I. Identification of 80S dissociable particles and evidence for the artifactual production of procapsids. J. Virol. 39:341-347.
    • (1981) J. Virol , vol.39 , pp. 341-347
    • Marongiu, M.E.1    Pani, A.2    Corrias, M.V.3    Sau, M.4    La Colla, P.5
  • 64
    • 0036094935 scopus 로고    scopus 로고
    • φ genome-capsid interactions influ- ence the biophysical properties of the virion: evidence for a scaffolding- like function for the genome during the final stages of morphogenesis
    • Hafenstein S, Fane BA. 2002. φ genome-capsid interactions influ- ence the biophysical properties of the virion: evidence for a scaffolding- like function for the genome during the final stages of morphogenesis. J. Virol. 76:5350-5356.
    • (2002) J. Virol , vol.76 , pp. 5350-5356
    • Hafenstein, S.1    Fane, B.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.