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Volumn 87, Issue 10, 2013, Pages 5755-5768

Crystal structure of enterovirus 71 RNA-dependent RNA polymerase complexed with its protein primer VPg: Implication for a trans mechanism of VPg uridylylation

Author keywords

[No Author keywords available]

Indexed keywords

ENTEROVIRUS 71 PROTEIN; RNA DIRECTED RNA POLYMERASE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84877616491     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02733-12     Document Type: Article
Times cited : (60)

References (49)
  • 1
    • 84877628781 scopus 로고    scopus 로고
    • The CpG suppression of polymerase segments and its impact on codon usage bias in H1N1 influenza virus
    • Gong X, Fan S, Zhang C, Li X. 2011. The CpG suppression of polymerase segments and its impact on codon usage bias in H1N1 influenza virus. Acta Biophys. Sin. 27:537-544.
    • (2011) Acta Biophys. Sin. , vol.27 , pp. 537-544
    • Gong, X.1    Fan, S.2    Zhang, C.3    Li, X.4
  • 3
    • 0035142039 scopus 로고    scopus 로고
    • Acute flaccid paralysis in infants and young children with enterovirus 71 infection: MR imaging findings and clinical correlates
    • Chen CY, Chang YC, Huang CC, Lui CC, Lee KW, Huang SC. 2001. Acute flaccid paralysis in infants and young children with enterovirus 71 infection: MR imaging findings and clinical correlates. Am. J. Neuroradiol. 22:200-205.
    • (2001) Am. J. Neuroradiol. , vol.22 , pp. 200-205
    • Chen, C.Y.1    Chang, Y.C.2    Huang, C.C.3    Lui, C.C.4    Lee, K.W.5    Huang, S.C.6
  • 6
    • 84856189670 scopus 로고    scopus 로고
    • Progress in targeted delivery of siRNA to combat coxsackievirus
    • Gautam A. 2011. Progress in targeted delivery of siRNA to combat coxsackievirus. Protein Cell 2:855-857.
    • (2011) Protein Cell , vol.2 , pp. 855-857
    • Gautam, A.1
  • 7
    • 68349134833 scopus 로고    scopus 로고
    • Neuropathology in 2 cases of fatal enterovirus type 71 infection from a recent epidemic in the People's Republic of China: a histopathologic, immunohistochemical, and reverse transcription polymerase chain reaction study
    • Yang Y, Wang H, Gong E, Du J, Zhao X, McNutt MA, Wang S, Zhong Y, Gao Z, Zheng J. 2009. Neuropathology in 2 cases of fatal enterovirus type 71 infection from a recent epidemic in the People's Republic of China: a histopathologic, immunohistochemical, and reverse transcription polymerase chain reaction study. Hum. Pathol. 40:1288-1295.
    • (2009) Hum. Pathol. , vol.40 , pp. 1288-1295
    • Yang, Y.1    Wang, H.2    Gong, E.3    Du, J.4    Zhao, X.5    McNutt, M.A.6    Wang, S.7    Zhong, Y.8    Gao, Z.9    Zheng, J.10
  • 9
    • 0036242282 scopus 로고    scopus 로고
    • An overview of the evolution of enterovirus 71 and its clinical and public health significance
    • McMinn PC. 2002. An overview of the evolution of enterovirus 71 and its clinical and public health significance. FEMS Microbiol. Rev. 26:91-107.
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 91-107
    • McMinn, P.C.1
  • 10
    • 0032146721 scopus 로고    scopus 로고
    • Switch from translation to RNA replication in a positive-stranded RNA virus
    • Gamarnik AV, Andino R. 1998. Switch from translation to RNA replication in a positive-stranded RNA virus. Genes Dev. 12:2293-2304.
    • (1998) Genes Dev. , vol.12 , pp. 2293-2304
    • Gamarnik, A.V.1    Andino, R.2
  • 11
    • 0034633840 scopus 로고    scopus 로고
    • Satellite and defective RNAs of Cryphonectria hypovirus 3-grand haven 2, a virus species in the family Hypoviridae with a single open reading frame
    • Hillman BI, Foglia R, Yuan W. 2000. Satellite and defective RNAs of Cryphonectria hypovirus 3-grand haven 2, a virus species in the family Hypoviridae with a single open reading frame. Virology 276:181-189.
    • (2000) Virology , vol.276 , pp. 181-189
    • Hillman, B.I.1    Foglia, R.2    Yuan, W.3
  • 12
    • 0023720048 scopus 로고
    • Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA
    • Pelletier J, Sonenberg N. 1988. Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA. Nature 334:320-325.
    • (1988) Nature , vol.334 , pp. 320-325
    • Pelletier, J.1    Sonenberg, N.2
  • 13
    • 0000095156 scopus 로고    scopus 로고
    • Picornaviridae: the viruses and their replication
    • In Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed),, 4th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • Racaniello VR. 2001. Picornaviridae: the viruses and their replication, p 685-722. In Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), Fields virology, 4th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2001) Fields virology , pp. 685-722
    • Racaniello, V.R.1
  • 15
    • 79952537148 scopus 로고    scopus 로고
    • Structures of EV71 RNA-dependent RNA polymerase in complex with substrate and analogue provide a drug target against the hand-footand-mouth disease pandemic in China
    • Wu Y, Lou Z, Miao Y, Yu Y, Dong H, Peng W, Bartlam M, Li X, Rao Z. 2010. Structures of EV71 RNA-dependent RNA polymerase in complex with substrate and analogue provide a drug target against the hand-footand-mouth disease pandemic in China. Protein Cell 1:491-500.
    • (2010) Protein Cell , vol.1 , pp. 491-500
    • Wu, Y.1    Lou, Z.2    Miao, Y.3    Yu, Y.4    Dong, H.5    Peng, W.6    Bartlam, M.7    Li, X.8    Rao, Z.9
  • 16
    • 0017809191 scopus 로고
    • Protein is linked to the 5′ end of poliovirus RNA by a phosphodiester linkage to tyrosine
    • Ambros V, Baltimore D. 1978. Protein is linked to the 5′ end of poliovirus RNA by a phosphodiester linkage to tyrosine. J. Biol. Chem. 253:5263-5266.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5263-5266
    • Ambros, V.1    Baltimore, D.2
  • 17
    • 0037223676 scopus 로고    scopus 로고
    • Biochemical and genetic studies of the VPg uridylylation reaction catalyzed by the RNA polymerase of poliovirus
    • Paul AV, Peters J, Mugavero J, Yin J, van Boom JH, Wimmer E. 2003. Biochemical and genetic studies of the VPg uridylylation reaction catalyzed by the RNA polymerase of poliovirus. J. Virol. 77:891-904.
    • (2003) J. Virol. , vol.77 , pp. 891-904
    • Paul, A.V.1    Peters, J.2    Mugavero, J.3    Yin, J.4    van Boom, J.H.5    Wimmer, E.6
  • 19
    • 0033766003 scopus 로고    scopus 로고
    • Identification of an RNA hairpin in poliovirus RNA that serves as the primary template in the in vitro uridylylation of VPg
    • Paul AV, Rieder E, Kim DW, van Boom JH, Wimmer E. 2000. Identification of an RNA hairpin in poliovirus RNA that serves as the primary template in the in vitro uridylylation of VPg. J. Virol. 74:10359-10370.
    • (2000) J. Virol. , vol.74 , pp. 10359-10370
    • Paul, A.V.1    Rieder, E.2    Kim, D.W.3    van Boom, J.H.4    Wimmer, E.5
  • 20
    • 47949130360 scopus 로고    scopus 로고
    • The cis-acting replication elements define human enterovirus and rhinovirus species
    • Cordey S, Gerlach D, Junier T, Zdobnov EM, Kaiser L, Tapparel C. 2008. The cis-acting replication elements define human enterovirus and rhinovirus species. RNA 14:1568-1578.
    • (2008) RNA , vol.14 , pp. 1568-1578
    • Cordey, S.1    Gerlach, D.2    Junier, T.3    Zdobnov, E.M.4    Kaiser, L.5    Tapparel, C.6
  • 21
    • 59749104648 scopus 로고    scopus 로고
    • cis-active RNA elements (CREs) and picornavirus RNA replication
    • Steil BP, Barton DJ. 2009. cis-active RNA elements (CREs) and picornavirus RNA replication. Virus Res. 139:240-252.
    • (2009) Virus Res. , vol.139 , pp. 240-252
    • Steil, B.P.1    Barton, D.J.2
  • 22
    • 0037276580 scopus 로고    scopus 로고
    • Structure and function analysis of the poliovirus cis-acting replication element (CRE)
    • Goodfellow IG, Kerrigan D, Evans DJ. 2003. Structure and function analysis of the poliovirus cis-acting replication element (CRE). RNA 9:124-137.
    • (2003) RNA , vol.9 , pp. 124-137
    • Goodfellow, I.G.1    Kerrigan, D.2    Evans, D.J.3
  • 23
    • 33748943522 scopus 로고    scopus 로고
    • Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication
    • Nayak A, Goodfellow IG, Woolaway KE, Birtley J, Curry S, Belsham GJ. 2006. Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication. J. Virol. 80:9865-9875.
    • (2006) J. Virol. , vol.80 , pp. 9865-9875
    • Nayak, A.1    Goodfellow, I.G.2    Woolaway, K.E.3    Birtley, J.4    Curry, S.5    Belsham, G.J.6
  • 24
    • 0037302691 scopus 로고    scopus 로고
    • The foot-and-mouth disease virus cis-acting replication element (cre) can be complemented in trans within infected cells
    • Tiley L, King AM, Belsham GJ. 2003. The foot-and-mouth disease virus cis-acting replication element (cre) can be complemented in trans within infected cells. J. Virol. 77:2243-2246.
    • (2003) J. Virol. , vol.77 , pp. 2243-2246
    • Tiley, L.1    King, A.M.2    Belsham, G.J.3
  • 25
    • 19944407924 scopus 로고    scopus 로고
    • Factors required for the uridylylation of the foot-and-mouth disease virus 3B1, 3B2, and 3B3 peptides by the RNA-dependent RNA polymerase (3Dpol) in vitro
    • Nayak A, Goodfellow IG, Belsham GJ. 2005. Factors required for the uridylylation of the foot-and-mouth disease virus 3B1, 3B2, and 3B3 peptides by the RNA-dependent RNA polymerase (3Dpol) in vitro. J. Virol. 79:7698-7706.
    • (2005) J. Virol. , vol.79 , pp. 7698-7706
    • Nayak, A.1    Goodfellow, I.G.2    Belsham, G.J.3
  • 27
    • 52649173300 scopus 로고    scopus 로고
    • The crystal structure of coxsackievirus B3 RNA-dependent RNA polymerase in complex with its protein primer VPg confirms the existence of a second VPg binding site on Picornaviridae polymerases
    • Gruez A, Selisko B, Roberts M, Bricogne G, Bussetta C, Jabafi I, Coutard B, De Palma AM, Neyts J, Canard B. 2008. The crystal structure of coxsackievirus B3 RNA-dependent RNA polymerase in complex with its protein primer VPg confirms the existence of a second VPg binding site on Picornaviridae polymerases. J. Virol. 82:9577-9590.
    • (2008) J. Virol. , vol.82 , pp. 9577-9590
    • Gruez, A.1    Selisko, B.2    Roberts, M.3    Bricogne, G.4    Bussetta, C.5    Jabafi, I.6    Coutard, B.7    De Palma, A.M.8    Neyts, J.9    Canard, B.10
  • 31
    • 4143072386 scopus 로고    scopus 로고
    • Complete three-dimensional structures of picornaviral RNA-dependent RNA polymerases
    • Crowder S, Kirkegaard K. 2004. Complete three-dimensional structures of picornaviral RNA-dependent RNA polymerases. Structure 12:1336-1339.
    • (2004) Structure , vol.12 , pp. 1336-1339
    • Crowder, S.1    Kirkegaard, K.2
  • 32
    • 33646773175 scopus 로고    scopus 로고
    • Novel, structure-based mechanism for uridylylation of the genome-linked peptide (VPg) of picornaviruses
    • Schein CH, Volk DE, Oezguen N, Paul A. 2006. Novel, structure-based mechanism for uridylylation of the genome-linked peptide (VPg) of picornaviruses. Proteins 63:719-726.
    • (2006) Proteins , vol.63 , pp. 719-726
    • Schein, C.H.1    Volk, D.E.2    Oezguen, N.3    Paul, A.4
  • 35
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. 1968. Solvent content of protein crystals. J. Mol. Biol. 33:491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 39
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R, MacArthur M, Moss D, Thornton J. 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 40
    • 0003845223 scopus 로고    scopus 로고
    • The PyMOL molecular graphics system
    • DeLano W. 2002. The PyMOL molecular graphics system. Schrödinger, LLC.
    • (2002) Schrödinger, LLC.
    • DeLano, W.1
  • 41
    • 84862936213 scopus 로고    scopus 로고
    • Structural vaccinology structure-based design of influenza A virus hemagglutinin subtype-specific subunit vaccines
    • Xuan C, Shi Y, Qi J, Zhang W, Xiao H, Gao GF. 2011. Structural vaccinology: structure-based design of influenza A virus hemagglutinin subtype-specific subunit vaccines. Protein Cell 2:997-1005.
    • (2011) Protein Cell , vol.2 , pp. 997-1005
    • Xuan, C.1    Shi, Y.2    Qi, J.3    Zhang, W.4    Xiao, H.5    Gao, G.F.6
  • 42
    • 84857431881 scopus 로고    scopus 로고
    • Innovator of in vitro virus culture-Dr
    • Cheng G. 2011. Innovator of in vitro virus culture-Dr. Chen-Hsiang Huang. Protein Cell 2:782-783.
    • (2011) Chen-Hsiang Huang. Protein Cell , vol.2 , pp. 782-783
    • Cheng, G.1
  • 43
    • 84872132019 scopus 로고    scopus 로고
    • Development and characterization of a stable eGFP enterovirus 71 for antiviral screening
    • Shang B, Deng C, Ye H, Xu W, Yuan Z, Shi PY, Zhang B. 2013. Development and characterization of a stable eGFP enterovirus 71 for antiviral screening. Antiviral Res. 97:198-205.
    • (2013) Antiviral Res. , vol.97 , pp. 198-205
    • Shang, B.1    Deng, C.2    Ye, H.3    Xu, W.4    Yuan, Z.5    Shi, P.Y.6    Zhang, B.7
  • 45
    • 0037150679 scopus 로고    scopus 로고
    • Visualization and functional analysis of RNA-dependent RNA polymerase lattices
    • Lyle JM, Bullitt E, Bienz K, Kirkegaard K. 2002. Visualization and functional analysis of RNA-dependent RNA polymerase lattices. Science 296:2218-2222.
    • (2002) Science , vol.296 , pp. 2218-2222
    • Lyle, J.M.1    Bullitt, E.2    Bienz, K.3    Kirkegaard, K.4
  • 47
    • 80052278508 scopus 로고    scopus 로고
    • Cleavage of the adaptor protein TRIF by enterovirus 71 3C inhibits antiviral responses mediated by Toll-like receptor 3
    • Lei X, Sun Z, Liu X, Jin Q, He B, Wang J. 2011. Cleavage of the adaptor protein TRIF by enterovirus 71 3C inhibits antiviral responses mediated by Toll-like receptor 3. J. Virol. 85:8811-8818.
    • (2011) J. Virol. , vol.85 , pp. 8811-8818
    • Lei, X.1    Sun, Z.2    Liu, X.3    Jin, Q.4    He, B.5    Wang, J.6
  • 48
    • 80054007220 scopus 로고    scopus 로고
    • Crystal structures of enterovirus 71 3C protease complexed with rupintrivir reveal the roles of catalytically important residues
    • Wang J, Fan T, Yao X, Wu Z, Guo L, Lei X, Wang J, Wang M, Jin Q, Cui S. 2011. Crystal structures of enterovirus 71 3C protease complexed with rupintrivir reveal the roles of catalytically important residues. J. Virol. 85:10021-10030.
    • (2011) J. Virol. , vol.85 , pp. 10021-10030
    • Wang, J.1    Fan, T.2    Yao, X.3    Wu, Z.4    Guo, L.5    Lei, X.6    Wang, J.7    Wang, M.8    Jin, Q.9    Cui, S.10
  • 49
    • 84870696312 scopus 로고    scopus 로고
    • Molecular imaging: an important tool and a main route for translational medicine
    • Wu C, Zhu Z, Li FCY, Jing H. 2011. Molecular imaging: an important tool and a main route for translational medicine. Acta Biophys. Sin. 27: 327-334.
    • (2011) Acta Biophys. Sin. , vol.27 , pp. 327-334
    • Wu, C.1    Zhu, Z.2    Li, F.C.Y.3    Jing, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.