메뉴 건너뛰기




Volumn 88, Issue 23, 2014, Pages 13747-13758

Characterization of an alphamesonivirus 3C-like protease defines a special group of nidovirus main proteases

Author keywords

[No Author keywords available]

Indexed keywords

CAVALLY VIRUS 3C LIKE PROTEASE; PROTEINASE; UNCLASSIFIED DRUG; VIRUS PROTEIN; 3C PROTEASES; CYSTEINE PROTEINASE; VIRAL PROTEIN;

EID: 84911442273     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02040-14     Document Type: Article
Times cited : (10)

References (45)
  • 2
    • 84864441738 scopus 로고    scopus 로고
    • Mesoniviridae: a proposed new family in the order Nidovirales formed by a single species of mosquito-borne viruses
    • Lauber C, Ziebuhr J, Junglen S, Drosten C, Zirkel F, Nga PT, Morita K, Snijder EJ, Gorbalenya AE. 2012. Mesoniviridae: a proposed new family in the order Nidovirales formed by a single species of mosquito-borne viruses. Arch. Virol. 157:1623-1628. http://dx.doi.org/10.1007/s00705 -012-1295-x.
    • (2012) Arch. Virol. , vol.157 , pp. 1623-1628
    • Lauber, C.1    Ziebuhr, J.2    Junglen, S.3    Drosten, C.4    Zirkel, F.5    Nga, P.T.6    Morita, K.7    Snijder, E.J.8    Gorbalenya, A.E.9
  • 3
    • 0034093105 scopus 로고    scopus 로고
    • Gill-associated virus of Penaeus monodon prawns: an invertebrate virus with ORF1a and ORF1b genes related to arteri- and coronaviruses
    • Cowley JA, Dimmock CM, Spann KM, Walker PJ. 2000. Gill-associated virus of Penaeus monodon prawns: an invertebrate virus with ORF1a and ORF1b genes related to arteri- and coronaviruses. J. Gen. Virol. 81:1473- 1484.
    • (2000) J. Gen. Virol. , vol.81 , pp. 1473-1484
    • Cowley, J.A.1    Dimmock, C.M.2    Spann, K.M.3    Walker, P.J.4
  • 5
    • 84888011629 scopus 로고    scopus 로고
    • A decade after SARS: strategies for controlling emerging coronaviruses
    • Graham RL, Donaldson EF, Baric RS. 2013. A decade after SARS: strategies for controlling emerging coronaviruses. Nat. Rev. Microbiol. 11: 836-848. http://dx.doi.org/10.1038/nrmicro3143.
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 836-848
    • Graham, R.L.1    Donaldson, E.F.2    Baric, R.S.3
  • 7
    • 84884170985 scopus 로고    scopus 로고
    • Arterivirus molecular biology and pathogenesis
    • Snijder EJ, Kikkert M, Fang Y. 2013. Arterivirus molecular biology and pathogenesis. J. Gen. Virol. 94:2141-2163. http://dx.doi.org/10.1099/vir.0.056341-0.
    • (2013) J. Gen. Virol. , vol.94 , pp. 2141-2163
    • Snijder, E.J.1    Kikkert, M.2    Fang, Y.3
  • 11
    • 84878185418 scopus 로고    scopus 로고
    • Identification and characterization of genetically divergent members of the newly established family
    • Zirkel F, Roth H, Kurth A, Drosten C, Ziebuhr J, Junglen S. 2013. Identification and characterization of genetically divergent members of the newly established family Mesoniviridae. J. Virol. 87:6346-6358. http: //dx.doi.org/10.1128/JVI.00416-13.
    • (2013) J. Virol.Mesoniviridae , vol.87 , pp. 6346-6358
    • Zirkel, F.1    Roth, H.2    Kurth, A.3    Drosten, C.4    Ziebuhr, J.5    Junglen, S.6
  • 12
    • 84882894162 scopus 로고    scopus 로고
    • A new nidovirus (NamDinh virus NDiV): its ultrastructural characterization in the C6/36 mosquito cell line
    • Thuy NT, Huy TQ, Nga PT, Morita K, Dunia I, Benedetti L. 2013. A new nidovirus (NamDinh virus NDiV): its ultrastructural characterization in the C6/36 mosquito cell line. Virology 444:337-342. http://dx.doi.org/10.1016/j.virol.2013.06.030.
    • (2013) Virology , vol.444 , pp. 337-342
    • Thuy, N.T.1    Huy, T.Q.2    Nga, P.T.3    Morita, K.4    Dunia, I.5    Benedetti, L.6
  • 13
    • 33645093947 scopus 로고    scopus 로고
    • Nidovirales: evolving the largest RNA virus genome
    • Gorbalenya AE, Enjuanes L, Ziebuhr J, Snijder EJ. 2006. Nidovirales: evolving the largest RNA virus genome. Virus Res. 117:17-37. http://dx.doi.org/10.1016/j.virusres.2006.01.017.
    • (2006) Virus Res , vol.117 , pp. 17-37
    • Gorbalenya, A.E.1    Enjuanes, L.2    Ziebuhr, J.3    Snijder, E.J.4
  • 15
    • 84911367999 scopus 로고    scopus 로고
    • In Perlman S, Gallagher T, Snijder EJ (ed), Nidoviruses. ASM Press, Washington, DC
    • Ziebuhr J. 2008. Coronavirus replicative proteins, p 65-81. In Perlman S, Gallagher T, Snijder EJ (ed), Nidoviruses. ASM Press, Washington, DC.
    • (2008) Coronavirus replicative proteins , pp. 65-81
    • Ziebuhr, J.1
  • 16
    • 0034072633 scopus 로고    scopus 로고
    • Virus-encoded proteinases and proteolytic processing in the Nidovirales
    • Ziebuhr J, Snijder EJ, Gorbalenya AE. 2000. Virus-encoded proteinases and proteolytic processing in the Nidovirales. J. Gen. Virol. 81:853-879.17.
    • (2000) J. Gen. Virol. , vol.81 , pp. 853-879
    • Ziebuhr, J.1    Snijder, E.J.2    Gorbalenya, A.E.3
  • 17
    • 33645753305 scopus 로고    scopus 로고
    • Characterization of a torovirus main proteinase
    • Smits SL, Snijder EJ, de Groot RJ. 2006. Characterization of a torovirus main proteinase. J. Virol. 80:4157-4167. http://dx.doi.org/10.1128/JVI.80.8.4157-4167.2006.
    • (2006) J. Virol. , vol.80 , pp. 4157-4167
    • Smits, S.L.1    Snijder, E.J.2    de Groot, R.J.3
  • 18
    • 78651386377 scopus 로고    scopus 로고
    • Characterization of bafinivirus main protease autoprocessing activities
    • Ulferts R, Mettenleiter TC, Ziebuhr J. 2011. Characterization of bafinivirus main protease autoprocessing activities. J. Virol. 85:1348-1359. http://dx.doi.org/10.1128/JVI.01716-10.
    • (2011) J. Virol. , vol.85 , pp. 1348-1359
    • Ulferts, R.1    Mettenleiter, T.C.2    Ziebuhr, J.3
  • 19
    • 0037228215 scopus 로고    scopus 로고
    • The 3C-like proteinase of an invertebrate nidovirus links coronavirus and potyvirus homologs
    • Ziebuhr J, Bayer S, Cowley JA, Gorbalenya AE. 2003. The 3C-like proteinase of an invertebrate nidovirus links coronavirus and potyvirus homologs. J. Virol. 77:1415-1426. http://dx.doi.org/10.1128/JVI.77.2.1415-1426.2003.
    • (2003) J. Virol. , vol.77 , pp. 1415-1426
    • Ziebuhr, J.1    Bayer, S.2    Cowley, J.A.3    Gorbalenya, A.E.4
  • 20
    • 0036646055 scopus 로고    scopus 로고
    • Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain
    • Anand K, Palm GJ, Mesters JR, Siddell SG, Ziebuhr J, Hilgenfeld R. 2002. Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain. EMBO J. 21:3213- 3224. http://dx.doi.org/10.1093/emboj/cdf327.
    • (2002) EMBO J , vol.21 , pp. 3213-3224
    • Anand, K.1    Palm, G.J.2    Mesters, J.R.3    Siddell, S.G.4    Ziebuhr, J.5    Hilgenfeld, R.6
  • 22
    • 0000686943 scopus 로고
    • Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications
    • U. S. A
    • Bazan JF, Fletterick RJ. 1988. Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications. Proc. Natl. Acad. Sci. U. S. A. 85:7872-7876. http://dx.doi.org /10.1073/pnas.85.21.7872.
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 7872-7876
    • Bazan, J.F.1    Fletterick, R.J.2
  • 23
    • 0028328469 scopus 로고
    • Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases
    • Allaire M, Chernaia MM, Malcolm BA, James MN. 1994. Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. Nature 369:72-76. http://dx.doi.org/10.1038/369072a0.
    • (1994) Nature , vol.369 , pp. 72-76
    • Allaire, M.1    Chernaia, M.M.2    Malcolm, B.A.3    James, M.N.4
  • 25
    • 0029966508 scopus 로고    scopus 로고
    • The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases
    • Snijder EJ, Wassenaar AL, van Dinten LC, Spaan WJ, Gorbalenya AE. 1996. The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases. J. Biol. Chem. 271:4864-4871. http://dx.doi.org/10.1074/jbc.271.9.4864.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4864-4871
    • Snijder, E.J.1    Wassenaar, A.L.2    van Dinten, L.C.3    Spaan, W.J.4    Gorbalenya, A.E.5
  • 26
    • 0030970783 scopus 로고    scopus 로고
    • Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase
    • Ziebuhr J, Heusipp G, Siddell SG. 1997. Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase. J. Virol. 71:3992-3997.
    • (1997) J. Virol. , vol.71 , pp. 3992-3997
    • Ziebuhr, J.1    Heusipp, G.2    Siddell, S.G.3
  • 27
    • 0029036797 scopus 로고
    • Characterisation and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein
    • Liu DX, Brown TD. 1995. Characterisation and mutational analysis of an ORF 1a-encoding proteinase domain responsible for proteolytic processing of the infectious bronchitis virus 1a/1b polyprotein. Virology 209: 420-427. http://dx.doi.org/10.1006/viro.1995.1274.
    • (1995) Virology , vol.209 , pp. 420-427
    • Liu, D.X.1    Brown, T.D.2
  • 28
    • 0036190639 scopus 로고    scopus 로고
    • Mutational analysis of the active centre of coronavirus 3C-like proteases
    • Hegyi A, Friebe A, Gorbalenya AE, Ziebuhr J. 2002. Mutational analysis of the active centre of coronavirus 3C-like proteases. J. Gen. Virol. 83:581- 593.
    • (2002) J. Gen. Virol. , vol.83 , pp. 581-593
    • Hegyi, A.1    Friebe, A.2    Gorbalenya, A.E.3    Ziebuhr, J.4
  • 29
    • 0014211618 scopus 로고
    • On the size of the active site in proteases
    • Schechter I, Berger A. 1967. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27:157-162. http://dx.doi.org /10.1016/S0006-291X(67)80055-X.
    • (1967) I. Papain. Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 31
    • 0026816908 scopus 로고
    • Site-directed mutagenesis of herpesvirus glycoprotein phosphorylation sites by recombination polymerase chain reaction
    • Yao Z, Jones DH, Grose C. 1992. Site-directed mutagenesis of herpesvirus glycoprotein phosphorylation sites by recombination polymerase chain reaction. PCR Methods Appl. 1:205-207. http://dx.doi.org/10.1101/gr.1.3.205.
    • (1992) PCR Methods Appl , vol.1 , pp. 205-207
    • Yao, Z.1    Jones, D.H.2    Grose, C.3
  • 32
    • 18244432238 scopus 로고    scopus 로고
    • Efficient autoproteolytic processing of the MHV-A59 3C-like proteinase from the flanking hydrophobic domains requires membranes.
    • Pinon JD, Mayreddy RR, Turner JD, Khan FS, Bonilla PJ, Weiss SR. 1997. Efficient autoproteolytic processing of the MHV-A59 3C-like proteinase from the flanking hydrophobic domains requires membranes. Virology 230:309-322. http://dx.doi.org/10.1006/viro.1997.8503.
    • (1997) Virology , vol.230 , pp. 309-322
    • Pinon, J.D.1    Mayreddy, R.R.2    Turner, J.D.3    Khan, F.S.4    Bonilla, P.J.5    Weiss, S.R.6
  • 33
    • 0030069011 scopus 로고    scopus 로고
    • Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus
    • Tibbles KW, Brierley I, Cavanagh D, Brown TD. 1996. Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus. J. Virol. 70:1923-1930.
    • (1996) J. Virol. , vol.70 , pp. 1923-1930
    • Tibbles, K.W.1    Brierley, I.2    Cavanagh, D.3    Brown, T.D.4
  • 34
    • 0029017145 scopus 로고
    • Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity
    • Ziebuhr J, Herold J, Siddell SG. 1995. Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity. J. Virol. 69:4331- 4338.
    • (1995) J. Virol. , vol.69 , pp. 4331-4338
    • Ziebuhr, J.1    Herold, J.2    Siddell, S.G.3
  • 35
    • 0027138172 scopus 로고
    • Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes
    • Dougherty WG, Semler BL. 1993. Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes. Microbiol. Rev. 57:781-822.
    • (1993) Microbiol. Rev. , vol.57 , pp. 781-822
    • Dougherty, W.G.1    Semler, B.L.2
  • 36
    • 9144268403 scopus 로고    scopus 로고
    • Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase
    • Fan K, Wei P, Feng Q, Chen S, Huang C, Ma L, Lai B, Pei J, Liu Y, Chen J, Lai L. 2004. Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase. J. Biol. Chem. 279:1637-1642. http://dx.doi.org/10.1074/jbc.M310875200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1637-1642
    • Fan, K.1    Wei, P.2    Feng, Q.3    Chen, S.4    Huang, C.5    Ma, L.6    Lai, B.7    Pei, J.8    Liu, Y.9    Chen, J.10    Lai, L.11
  • 37
    • 0036187709 scopus 로고    scopus 로고
    • Conservation of substrate specificities among coronavirus main proteases
    • Hegyi A, Ziebuhr J. 2002. Conservation of substrate specificities among coronavirus main proteases. J. Gen. Virol. 83:595-599.
    • (2002) J. Gen. Virol. , vol.83 , pp. 595-599
    • Hegyi, A.1    Ziebuhr, J.2
  • 38
    • 0031047974 scopus 로고    scopus 로고
    • The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition
    • Bergmann EM, Mosimann SC, Chernaia MM, Malcolm BA, James MN. 1997. The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition. J. Virol. 71:2436- 2448.
    • (1997) J. Virol. , vol.71 , pp. 2436-2448
    • Bergmann, E.M.1    Mosimann, S.C.2    Chernaia, M.M.3    Malcolm, B.A.4    James, M.N.5
  • 39
    • 0031567786 scopus 로고    scopus 로고
    • Refined X-ray crystallographic structure of the poliovirus 3C gene product
    • Mosimann SC, Cherney MM, Sia S, Plotch S, James MN. 1997. Refined X-ray crystallographic structure of the poliovirus 3C gene product. J. Mol. Biol. 273:1032-1047. http://dx.doi.org/10.1006/jmbi.1997.1306.
    • (1997) J. Mol. Biol. , vol.273 , pp. 1032-1047
    • Mosimann, S.C.1    Cherney, M.M.2    Sia, S.3    Plotch, S.4    James, M.N.5
  • 41
    • 84883591545 scopus 로고    scopus 로고
    • Scalable web services for the PSIPRED Protein Analysis Workbench
    • Buchan DW, Minneci F, Nugent TC, Bryson K, Jones DT. 2013. Scalable web services for the PSIPRED Protein Analysis Workbench. Nucleic Acids Res. 41:W349-W357. http://dx.doi.org/10.1093/nar/gkt381.
    • (2013) Nucleic Acids Res , vol.41 , pp. W349-W357
    • Buchan, D.W.1    Minneci, F.2    Nugent, T.C.3    Bryson, K.4    Jones, D.T.5
  • 42
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT. 1999. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292:195-202. http://dx.doi.org /10.1006/jmbi.1999.3091.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 43
    • 0025008168 scopus 로고
    • Sequence logos: a new way to display consensus sequences
    • Schneider TD, Stephens RM. 1990. Sequence logos: a new way to display consensus sequences. Nucleic Acids Res. 18:6097-6100. http://dx.doi.org /10.1093/nar/18.20.6097.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.