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Volumn 12, Issue 2, 2013, Pages 234-241

Pilot study on degradation of classical swine fever virus nonstructural 2 protein in cells

Author keywords

China; Classical swine fever virus; NS2 protein; Phosphorylation; Protein degradation

Indexed keywords


EID: 84880654980     PISSN: 16805593     EISSN: 1993601X     Source Type: Journal    
DOI: 10.3923/javaa.2013.234.241     Document Type: Article
Times cited : (3)

References (36)
  • 1
    • 1242319434 scopus 로고    scopus 로고
    • UncleavedNS2-3 is required for production of infectious bovine viral diarrhea virus
    • Agapov, E.V., C.L. Murray, I. Frolov, L. Qu, T.M. Myers and CM. Rice, 2004. UncleavedNS2-3 is required for production of infectious bovine viral diarrhea virus. J. Virol., 78: 2414-2425.
    • (2004) J. Virol. , vol.78 , pp. 2414-2425
    • Agapov, E.V.1    Murray, C.L.2    Frolov, I.3    Qu, L.4    Myers, T.M.5    Rice, C.M.6
  • 2
    • 0031888265 scopus 로고    scopus 로고
    • Characterization of an autonomous subgenomic pestivirus rna replicon
    • Behrens, S.E., C.W. Grassmann, H.J. Thiel, G. Meyers and N. Tautz, 1998. Characterization of an autonomous subgenomic pestivirus rna replicon. J. Virol., 72: 2364-2372.
    • (1998) J. Virol. , vol.72 , pp. 2364-2372
    • Behrens, S.E.1    Grassmann, C.W.2    Thiel, H.J.3    Meyers, G.4    Tautz, N.5
  • 3
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover, A., 1998. The ubiquitin-proteasome pathway: On protein death and cell life. EMBOJ., 17: 7151-7160.
    • (1998) EMBOJ. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 4
    • 0037010150 scopus 로고    scopus 로고
    • Stabilization signals: A novel regulatory mechanism in the ubiquitin/proteasome system
    • Dantuma, N.P. and M.G. Masucci, 2002. Stabilization signals: A novel regulatory mechanism in the ubiquitin/proteasome system. FEBS Lett., 529: 22-26.
    • (2002) FEBS Lett. , vol.529 , pp. 22-26
    • Dantuma, N.P.1    Masucci, M.G.2
  • 5
    • 33846579485 scopus 로고    scopus 로고
    • A sequence database allowing automated genotyping of classical swine fever virus isolates
    • Dreier, S., B. Zimmermann, V. Moennig and I. Greiser-Wilke, 2007. A sequence database allowing automated genotyping of classical swine fever virus isolates. J. Virol. Methods, 140: 95-99.
    • (2007) J. Virol. Methods , vol.140 , pp. 95-99
    • Dreier, S.1    Zimmermann, B.2    Moennig, V.3    Greiser-Wilke, I.4
  • 6
    • 0029893139 scopus 로고    scopus 로고
    • Processing in the pestivirus E2-NS2 region: Identification of proteins p7 and E2p7
    • Elbers, K., N. Tautz, P. Becher, D. Stall, T. Rumenapf and H.J. Thiel, 1996. Processing in the pestivirus E2-NS2 region: Identification of proteins p7 and E2p7. J. Virol., 70: 4131-4135.
    • (1996) J. Virol. , vol.70 , pp. 4131-4135
    • Elbers, K.1    Tautz, N.2    Becher, P.3    Stall, D.4    Rumenapf, T.5    Thiel, H.J.6
  • 7
    • 13944275171 scopus 로고    scopus 로고
    • Hepatitis C virus NS2 protein is phosphorylated by the protein kinase CK2 and targeted for degradation to the proteasome
    • Franck, N, J. le Seyec, C. Guguen-Guillouzo and L. Erdtmann, 2005. Hepatitis C virus NS2 protein is phosphorylated by the protein kinase CK2 and targeted for degradation to the proteasome. J. Virol., 79: 2700-2708.
    • (2005) J. Virol. , vol.79 , pp. 2700-2708
    • Franck, N.1    le Seyec, J.2    Guguen-Guillouzo, C.3    Erdtmann, L.4
  • 8
    • 13444261167 scopus 로고    scopus 로고
    • Characterization of helper virus-independent cytopathogenic classical swine fever virus generated by an in vivo RNA recombination system
    • Gallei, A., T. Rumenapf, H.J. Thiel and P. Becher, 2005. Characterization of helper virus-independent cytopathogenic classical swine fever virus generated by an in vivo RNA recombination system. J. Virol., 79: 2440-2448.
    • (2005) J. Virol. , vol.79 , pp. 2440-2448
    • Gallei, A.1    Rumenapf, T.2    Thiel, H.J.3    Becher, P.4
  • 9
    • 0037378613 scopus 로고    scopus 로고
    • Interaction with a ubiquitin-like protein enhances the ubiquitination and degradation of hepatitis C virus RNA-dependent RNA polymerase
    • Gao, L., H. Tu, S.T. Shi, K.J. Lee, M. Asanaka, S.B. Hwang and M.M.C. Lai, 2003. Interaction with a ubiquitin-like protein enhances the ubiquitination and degradation of hepatitis C virus RNA-dependent RNA polymerase. J. Virol, 77: 4149-4159.
    • (2003) J. Virol , vol.77 , pp. 4149-4159
    • Gao, L.1    Tu, H.2    Shi, S.T.3    Lee, K.J.4    Asanaka, M.5    Hwang, S.B.6    Lai, M.M.C.7
  • 10
    • 30344487269 scopus 로고    scopus 로고
    • The amino-terminal domain of bovine viral diarrhea virus npro protein is necessary for alpha/beta interferon antagonism
    • Gil, L.H.V.G., I.H. Ansari, V. Vassilev, D. Liang and V.C.H. Lai et al, 2006. The amino-terminal domain of bovine viral diarrhea virus npro protein is necessary for alpha/beta interferon antagonism. J. Virol., 80: 900-911.
    • (2006) J. Virol. , vol.80 , pp. 900-911
    • Gil, L.H.V.G.1    Ansari, I.H.2    Vassilev, V.3    Liang, D.4    Lai, V.C.H.5
  • 11
    • 79955977371 scopus 로고    scopus 로고
    • Identification of two internal signal peptide sequences: Critical for classical swine fever virus non-structural protein 2 to trans-localize to the endoplasmic reticulum
    • 10.1186/1743-422X-8-236
    • Guo, K.K., Q.H. Tang, Y.M. Zhang, K. Kang andL. He, 2011. Identification of two internal signal peptide sequences: Critical for classical swine fever virus non-structural protein 2 to trans-localize to the endoplasmic reticulum. Virol. J., Vol. 8. 10.1186/1743-422X-8-236.
    • (2011) Virol. J. , vol.8
    • Guo, K.K.1    Tang, Q.H.2    Zhang, Y.M.3    Kang, K.4    He, L.5
  • 12
    • 0033819541 scopus 로고    scopus 로고
    • E2-p7 region of the bovine viral diarrhea virus polyprotein: Processing and functional studies
    • Harada, T., N. Tautz andH.J. Thiel, 2000. E2-p7 region of the bovine viral diarrhea virus polyprotein: Processing and functional studies. J. Virol., 74: 9498-9506.
    • (2000) J. Virol. , vol.74 , pp. 9498-9506
    • Harada, T.1    Tautz, N.2    Thiel, H.J.3
  • 13
    • 38349002990 scopus 로고    scopus 로고
    • Immortalization of swine umbilical wein endothelial cells with human telomerase reverse transcriptase
    • Hong, H.X., Y.M. Zhang, H. Xu, Z.Y. SuandP. Sun, 2007. Immortalization of swine umbilical wein endothelial cells with human telomerase reverse transcriptase. Mol. Cells, 3: 358-363.
    • (2007) Mol. Cells , vol.3 , pp. 358-363
    • Hong, H.X.1    Zhang, Y.M.2    Xu, H.3    Su, Z.Y.4    Sun, P.5
  • 14
    • 70349266012 scopus 로고    scopus 로고
    • Small molecule targets env for endoplasmic reticulum-associated protein degradation and inhibits human immunodeficiency virus type 1 propagation
    • Jejcic, A., R. Daniels, L. Goobar-Larsson, D.N. Hebert and A. Vahlne, 2009. Small molecule targets env for endoplasmic reticulum-associated protein degradation and inhibits human immunodeficiency virus type 1 propagation. J. Virol, 83: 10075-10084.
    • (2009) J. Virol , vol.83 , pp. 10075-10084
    • Jejcic, A.1    Daniels, R.2    Goobar-Larsson, L.3    Hebert, D.N.4    Vahlne, A.5
  • 15
    • 34547734952 scopus 로고    scopus 로고
    • Hepatitis C virus p7 and NS2 proteins are essential for production of infectious virus
    • Jones, C.T., C.L. Murray, D.K. Eastman, J. Tassello and CM. Rice, 2007. Hepatitis C virus p7 and NS2 proteins are essential for production of infectious virus. J. Virol, 81: 8374-8383.
    • (2007) J. Virol , vol.81 , pp. 8374-8383
    • Jones, C.T.1    Murray, C.L.2    Eastman, D.K.3    Tassello, J.4    Rice, C.M.5
  • 16
    • 0037452979 scopus 로고    scopus 로고
    • Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein
    • Kalejta, R.F. and T. Shenk, 2003. Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein. Proc. Natl. Acad. Sci. USA., 100: 3263-3268.
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 3263-3268
    • Kalejta, R.F.1    Shenk, T.2
  • 17
    • 85027945595 scopus 로고    scopus 로고
    • Interactive cellular proteins related to classical swine fever virus non-structure protein 2 by yeast two-hybrid analysis
    • Kang, K., K. Guo, Q. Tang, Y. Zhang, J. Wu, W. Li and Z. Lin, 2012. Interactive cellular proteins related to classical swine fever virus non-structure protein 2 by yeast two-hybrid analysis. Mol. Biol. Rep., 39: 10515-10524.
    • (2012) Mol. Biol. Rep. , vol.39 , pp. 10515-10524
    • Kang, K.1    Guo, K.2    Tang, Q.3    Zhang, Y.4    Wu, J.5    Li, W.6    Lin, Z.7
  • 18
    • 22544449902 scopus 로고    scopus 로고
    • Persistence of bovine viral diarrhea virus is determined by a cellular cofactor of a viral autoprotease
    • Lackner, T., A. Muller, M. Komg, H.J. Thiel andN. Tautz, 2005. Persistence of bovine viral diarrhea virus is determined by a cellular cofactor of a viral autoprotease. J. Virol, 79: 9746-9755.
    • (2005) J. Virol , vol.79 , pp. 9746-9755
    • Lackner, T.1    Muller, A.2    Komg, M.3    Thiel, H.J.4    Tautz, N.5
  • 19
    • 31944434363 scopus 로고    scopus 로고
    • Dissection of a viral autoprotease elucidates a function of a cellular chaperone in proteolysis
    • Lackner, T., H.J. Thiel andN. Tautz, 2006. Dissection of a viral autoprotease elucidates a function of a cellular chaperone in proteolysis. Proc. Natl. Acad. Sci. USA., 103: 1510-1515.
    • (2006) Proc. Natl. Acad. Sci. USA. , vol.103 , pp. 1510-1515
    • Lackner, T.1    Thiel, H.J.2    Tautz, N.3
  • 20
    • 0033938356 scopus 로고    scopus 로고
    • Generation and characterization of a hepatitis C virus NS3 protease-dependent bovine viral diarrhea virus
    • Lai, V.C.H., W. Zhong, A. Skelton, P. Ingravallo and V. Vassileve? a/., 2000. Generation and characterization of a hepatitis C virus NS3 protease-dependent bovine viral diarrhea virus. J. Virol, 74: 6339-6347.
    • (2000) J. Virol , vol.74 , pp. 6339-6347
    • Lai, V.C.H.1    Zhong, W.2    Skelton, A.3    Ingravallo, P.4    Vassilev, V.5
  • 21
    • 79952580332 scopus 로고    scopus 로고
    • Biosynthesis of classical swine fever virus nonstructural proteins
    • Lamp, B., C. Riedel, G. Roman-Sosa, M. Heimann and S. Jacobi et al., 2011. Biosynthesis of classical swine fever virus nonstructural proteins. J. Virol, 85: 3607-3620.
    • (2011) J. Virol , vol.85 , pp. 3607-3620
    • Lamp, B.1    Riedel, C.2    Roman-Sosa, G.3    Heimann, M.4    Jacobi, S.5
  • 22
    • 33747452685 scopus 로고    scopus 로고
    • Structure of the catalytic domain of the hepatitis C virus NS2-3 protease
    • Lorenz, I.C., J. Marcotrigiano, T.G. Dentzer and CM. Rice, 2006. Structure of the catalytic domain of the hepatitis C virus NS2-3 protease. Nature, 442: 831-835.
    • (2006) Nature , vol.442 , pp. 831-835
    • Lorenz, I.C.1    Marcotrigiano, J.2    Dentzer, T.G.3    Rice, C.M.4
  • 24
    • 0032864837 scopus 로고    scopus 로고
    • Cytopathogenic and noncytopathogenic RNA replicons of classical swine fever virus
    • Moser, C, P. Stettler, J.D. TratschinandM.A. Hofmann, 1999. Cytopathogenic and noncytopathogenic RNA replicons of classical swine fever virus. J. Virol, 73: 7787-7794.
    • (1999) J. Virol , vol.73 , pp. 7787-7794
    • Moser, C.1    Stettler, P.2    Tratschin, J.D.3    Hofmann, M.A.4
  • 25
    • 34547686361 scopus 로고    scopus 로고
    • Nonstructural proteins NS2-3 and NS4A of classical swine fever virus: Essential features for infectious particle formation
    • Moulin, H.R., T. Seuberlich, O. Bauhofer, L.C. Bennett, J.D. Tratschm, M.A. Hofmann andN. Ruggli, 2007. Nonstructural proteins NS2-3 and NS4A of classical swine fever virus: Essential features for infectious particle formation. Virology, 365: 376-389.
    • (2007) Virology , vol.365 , pp. 376-389
    • Moulin, H.R.1    Seuberlich, T.2    Bauhofer, O.3    Bennett, L.C.4    Tratschm, J.D.5    Hofmann, M.A.6    Ruggli, N.7
  • 26
    • 49649102821 scopus 로고    scopus 로고
    • Architects of assembly: Roles of Flaviviridae non-structural proteins in virion morphogenesis
    • Munay, C.L., C.T. Jones and CM. Rice, 2008. Architects of assembly: Roles of Flaviviridae non-structural proteins in virion morphogenesis. Nat. Rev. Microbiol, 6: 699-708.
    • (2008) Nat. Rev. Microbiol , vol.6 , pp. 699-708
    • Munay, C.L.1    Jones, C.T.2    Rice, C.M.3
  • 27
    • 0034791090 scopus 로고    scopus 로고
    • Ubiquitin enters the new millennium
    • Pickart, CM., 2001. Ubiquitin enters the new millennium. Mol. Cell, 8: 499-504.
    • (2001) Mol. Cell , vol.8 , pp. 499-504
    • Pickart, C.M.1
  • 29
    • 65249157102 scopus 로고    scopus 로고
    • Hepatitis C virus NS2 is a protease stimulated by cofactor domains inNS3
    • Schregel, V., S. Jacobi, F. Penin and N. Tautz, 2009. Hepatitis C virus NS2 is a protease stimulated by cofactor domains inNS3. Proc. Natl. Acad. Sci USA., 106: 5342-5347.
    • (2009) Proc. Natl. Acad. Sci USA. , vol.106 , pp. 5342-5347
    • Schregel, V.1    Jacobi, S.2    Penin, F.3    Tautz, N.4
  • 30
    • 0027254336 scopus 로고
    • RNA-stimulated ntpase activity associated with the p80 protein of the pestivirus bovine viral diarrhea virus
    • Tamura, J.K., P. Warrener and M.S. Collett, 1993. RNA-stimulated ntpase activity associated with the p80 protein of the pestivirus bovine viral diarrhea virus. Virology, 193: 1-10.
    • (1993) Virology , vol.193 , pp. 1-10
    • Tamura, J.K.1    Warrener, P.2    Collett, M.S.3
  • 31
    • 0028872259 scopus 로고
    • Pestivirus NS3 (p80) protein possesses RNA helicase activity
    • Warrener, P. andM.S. Collett 1995. Pestivirus NS3 (p80) protein possesses RNA helicase activity. J. Virol, 69: 1720-1726.
    • (1995) J. Virol , vol.69 , pp. 1720-1726
    • Warrener, P.1    Collett, M.S.2
  • 32
    • 33846424965 scopus 로고    scopus 로고
    • The hepatitis C virus NS2/3 protease
    • Welbourn, S. and A. Pause, 2007. The hepatitis C virus NS2/3 protease. Curr. Issues Mol. Biol, 9: 63-69.
    • (2007) Curr. Issues Mol. Biol , vol.9 , pp. 63-69
    • Welbourn, S.1    Pause, A.2
  • 33
    • 0031010133 scopus 로고    scopus 로고
    • Bovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage sites, cofactor requirements and molecular model of an enzyme essential for pestivirus replication
    • Xu, J., E. Mendez, P.R Caron, C. Lin, M.A. Murcko, M.S. Collett and CM. Rice, 1997. Bovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage sites, cofactor requirements and molecular model of an enzyme essential for pestivirus replication. J. Virol, 71: 5312-5322.
    • (1997) J. Virol , vol.71 , pp. 5312-5322
    • Xu, J.1    Mendez, E.2    Caron, P.R.3    Lin, C.4    Murcko, M.A.5    Collett, M.S.6    Rice, C.M.7
  • 34
    • 0037031947 scopus 로고    scopus 로고
    • Membrane topology of the hepatitis C virus NS2 protein
    • Yamaga, A.K. and J.H. Ou, 2002. Membrane topology of the hepatitis C virus NS2 protein. J. Biol. Chem., 277: 33228-33234.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33228-33234
    • Yamaga, A.K.1    Ou, J.H.2
  • 35
    • 67249088420 scopus 로고    scopus 로고
    • Trans-complementation of an NS2 defect in a late step in hepatitis C virus (HCV) particle assembly and maturation
    • 10.1371/journalppat.l 000403
    • Yi, M., Y. Ma, J. Yates and S.M. Lemon, 2009. Trans-complementation of an NS2 defect in a late step in hepatitis C virus (HCV) particle assembly and maturation. PLoS Pathogens, Vol. 5, No. 5. 10.1371/journalppat.l 000403.
    • (2009) PLoS Pathogens , vol.5 , Issue.5
    • Yi, M.1    Ma, Y.2    Yates, J.3    Lemon, S.M.4
  • 36
    • 58149517677 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of hepatitis C virus F protein
    • Yuksek, K., W.L. Chen, D. Chien and J.H.J. Ou, 2009. Ubiquitin-independent degradation of hepatitis C virus F protein. J. Virol, 83: 612-621.
    • (2009) J. Virol , vol.83 , pp. 612-621
    • Yuksek, K.1    Chen, W.L.2    Chien, D.3    Ou, J.H.J.4


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