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Volumn 86, Issue 12, 2012, Pages 6778-6791

Classical swine fever virus p7 protein is a viroporin involved in virulence in swine

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN VP7;

EID: 84863986411     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00560-12     Document Type: Article
Times cited : (54)

References (40)
  • 1
    • 77956996035 scopus 로고    scopus 로고
    • Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus
    • Acharya R, et al. 2010. Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus. Proc. Natl. Acad. Sci. U. S. A. 107:15075-15080.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 15075-15080
    • Acharya, R.1
  • 2
    • 35648943768 scopus 로고    scopus 로고
    • Toward high-resolution prediction and design of transmembrane helical protein structures
    • Barth P, Schonbrun J, Baker D. 2007. Toward high-resolution prediction and design of transmembrane helical protein structures. Proc. Natl. Acad. Sci. U. S. A. 104:15682-15687.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 15682-15687
    • Barth, P.1    Schonbrun, J.2    Baker, D.3
  • 3
    • 0037708784 scopus 로고    scopus 로고
    • Genetic and antigenic characterization of novel pestivirus genotypes: implications for classification
    • Becher P, et al. 2003. Genetic and antigenic characterization of novel pestivirus genotypes: implications for classification. Virology 311:96 - 104.
    • (2003) Virolog , vol.311 , pp. 96-104
    • Becher, P.1
  • 4
    • 55749093073 scopus 로고    scopus 로고
    • Patterns of cellular gene expression in swine macrophages infected with highly virulent classical swine fever virus strain Brescia
    • Borca MV, Gudmundsdottir I, Fernandez-Sainz IJ, Holinka LG, Risatti GR. 2008. Patterns of cellular gene expression in swine macrophages infected with highly virulent classical swine fever virus strain Brescia. Virus Res. 138:89 -96.
    • (2008) Virus Res , vol.138 , pp. 89-96
    • Borca, M.V.1    Gudmundsdottir, I.2    Fernandez-Sainz, I.J.3    Holinka, L.G.4    Risatti, G.R.5
  • 5
    • 0036199092 scopus 로고    scopus 로고
    • Subcellular localization and topology of the p7 polypeptide of hepatitis C virus
    • Carrere-Kremer S, et al. 2002. Subcellular localization and topology of the p7 polypeptide of hepatitis C virus. J. Virol. 76:3720 -3730.
    • (2002) J. Virol. , vol.76 , pp. 3720-3730
    • Carrere-Kremer, S.1
  • 6
    • 0025788574 scopus 로고
    • The development of aninternational reference panel of monoclonal antibodies for the differentiation of hog cholera virus from other pestiviruses
    • Edwards S, Moennig V, Wensvoort G. 1991. The development of aninternational reference panel of monoclonal antibodies for the differentiation of hog cholera virus from other pestiviruses. Vet. Microbiol. 29:101- 108.
    • (1991) Vet. Microbiol. , vol.29 , pp. 101-108
    • Edwards, S.1    Moennig, V.2    Wensvoort, G.3
  • 7
    • 0029893139 scopus 로고    scopus 로고
    • Processing in the pestivirus E2-NS2 region: identification of proteins p7 and E2p7
    • Elbers K, et al. 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
  • 8
    • 0021890825 scopus 로고
    • +-induced fusion and destabilization of liposomes
    • +-induced fusion and destabilization of liposomes. Biochemistry 24:3099 -3106.
    • (1985) Biochemistry , vol.24 , pp. 3099-3106
    • Ellens, H.1    Bentz, J.2    Szoka, F.C.3
  • 9
    • 73949160126 scopus 로고    scopus 로고
    • Mutations in classical swine fever virus NS4B affect virulence in swine
    • Fernandez-Sainz I, et al. 2010. Mutations in classical swine fever virus NS4B affect virulence in swine. J. Virol. 84:1536 -1549.
    • (2010) J. Virol. , vol.84 , pp. 1536-1549
    • Fernandez-Sainz, I.1
  • 10
    • 52649123300 scopus 로고    scopus 로고
    • Cytopathogenicity of classical swine fever virus correlates with attenuation in the natural host
    • Gallei A, et al. 2008. Cytopathogenicity of classical swine fever virus correlates with attenuation in the natural host. J. Virol. 82:9717-9729.
    • (2008) J. Virol. , vol.82 , pp. 9717-9729
    • Gallei, A.1
  • 12
    • 0037472806 scopus 로고    scopus 로고
    • The p7 protein of hepatitis C virus forms an ion channel that is blocked by the antiviral drug, amantadine
    • Griffin SD, et al. 2003. The p7 protein of hepatitis C virus forms an ion channel that is blocked by the antiviral drug, amantadine. FEBS Lett. 535: 34-38.
    • (2003) FEBS Lett , vol.535 , pp. 34-38
    • Griffin, S.D.1
  • 13
    • 1342289027 scopus 로고    scopus 로고
    • A conserved basic loop in hepatitis C virus p7 protein is required for amantadine-sensitive ion channel activity in mammalian cells but is dispensable for localization to mitochondria
    • Griffin SD, et al. 2004. A conserved basic loop in hepatitis C virus p7 protein is required for amantadine-sensitive ion channel activity in mammalian cells but is dispensable for localization to mitochondria. J. Gen. Virol. 85:451- 461.
    • (2004) J. Gen. Virol , vol.85 , pp. 451-461
    • Griffin, S.D.1
  • 14
    • 0033819541 scopus 로고    scopus 로고
    • E2-p7 region of the bovine viral diarrhea virus polyprotein: processing and functional studies
    • Harada T, Tautz N, Thiel HJ. 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
  • 15
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure: characterization of size distribution, trapped volume, and ability to maintain a membrane potential
    • Hope MJ, et al. 1985. Production of large unilamellar vesicles by a rapid extrusion procedure: characterization of size distribution, trapped volume, and ability to maintain a membrane potential. Biochim. Biophys. Acta 812:55- 65.
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 55-65
    • Hope, M.J.1
  • 16
    • 77958162674 scopus 로고    scopus 로고
    • Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMR
    • Hu F, Luo W, Hong M. 2010. Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMR. Science 330:505-508.
    • (2010) Science , vol.330 , pp. 505-508
    • Hu, F.1    Luo, W.2    Hong, M.3
  • 17
    • 50949104097 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 4E10 monoclonal antibody is better adapted to membrane-bound epitope recognition and blocking than 2F5
    • Huarte N, et al. 2008. The broadly neutralizing anti-human immunodeficiency virus type 1 4E10 monoclonal antibody is better adapted to membrane-bound epitope recognition and blocking than 2F5. J. Virol. 82: 8986-8996.
    • (2008) J. Virol , vol.82 , pp. 8986-8996
    • Huarte, N.1
  • 18
    • 34547734952 scopus 로고    scopus 로고
    • Hepatitis C virus p7 and NS2 proteins are essential for production of infectious virus
    • Jones CT, Murray CL, Eastman DK, Tassello J, Rice CM. 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
  • 19
    • 67849103757 scopus 로고    scopus 로고
    • SAM-T08 HMM-based protein structure prediction
    • Karplus K. 2009. SAM-T08, HMM-based protein structure prediction. Nucleic Acids Res. 37:W492-W497.
    • (2009) Nucleic Acids Res , vol.37
    • Karplus, K.1
  • 20
    • 79952580332 scopus 로고    scopus 로고
    • Biosynthesis of classical swine fever virus nonstructural proteins
    • Lamp B, et al. Biosynthesis of classical swine fever virus nonstructural proteins. J. Virol. 85:3607-3620.
    • J. Virol , vol.85 , pp. 3607-3620
    • Lamp, B.1
  • 21
    • 77951296857 scopus 로고    scopus 로고
    • A novel hepatitis C virus p7 ion channel inhibitor, BIT225, inhibits bovine viral diarrhea virus in vitro and shows synergism with recombinant interferon-_-2b and nucleoside analogues
    • Luscombe CA, et al. 2010. A novel hepatitis C virus p7 ion channel inhibitor, BIT225, inhibits bovine viral diarrhea virus in vitro and shows synergism with recombinant interferon-_-2b and nucleoside analogues. Antivir. Res. 86:144 -153.
    • (2010) Antivir. Res , vol.86 , pp. 144-153
    • Luscombe, C.A.1
  • 22
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin LJ, Bryson K, Jones DT. 2000. The PSIPRED protein structure prediction server. Bioinformatics 16:404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 23
    • 0034641033 scopus 로고    scopus 로고
    • Analysis of classical swine fever virus replication kinetics allows differentiation of highly virulent from avirulent strains
    • Mittelholzer C, Moser C, Tratschin JD, Hofmann MA. 2000. Analysis of classical swine fever virus replication kinetics allows differentiation of highly virulent from avirulent strains. Vet. Microbiol. 74:293-308.
    • (2000) Vet. Microbiol , vol.74 , pp. 293-308
    • Mittelholzer, C.1    Moser, C.2    Tratschin, J.D.3    Hofmann, M.A.4
  • 24
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips R, Ursell T, Wiggins P, Sens P. 2009. Emerging roles for lipids in shaping membrane-protein function. Nature 459:379 -385.
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 25
    • 33745158157 scopus 로고
    • A simple method of estimating fifty per cent endpoints
    • Reed LJ, Muench HA. 1938. A simple method of estimating fifty per cent endpoints. Am. J. Hyg. 27:493- 497.
    • (1938) Am. J. Hyg , vol.27
    • Reed, L.J.1    Muench, H.A.2
  • 26
    • 14744267515 scopus 로고    scopus 로고
    • The E2 glycoprotein of classical swine fever virus is a virulence determinant in swine
    • Risatti GR, et al. 2005. The E2 glycoprotein of classical swine fever virus is a virulence determinant in swine. J. Virol. 79:3787-3796.
    • (2005) J. Virol , vol.79 , pp. 3787-3796
    • Risatti, G.R.1
  • 27
    • 27644442081 scopus 로고    scopus 로고
    • Mutation of E1 glycoprotein of classical swine fever virus affects viral virulence in swine
    • Risatti GR, et al. 2005. Mutation of E1 glycoprotein of classical swine fever virus affects viral virulence in swine. Virology 343:116 -127.
    • (2005) Virology , vol.343 , pp. 116-127
    • Risatti, G.R.1
  • 28
    • 36549074575 scopus 로고    scopus 로고
    • Removal of a N-linked glycosylation site of classical swine fever virus strain Brescia Erns glycoprotein affects virulence in swine
    • Sainz IF, Holinka LG, Lu Z, Risatti GR, Borca MV. 2008. Removal of a N-linked glycosylation site of classical swine fever virus strain Brescia Erns glycoprotein affects virulence in swine. Virology 370:122-129.
    • (2008) Virology , vol.370 , pp. 122-129
    • Sainz, I.F.1    Holinka, L.G.2    Lu, Z.3    Risatti, G.R.4    Borca, M.V.5
  • 29
    • 0141816748 scopus 로고    scopus 로고
    • The p7 polypeptide of hepatitis C virus is critical for infectivity and contains functionally important genotype-specific sequences
    • Sakai A, et al. 2003. The p7 polypeptide of hepatitis C virus is critical for infectivity and contains functionally important genotype-specific sequences. Proc. Natl. Acad. Sci. U. S. A. 100:11646 -11651.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 11646-11651
    • Sakai, A.1
  • 32
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N, Woody RW. 2000. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287:252-260.33.
    • (2000) Anal. Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 33
    • 34547616693 scopus 로고    scopus 로고
    • Hepatitis C virus p7 protein is crucial for assembly and release of infectious virions
    • Steinmann E, et al. 2007. Hepatitis C virus p7 protein is crucial for assembly and release of infectious virions. PLoS Pathog. 3:-103.
    • (2007) PLoS Pathog , vol.3 , pp. 103
    • Steinmann, E.1
  • 34
    • 67749139975 scopus 로고    scopus 로고
    • Determinants of hepatitis C virus p7 ion channel function and drug sensitivity identified in vitro
    • St Gelais C, et al. 2009. Determinants of hepatitis C virus p7 ion channel function and drug sensitivity identified in vitro. J. Virol. 83: 7970 -7981.
    • (2009) J. Virol , vol.83 , pp. 7970-7981
    • St Gelais, C.1
  • 35
    • 0025377823 scopus 로고
    • Development and properties of a cell culture produced vaccine for hog cholera based on the Chinese strain
    • Terpstra C, Woortmeyer R, Barteling SJ. 1990. Development and properties of a cell culture produced vaccine for hog cholera based on the Chinese strain. Dtsch. Tierarztl. Wochenschr. 97:77-79.
    • (1990) Dtsch. Tierarztl. Wochenschr , vol.97 , pp. 77-79
    • Terpstra, C.1    Woortmeyer, R.2    Barteling, S.J.3
  • 36
    • 0025955758 scopus 로고
    • Hog cholera virus: molecular composition of virions from a pestivirus
    • Thiel HJ, Stark R, Weiland E, Rumenapf T, Meyers G. 1991. Hog cholera virus: molecular composition of virions from a pestivirus. J. Virol. 65:4705- 4712.
    • (1991) J. Virol , vol.65
    • Thiel, H.J.1    Stark, R.2    Weiland, E.3    Rumenapf, T.4    Meyers, G.5
  • 38
    • 20444385829 scopus 로고    scopus 로고
    • Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virus
    • Venkataraman P, Lamb RA, Pinto LH. 2005. Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virus. J. Biol. Chem. 280:21463-21472.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21463-21472
    • Venkataraman, P.1    Lamb, R.A.2    Pinto, L.H.3
  • 39
    • 57249083976 scopus 로고    scopus 로고
    • SPOCTOPUS: a combined predictor of signal peptides and membrane protein topology
    • Viklund H, Bernsel A, Skwark M, Elofsson A. 2008. SPOCTOPUS: a combined predictor of signal peptides and membrane protein topology. Bioinformatics 24:2928 -2929.
    • (2008) Bioinformatics , vol.24 , pp. 2928-2929
    • Viklund, H.1    Bernsel, A.2    Skwark, M.3    Elofsson, A.4
  • 40
    • 0029911070 scopus 로고    scopus 로고
    • An African swine fever virus virulence-associated gene NL-S with similarity to the herpes simplex virus ICP34
    • Zsak L, Lu Z, Kutish GF, Neilan JG, Rock DL. 1996. An African swine fever virus virulence-associated gene NL-S with similarity to the herpes simplex virus ICP34.5 gene. J. Virol. 70:8865- 8871.
    • (1996) 5 gene. J. Virol , vol.70 , pp. 8865-8871
    • Zsak, L.1    Lu, Z.2    Kutish, G.F.3    Neilan, J.G.4    Rock, D.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.