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Volumn 586, Issue 4, 2012, Pages 384-391

PEDV ORF3 encodes an ion channel protein and regulates virus production

Author keywords

Ion channel; Molecular dynamics; ORF3; PEDV

Indexed keywords

ION CHANNEL; ORF3 PROTEIN; POTASSIUM CHANNEL; SMALL INTERFERING RNA; TM4 PROTEIN; TYROSINE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84862831888     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.01.005     Document Type: Article
Times cited : (143)

References (34)
  • 1
    • 0034749116 scopus 로고    scopus 로고
    • Completion of the porcine epidemic diarrhoea coronavirus (PEDV) genome sequence
    • DOI 10.1023/A:1011831902219
    • R. Kocherhans, A. Bridgen, M. Ackermann, and K. Tobler Completion of the porcine epidemic diarrhoea coronavirus (PEDV) genome sequence Virus Genes 23 2001 137 144 (Pubitemid 33020687)
    • (2001) Virus Genes , vol.23 , Issue.2 , pp. 137-144
    • Kocherhans, R.1    Bridgen, A.2    Ackermann, M.3    Tobler, K.4
  • 2
    • 0019830599 scopus 로고
    • The pathogenesis of an enteric infection in pigs, experimentally induced by the coronavirus-like agent, CV 777
    • DOI 10.1016/0378-1135(81)90007-9
    • P. Debouck, M. Pensaert, and W. Coussement The pathogenesis of an enteric infection in pigs, experimentally induced by the coronavirus-like agent, CV777 Vet. Microbiol. 6 1981 157 165 (Pubitemid 11043902)
    • (1981) Veterinary Microbiology , vol.6 , Issue.2 , pp. 157-165
    • Debouck, P.1    Pensaert, M.2    Coussement, W.3
  • 4
    • 0037449096 scopus 로고    scopus 로고
    • Differentiation of a Vero cell adapted porcine epidemic diarrhea virus from Korean field strains by restriction fragment length polymorphism analysis of ORF 3
    • DOI 10.1016/S0264-410X(03)00027-6
    • D.S. Song, J.S. Yang, J.S. Oh, J.H. Han, and B.K. Park Differentiation of a Vero cell adapted porcine epidemic diarrhea virus from Korean field strains by restriction fragment length polymorphism analysis of ORF 3 Vaccine 21 2003 1833 1842 (Pubitemid 36428773)
    • (2003) Vaccine , vol.21 , Issue.17-18 , pp. 1833-1842
    • Song, D.S.1    Yang, J.S.2    Oh, J.S.3    Han, J.H.4    Park, B.K.5
  • 5
    • 0028227851 scopus 로고
    • Sequence analysis of the porcine epidemic diarrhea virus genome between the nucleocapsid and spike protein genes reveals a polymorphic ORF
    • M. Duarte, K. Tobler, A. Bridgen, D. Rasschaert, M. Ackermann, and H. Laude Sequence analysis of the porcine epidemic diarrhea virus genome between the nucleocapsid and spike protein genes reveals a polymorphic ORF Virology 198 1994 466 476
    • (1994) Virology , vol.198 , pp. 466-476
    • Duarte, M.1    Tobler, K.2    Bridgen, A.3    Rasschaert, D.4    Ackermann, M.5    Laude, H.6
  • 9
    • 38849173816 scopus 로고    scopus 로고
    • Cloning and further sequence analysis of the ORF3 gene of wild- and attenuated-type porcine epidemic diarrhea viruses
    • DOI 10.1007/s11262-007-0164-2
    • S.J. Park, H.J. Moon, Y. Luo, H.K. Kim, E.M. Kim, J.S. Yang, D.S. Song, B.K. Kang, C.S. Lee, and B.K. Park Cloning and further sequence analysis of the ORF3 gene of wild- and attenuated-type porcine epidemic diarrhea viruses Virus Genes 36 2008 95 104 (Pubitemid 351195185)
    • (2008) Virus Genes , vol.36 , Issue.1 , pp. 95-104
    • Park, S.-J.1    Moon, H.-J.2    Luo, Y.3    Kim, H.-K.4    Kim, E.-M.5    Yang, J.-S.6    Song, D.-S.7    Kang, B.-K.8    Lee, C.-S.9    Park, B.-K.10
  • 11
    • 84862811004 scopus 로고
    • Adaption of porcine epidemic diarrhea virus to growth in cell cultures and efficacy of the killed virus vaccine
    • M. Siqi, W. Ming, Z. Jinfa, and F. Li Adaption of porcine epidemic diarrhea virus to growth in cell cultures and efficacy of the killed virus vaccine Chin. J. Prev. Vet. Med. 75 1994 15 19
    • (1994) Chin. J. Prev. Vet. Med. , vol.75 , pp. 15-19
    • Siqi, M.1    Ming, W.2    Jinfa, Z.3    Li, F.4
  • 12
    • 0023738041 scopus 로고
    • Propagation of the virus of porcine epidemic diarrhea in cell culture
    • M. Hofmann, and R. Wyler Propagation of the virus of porcine epidemic diarrhea in cell culture J. Clin. Microbiol. 26 1988 2235 2239
    • (1988) J. Clin. Microbiol. , vol.26 , pp. 2235-2239
    • Hofmann, M.1    Wyler, R.2
  • 14
  • 17
    • 33847033738 scopus 로고    scopus 로고
    • Inhibition of SARS-CoV replication cycle by small interference RNAs silencing specific SARS proteins, 7a/7b, 3a/3b and S
    • S. Akerstrom, A. Mirazimi, and Y.J. Tan Inhibition of SARS-CoV replication cycle by small interference RNAs silencing specific SARS proteins, 7a/7b, 3a/3b and S Antiviral Res. 73 2007 219 227
    • (2007) Antiviral Res. , vol.73 , pp. 219-227
    • Akerstrom, S.1    Mirazimi, A.2    Tan, Y.J.3
  • 18
    • 0028884078 scopus 로고
    • PEDV leader sequence and junction sites
    • K. Tobler, and M. Ackermann PEDV leader sequence and junction sites Adv. Exp. Med. Biol. 380 1995 541 542
    • (1995) Adv. Exp. Med. Biol. , vol.380 , pp. 541-542
    • Tobler, K.1    Ackermann, M.2
  • 20
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane α-helices in prokaryotic membrane proteins: The dense alignment surface method
    • M. Cserzo, E. Wallin, I. Simon, G. von Heijne, and A. Elofsson Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method Protein Eng. 10 1997 673 676 (Pubitemid 27332074)
    • (1997) Protein Engineering , vol.10 , Issue.6 , pp. 673-676
    • Cserzo, M.1    Wallin, E.2    Simon, I.3    Von Heijne, G.4    Elofsson, A.5
  • 22
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning proteins segments
    • K. Hofmann, and W. Stoffel TMbase - a database of membrane spanning proteins segments Biol. Chem. Hoppe-Seyler 347 1993 166
    • (1993) Biol. Chem. Hoppe-Seyler , vol.347 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 23
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. hydrophobicity analysis and the positive-inside rule
    • G. von Heijne Membrane protein structure prediction. hydrophobicity analysis and the positive-inside rule J. Mol. Biol. 225 1992 487 494
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 24
    • 78650280529 scopus 로고    scopus 로고
    • Viral channel forming proteins - Modeling the target
    • W.B. Fischer, and H.J. Hsu Viral channel forming proteins - modeling the target Biochim. Biophys. Acta. 1808 2011 561 571
    • (2011) Biochim. Biophys. Acta. , vol.1808 , pp. 561-571
    • Fischer, W.B.1    Hsu, H.J.2
  • 25
    • 78650261371 scopus 로고    scopus 로고
    • Viral proteins function as ion channels
    • K. Wang, S. Xie, and B. Sun Viral proteins function as ion channels Biochim. Biophys. Acta. 1808 2011 510 515
    • (2011) Biochim. Biophys. Acta. , vol.1808 , pp. 510-515
    • Wang, K.1    Xie, S.2    Sun, B.3
  • 26
    • 0041333863 scopus 로고    scopus 로고
    • Viroporins
    • DOI 10.1016/S0014-5793(03)00780-4
    • M.E. Gonzalez, and L. Carrasco Viroporins FEBS Lett. 552 2003 28 34 (Pubitemid 37103005)
    • (2003) FEBS Letters , vol.552 , Issue.1 , pp. 28-34
    • Gonzalez, M.E.1    Carrasco, L.2
  • 27
    • 38049161643 scopus 로고    scopus 로고
    • Viroporins from RNA viruses induce caspase-dependent apoptosis
    • V. Madan, A. Castello, and L. Carrasco Viroporins from RNA viruses induce caspase-dependent apoptosis Cell Microbiol. 10 2008 437 451
    • (2008) Cell Microbiol. , vol.10 , pp. 437-451
    • Madan, V.1    Castello, A.2    Carrasco, L.3
  • 28
    • 21244447668 scopus 로고    scopus 로고
    • Viroporin activity of murine hepatitis virus E protein
    • DOI 10.1016/j.febslet.2005.05.046, PII S001457930500654X
    • V. Madan, J. Garcia Mde, M.A. Sanz, and L. Carrasco Viroporin activity of murine hepatitis virus E protein FEBS Lett. 579 2005 3607 3612 (Pubitemid 40897699)
    • (2005) FEBS Letters , vol.579 , Issue.17 , pp. 3607-3612
    • Madan, V.1    Garcia, M.D.J.2    Sanz, M.A.3    Carrasco, L.4
  • 29
    • 33646746935 scopus 로고    scopus 로고
    • Biochemical and functional characterization of the membrane association and membrane permeabilizing activity of the severe acute respiratory syndrome coronavirus envelope protein
    • DOI 10.1016/j.virol.2006.01.028, PII S0042682206000560
    • Y. Liao, Q. Yuan, J. Torres, J.P. Tam, and D.X. Liu Biochemical and functional characterization of the membrane association and membrane permeabilizing activity of the severe acute respiratory syndrome coronavirus envelope protein Virology 349 2006 264 275 (Pubitemid 43796240)
    • (2006) Virology , vol.349 , Issue.2 , pp. 264-275
    • Liao, Y.1    Yuan, Q.2    Torres, J.3    Tam, J.P.4    Liu, D.X.5
  • 30
    • 7444244373 scopus 로고    scopus 로고
    • Expression of SARS-coronavirus envelope protein in Escherichia coli cells alters membrane permeability
    • DOI 10.1016/j.bbrc.2004.10.050, PII S0006291X04022958
    • Y. Liao, J. Lescar, J.P. Tam, and D.X. Liu Expression of SARS-coronavirus envelope protein in Escherichia coli cells alters membrane permeability Biochem. Biophys. Res. Commun. 325 2004 374 380 (Pubitemid 39441202)
    • (2004) Biochemical and Biophysical Research Communications , vol.325 , Issue.1 , pp. 374-380
    • Liao, Y.1    Lescar, J.2    Tam, J.P.3    Liu, D.X.4
  • 31
    • 7444229230 scopus 로고    scopus 로고
    • SARS coronavirus E protein forms cation-selective ion channels
    • DOI 10.1016/j.virol.2004.09.033, PII S0042682204006440
    • L. Wilson, C. McKinlay, P. Gage, and G. Ewart SARS coronavirus E protein forms cation-selective ion channels Virology 330 2004 322 331 (Pubitemid 39446589)
    • (2004) Virology , vol.330 , Issue.1 , pp. 322-331
    • Wilson, L.1    Mckinlay, C.2    Gage, P.3    Ewart, G.4
  • 32
    • 33748714028 scopus 로고    scopus 로고
    • Hexamethylene amiloride blocks E protein ion channels and inhibits coronavirus replication
    • DOI 10.1016/j.virol.2006.05.028, PII S004268220600359X
    • L. Wilson, P. Gage, and G. Ewart Hexamethylene amiloride blocks E protein ion channels and inhibits coronavirus replication Virology 353 2006 294 306 (Pubitemid 44397131)
    • (2006) Virology , vol.353 , Issue.2 , pp. 294-306
    • Wilson, L.1    Gage, P.2    Ewart, G.3
  • 33
    • 33947419673 scopus 로고    scopus 로고
    • Role of the coronavirus E viroporin protein transmembrane domain in virus assembly
    • DOI 10.1128/JVI.01472-06
    • Y. Ye, and B.G. Hogue Role of the coronavirus E viroporin protein transmembrane domain in virus assembly J. Virol. 81 2007 3597 3607 (Pubitemid 46456668)
    • (2007) Journal of Virology , vol.81 , Issue.7 , pp. 3597-3607
    • Ye, Y.1    Hogue, B.G.2
  • 34
    • 70049096788 scopus 로고    scopus 로고
    • Structure and inhibition of the SARS coronavirus envelope protein ion channel
    • K. Pervushin Structure and inhibition of the SARS coronavirus envelope protein ion channel PLoS Pathog. 5 2009 e1000511
    • (2009) PLoS Pathog. , vol.5 , pp. 1000511
    • Pervushin, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.