메뉴 건너뛰기




Volumn 15, Issue 11, 2015, Pages 1819-1828

Proteome analysis of porcine epidemic diarrhea virus (PEDV)-infected Vero cells

Author keywords

Differentially expressed proteins; ITRAQ; Microbiology; Porcine epidemic diarrhea virus (PEDV); Quantitative proteomics

Indexed keywords

ACETYL COENZYME A ACETYLTRANSFERASE; ACTIN DEPOLYMERIZING FACTOR; ADENYLATE CYCLASE; ALPHA ENOLASE; GEPHYRIN; GLYCEROPHOSPHOINOSITOL INOSITOLPHOSPHODIESTERASE; HEPATOMA DERIVED GROWTH FACTOR; HIGH MOBILITY GROUP PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 3; NEURON SPECIFIC ENOLASE; PHOSPHOPROTEIN PHOSPHATASE 1; PROSTAGLANDIN E SYNTHASE; PROTEIN 14 3 3; SMALL NUCLEAR RIBONUCLEOPROTEIN; TUBULIN; PROTEIN; PROTEOME;

EID: 84930276335     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201400458     Document Type: Article
Times cited : (59)

References (43)
  • 1
    • 33748743162 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the N gene of porcine epidemic diarrhea virus LJB/03
    • Junwei, G., Baoxian, L., Lijie, T., Yijing, L., Cloning and sequence analysis of the N gene of porcine epidemic diarrhea virus LJB/03. Virus Genes 2006, 33, 215-219.
    • (2006) Virus Genes , vol.33 , pp. 215-219
    • Junwei, G.1    Baoxian, L.2    Lijie, T.3    Yijing, L.4
  • 2
    • 0017778863 scopus 로고
    • An apparently new syndrome of porcine epidemic diarrhoea
    • Wood, E. N., An apparently new syndrome of porcine epidemic diarrhoea. Vet. Rec. 1977, 100, 243-244.
    • (1977) Vet. Rec. , vol.100 , pp. 243-244
    • Wood, E.N.1
  • 3
    • 0018119572 scopus 로고
    • Virus-like particles associated with porcine epidemic diarrhoea
    • Chasey, D., Cartwright, S. F., Virus-like particles associated with porcine epidemic diarrhoea. Res. Vet. Sci. 1978, 25, 255-256.
    • (1978) Res. Vet. Sci. , vol.25 , pp. 255-256
    • Chasey, D.1    Cartwright, S.F.2
  • 4
    • 84864443634 scopus 로고    scopus 로고
    • New variants of porcine epidemic diarrhea virus, China, 2011
    • Li, W., Li, H., Liu, Y., Pan, Y. et al., New variants of porcine epidemic diarrhea virus, China, 2011. Emerg. Infect. Dis. 2012, 18, 1350-1353.
    • (2012) Emerg. Infect. Dis. , vol.18 , pp. 1350-1353
    • Li, W.1    Li, H.2    Liu, Y.3    Pan, Y.4
  • 5
    • 84868284310 scopus 로고    scopus 로고
    • Complete genome sequence of porcine epidemic diarrhea virus strain AJ1102 isolated from a suckling piglet with acute diarrhea in China
    • Bi, J., Zeng, S., Xiao, S., Chen, H., Fang, L., Complete genome sequence of porcine epidemic diarrhea virus strain AJ1102 isolated from a suckling piglet with acute diarrhea in China. J. Virol. 2012, 86, 10910-10911.
    • (2012) J. Virol. , vol.86 , pp. 10910-10911
    • Bi, J.1    Zeng, S.2    Xiao, S.3    Chen, H.4    Fang, L.5
  • 6
    • 84887934820 scopus 로고    scopus 로고
    • Genetic properties of endemic Chinese porcine epidemic diarrhea virus strains isolated since 2010
    • Wang, X. M., Niu, B. B., Yan, H., Gao, D. S. et al., Genetic properties of endemic Chinese porcine epidemic diarrhea virus strains isolated since 2010. Arch. Virol. 2013, 158, 2487-2494.
    • (2013) Arch. Virol. , vol.158 , pp. 2487-2494
    • Wang, X.M.1    Niu, B.B.2    Yan, H.3    Gao, D.S.4
  • 7
    • 84863270086 scopus 로고    scopus 로고
    • Complete genome sequence of a porcine epidemic diarrhea virus variant
    • Chen, J., Liu, X., Shi, D., Shi, H. et al., Complete genome sequence of a porcine epidemic diarrhea virus variant. J. Virol. 2012, 86, 3408.
    • (2012) J. Virol. , vol.86 , pp. 3408
    • Chen, J.1    Liu, X.2    Shi, D.3    Shi, H.4
  • 8
    • 84863012775 scopus 로고    scopus 로고
    • Outbreak of porcine epidemic diarrhea in suckling piglets, China
    • Sun, R. Q., Cai, R. J., Chen, Y. Q., Liang, P. S. et al., Outbreak of porcine epidemic diarrhea in suckling piglets, China. Emerg. Infect. Dis. 2012, 18, 161-163.
    • (2012) Emerg. Infect. Dis. , vol.18 , pp. 161-163
    • Sun, R.Q.1    Cai, R.J.2    Chen, Y.Q.3    Liang, P.S.4
  • 9
    • 84891513701 scopus 로고    scopus 로고
    • Isolation and characterization of porcine epidemic diarrhea viruses associated with the 2013 disease outbreak among swine in the United States
    • Chen, Q., Li, G., Stasko, J., Thomas, J. T. et al., Isolation and characterization of porcine epidemic diarrhea viruses associated with the 2013 disease outbreak among swine in the United States. J. Clin. Microbiol. 2014, 52, 234-243.
    • (2014) J. Clin. Microbiol. , vol.52 , pp. 234-243
    • Chen, Q.1    Li, G.2    Stasko, J.3    Thomas, J.T.4
  • 10
    • 84884153028 scopus 로고    scopus 로고
    • Emergence of Porcine epidemic diarrhea virus in the United States: clinical signs, lesions, and viral genomic sequences
    • Stevenson, G. W., Hoang, H., Schwartz, K. J., Burrough, E. R. et al., Emergence of Porcine epidemic diarrhea virus in the United States: clinical signs, lesions, and viral genomic sequences. J. Vet. Diagn. Invest. 2013, 25, 649-654.
    • (2013) J. Vet. Diagn. Invest. , vol.25 , pp. 649-654
    • Stevenson, G.W.1    Hoang, H.2    Schwartz, K.J.3    Burrough, E.R.4
  • 11
    • 84871829547 scopus 로고    scopus 로고
    • Epimedium koreanum Nakai water extract exhibits antiviral activity against porcine epidermic diarrhea virus in vitro and in vivo
    • Cho, W. K., Kim, H., Choi, Y. J., Yim, N. H. et al., Epimedium koreanum Nakai water extract exhibits antiviral activity against porcine epidermic diarrhea virus in vitro and in vivo. Evid. Based Complement. Alternat. Med. 2012, 2012, 985151. doi: 10.1155/2012/985151.
    • (2012) Evid. Based Complement. Alternat. Med. , vol.2012 , pp. 985151
    • Cho, W.K.1    Kim, H.2    Choi, Y.J.3    Yim, N.H.4
  • 13
    • 84859238947 scopus 로고    scopus 로고
    • Using SILAC and quantitative proteomics to investigate the interactions between viral and host proteomes
    • Munday, D. C., Surtees, R., Emmott, E., Dove, B. K. et al., Using SILAC and quantitative proteomics to investigate the interactions between viral and host proteomes. Proteomics 2012, 12, 666-672.
    • (2012) Proteomics , vol.12 , pp. 666-672
    • Munday, D.C.1    Surtees, R.2    Emmott, E.3    Dove, B.K.4
  • 14
    • 4444311436 scopus 로고    scopus 로고
    • Proteomic analysis of SARS associated coronavirus using two-dimensional liquid chromatography mass spectrometry and one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by mass spectroemtric analysis
    • Zeng, R., Ruan, H. Q., Jiang, X. S., Zhou, H. et al., Proteomic analysis of SARS associated coronavirus using two-dimensional liquid chromatography mass spectrometry and one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by mass spectroemtric analysis. J. Proteome Res. 2004, 3, 549-555.
    • (2004) J. Proteome Res. , vol.3 , pp. 549-555
    • Zeng, R.1    Ruan, H.Q.2    Jiang, X.S.3    Zhou, H.4
  • 15
    • 84901819162 scopus 로고    scopus 로고
    • Comparative proteome analysis of tracheal tissues in response to infectious bronchitis coronavirus, Newcastle disease virus, and avian influenza virus H9 subtype virus infection
    • Sun, J., Han, Z., Shao, Y., Cao, Z. et al., Comparative proteome analysis of tracheal tissues in response to infectious bronchitis coronavirus, Newcastle disease virus, and avian influenza virus H9 subtype virus infection. Proteomics 2014, 14, 1403-1423.
    • (2014) Proteomics , vol.14 , pp. 1403-1423
    • Sun, J.1    Han, Z.2    Shao, Y.3    Cao, Z.4
  • 16
    • 84880088942 scopus 로고    scopus 로고
    • Identification of cellular proteome using two-dimensional difference gel electrophoresis in ST cells infected with transmissible gastroenteritis coronavirus
    • Zhang, X., Shi, H. Y., Chen, J. F., Shi, D. et al., Identification of cellular proteome using two-dimensional difference gel electrophoresis in ST cells infected with transmissible gastroenteritis coronavirus. Proteome Sci. 2013, 11, 31.
    • (2013) Proteome Sci. , vol.11 , pp. 31
    • Zhang, X.1    Shi, H.Y.2    Chen, J.F.3    Shi, D.4
  • 17
    • 33750333638 scopus 로고    scopus 로고
    • Biochemical aspects of coronavirus replication and virus-host interaction
    • Enjuanes, L., Almazan, F., Sola, I., Zuniga, S., Biochemical aspects of coronavirus replication and virus-host interaction. Annu. Rev. Microbiol. 2006, 60, 211-230.
    • (2006) Annu. Rev. Microbiol. , vol.60 , pp. 211-230
    • Enjuanes, L.1    Almazan, F.2    Sola, I.3    Zuniga, S.4
  • 18
    • 0023738041 scopus 로고
    • Propagation of the virus of porcine epidemic diarrhea in cell culture
    • Hofmann, M., Wyler, R., Propagation of the virus of porcine epidemic diarrhea in cell culture. J. Clin. Microbiol. 1988, 26, 2235-2239.
    • (1988) J. Clin. Microbiol. , vol.26 , pp. 2235-2239
    • Hofmann, M.1    Wyler, R.2
  • 19
    • 84864815807 scopus 로고    scopus 로고
    • Enhanced peptide identification by electron transfer dissociation using an improved Mascot Percolator
    • Wright, J. C., Collins, M. O., Yu, L., Kall, L. et al., Enhanced peptide identification by electron transfer dissociation using an improved Mascot Percolator. Mol. Cell. Proteomics 2012, 11, 478-491.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 478-491
    • Wright, J.C.1    Collins, M.O.2    Yu, L.3    Kall, L.4
  • 20
    • 27644555055 scopus 로고    scopus 로고
    • Interpretation of shotgun proteomic data: the protein inference problem
    • Nesvizhskii, A. I., Aebersold, R., Interpretation of shotgun proteomic data: the protein inference problem. Mol. Cell. Proteomics 2005, 4, 1419-1440.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1419-1440
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 21
    • 70449381259 scopus 로고    scopus 로고
    • Differential proteome analysis of host cells infected with porcine circovirus type 2
    • Zhang, X., Zhou, J., Wu, Y., Zheng, X. et al., Differential proteome analysis of host cells infected with porcine circovirus type 2. J. Proteome Res. 2009, 8, 5111-5119.
    • (2009) J. Proteome Res. , vol.8 , pp. 5111-5119
    • Zhang, X.1    Zhou, J.2    Wu, Y.3    Zheng, X.4
  • 22
    • 77949503809 scopus 로고    scopus 로고
    • Classical swine fever virus infection protects aortic endothelial cells from pIpC-mediated apoptosis
    • Johns, H. L., Bensaude, E., LaRocca, S. A., Seago, J. et al., Classical swine fever virus infection protects aortic endothelial cells from pIpC-mediated apoptosis. J. Gen. Virol. 2010, 91, 1038-1046.
    • (2010) J. Gen. Virol. , vol.91 , pp. 1038-1046
    • Johns, H.L.1    Bensaude, E.2    La Rocca, S.A.3    Seago, J.4
  • 23
    • 0034788964 scopus 로고    scopus 로고
    • 14-3-3 proteins: key regulators of cell division, signalling and apoptosis
    • vanHemert, M. J., Steensma, H. Y., vanHeusden, G. P., 14-3-3 proteins: key regulators of cell division, signalling and apoptosis. Bioessays 2001, 23, 936-946.
    • (2001) Bioessays , vol.23 , pp. 936-946
    • van Hemert, M.J.1    Steensma, H.Y.2    van Heusden, G.P.3
  • 24
    • 0034141550 scopus 로고    scopus 로고
    • 14-3-3 proteins block apoptosis and differentially regulate MAPK cascades
    • Xing, H., Zhang, S., Weinheimer, C., Kovacs, A., Muslin, A. J., 14-3-3 proteins block apoptosis and differentially regulate MAPK cascades. EMBO J. 2000, 19, 349-358.
    • (2000) EMBO J. , vol.19 , pp. 349-358
    • Xing, H.1    Zhang, S.2    Weinheimer, C.3    Kovacs, A.4    Muslin, A.J.5
  • 25
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: the executioners of apoptosis
    • Cohen, G. M., Caspases: the executioners of apoptosis. Biochem. J. 1997, 326(Pt 1), 1-16.
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 26
    • 77955078843 scopus 로고    scopus 로고
    • Comparative host gene transcription by microarray analysis early after infection of the Huh7 cell line by SARS coronavirus and human coronavirus 229E
    • Tang, B. S., Chan, K. H., Cheng, V. C., Yuen, K. Y., Comparative host gene transcription by microarray analysis early after infection of the Huh7 cell line by SARS coronavirus and human coronavirus 229E. Hong Kong Med. J. 2009, 15(Suppl 9), 23-26.
    • (2009) Hong Kong Med. J. , vol.15 , pp. 23-26
    • Tang, B.S.1    Chan, K.H.2    Cheng, V.C.3    Yuen, K.Y.4
  • 27
    • 17844368327 scopus 로고    scopus 로고
    • The MAPK signalling pathways and colorectal cancer
    • Fang, J. Y., Richardson, B. C., The MAPK signalling pathways and colorectal cancer. Lancet Oncol. 2005, 6, 322-327.
    • (2005) Lancet Oncol. , vol.6 , pp. 322-327
    • Fang, J.Y.1    Richardson, B.C.2
  • 28
    • 27344446874 scopus 로고    scopus 로고
    • Phosphorylation of PI3K/Akt and MAPK/ERK in an early entry step of enterovirus 71
    • Wong, W. R., Chen, Y. Y., Yang, S. M., Chen, Y. L., Horng, J. T., Phosphorylation of PI3K/Akt and MAPK/ERK in an early entry step of enterovirus 71. Life Sci. 2005, 78, 82-90.
    • (2005) Life Sci. , vol.78 , pp. 82-90
    • Wong, W.R.1    Chen, Y.Y.2    Yang, S.M.3    Chen, Y.L.4    Horng, J.T.5
  • 29
    • 77955275486 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus replication is suppressed by inhibition of the extracellular signal-regulated kinase (ERK) signaling pathway
    • Lee, Y. J., Lee, C., Porcine reproductive and respiratory syndrome virus replication is suppressed by inhibition of the extracellular signal-regulated kinase (ERK) signaling pathway. Virus Res. 2010, 152, 50-58.
    • (2010) Virus Res. , vol.152 , pp. 50-58
    • Lee, Y.J.1    Lee, C.2
  • 30
    • 33846557891 scopus 로고    scopus 로고
    • The ERK mitogen-activated protein kinase pathway contributes to Ebola virus glycoprotein-induced cytotoxicity
    • Zampieri, C. A., Fortin, J. F., Nolan, G. P., Nabel, G. J., The ERK mitogen-activated protein kinase pathway contributes to Ebola virus glycoprotein-induced cytotoxicity. J. Virol. 2007, 81, 1230-1240.
    • (2007) J. Virol. , vol.81 , pp. 1230-1240
    • Zampieri, C.A.1    Fortin, J.F.2    Nolan, G.P.3    Nabel, G.J.4
  • 31
    • 23844480660 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr-dependent cell cycle arrest through a mitogen-activated protein kinase signal transduction pathway
    • Yoshizuka, N., Yoshizuka-Chadani, Y., Krishnan, V., Zeichner, S. L., Human immunodeficiency virus type 1 Vpr-dependent cell cycle arrest through a mitogen-activated protein kinase signal transduction pathway. J. Virol. 2005, 79, 11366-11381.
    • (2005) J. Virol. , vol.79 , pp. 11366-11381
    • Yoshizuka, N.1    Yoshizuka-Chadani, Y.2    Krishnan, V.3    Zeichner, S.L.4
  • 32
    • 6344233443 scopus 로고    scopus 로고
    • The SARS coronavirus nucleocapsid protein induces actin reorganization and apoptosis in COS-1 cells in the absence of growth factors
    • Surjit, M., Liu, B., Jameel, S., Chow, V. T., Lal, S. K., The SARS coronavirus nucleocapsid protein induces actin reorganization and apoptosis in COS-1 cells in the absence of growth factors. Biochem. J. 2004, 383, 13-18.
    • (2004) Biochem. J. , vol.383 , pp. 13-18
    • Surjit, M.1    Liu, B.2    Jameel, S.3    Chow, V.T.4    Lal, S.K.5
  • 33
    • 33846085104 scopus 로고    scopus 로고
    • Suppression of coronavirus replication by inhibition of the MEK signaling pathway
    • Cai, Y., Liu, Y., Zhang, X., Suppression of coronavirus replication by inhibition of the MEK signaling pathway. J. Virol. 2007, 81, 446-456.
    • (2007) J. Virol. , vol.81 , pp. 446-456
    • Cai, Y.1    Liu, Y.2    Zhang, X.3
  • 34
    • 47749125033 scopus 로고    scopus 로고
    • Suppression of astrovirus replication by an ERK1/2 inhibitor
    • Moser, L. A., Schultz-Cherry, S., Suppression of astrovirus replication by an ERK1/2 inhibitor. J. Virol. 2008, 82, 7475-7482.
    • (2008) J. Virol. , vol.82 , pp. 7475-7482
    • Moser, L.A.1    Schultz-Cherry, S.2
  • 35
    • 0034648790 scopus 로고    scopus 로고
    • Activation of heat-shock response by an adenovirus is essential for virus replication
    • Glotzer, J. B., Saltik, M., Chiocca, S., Michou, A. I. et al., Activation of heat-shock response by an adenovirus is essential for virus replication. Nature 2000, 407, 207-211.
    • (2000) Nature , vol.407 , pp. 207-211
    • Glotzer, J.B.1    Saltik, M.2    Chiocca, S.3    Michou, A.I.4
  • 36
    • 84865170479 scopus 로고    scopus 로고
    • Heat shock protein 27 (HSP27): biomarker of disease and therapeutic target
    • Vidyasagar, A., Wilson, N. A., Djamali, A., Heat shock protein 27 (HSP27): biomarker of disease and therapeutic target. Fibrogenesis Tissue Repair 2012, 5, 7.
    • (2012) Fibrogenesis Tissue Repair , vol.5 , pp. 7
    • Vidyasagar, A.1    Wilson, N.A.2    Djamali, A.3
  • 38
    • 33644863314 scopus 로고    scopus 로고
    • Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection
    • Leong, W. F., Chow, V. T., Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell Microbiol. 2006, 8, 565-580.
    • (2006) Cell Microbiol. , vol.8 , pp. 565-580
    • Leong, W.F.1    Chow, V.T.2
  • 39
    • 41549087403 scopus 로고    scopus 로고
    • Proteomics analysis of host cells infected with infectious bursal disease virus
    • Zheng, X., Hong, L., Shi, L., Guo, J. et al., Proteomics analysis of host cells infected with infectious bursal disease virus. Mol. Cell. Proteomics 2008, 7, 612-625.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 612-625
    • Zheng, X.1    Hong, L.2    Shi, L.3    Guo, J.4
  • 40
    • 33748302761 scopus 로고    scopus 로고
    • Mass spectrometry reveals specific and global molecular transformations during viral infection
    • Go, E. P., Wikoff, W. R., Shen, Z., O'Maille, G. et al., Mass spectrometry reveals specific and global molecular transformations during viral infection. J. Proteome Res. 2006, 5, 2405-2416.
    • (2006) J. Proteome Res. , vol.5 , pp. 2405-2416
    • Go, E.P.1    Wikoff, W.R.2    Shen, Z.3    O'Maille, G.4
  • 41
    • 0024324330 scopus 로고
    • The expression of heat shock protein hsp27 and a complexed 22-kilodalton protein is inversely correlated with oncogenicity of adenovirus-transformed cells
    • Zantema, A., deJong, E., Lardenoije, R., vander Eb, A. J., The expression of heat shock protein hsp27 and a complexed 22-kilodalton protein is inversely correlated with oncogenicity of adenovirus-transformed cells. J. Virol. 1989, 63, 3368-3375.
    • (1989) J. Virol. , vol.63 , pp. 3368-3375
    • Zantema, A.1    de Jong, E.2    Lardenoije, R.3    van der Eb, A.J.4
  • 42
    • 61349162384 scopus 로고    scopus 로고
    • Proteomic alteration of PK-15 cells after infection by classical swine fever virus
    • Sun, J., Jiang, Y., Shi, Z., Yan, Y. et al., Proteomic alteration of PK-15 cells after infection by classical swine fever virus. J. Proteome Res. 2008, 7, 5263-5269.
    • (2008) J. Proteome Res. , vol.7 , pp. 5263-5269
    • Sun, J.1    Jiang, Y.2    Shi, Z.3    Yan, Y.4
  • 43
    • 84869479551 scopus 로고    scopus 로고
    • HSPB1 is an intracellular antiviral factor against hepatitis B virus
    • Tong, S. W., Yang, Y. X., Hu, H. D., An, X. et al., HSPB1 is an intracellular antiviral factor against hepatitis B virus. J. Cell Biochem. 2013, 114, 162-173.
    • (2013) J. Cell Biochem. , vol.114 , pp. 162-173
    • Tong, S.W.1    Yang, Y.X.2    Hu, H.D.3    An, X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.