메뉴 건너뛰기




Volumn 509, Issue , 2017, Pages 222-231

Foot-and-mouth disease virus induces lysosomal degradation of host protein kinase PKR by 3C proteinase to facilitate virus replication

Author keywords

3Cpro; Foot and mouth disease virus; Lysosomes; PKR

Indexed keywords

3C PROTEINASE; INITIATION FACTOR 4G; PROTEIN KINASE R; UNCLASSIFIED DRUG; VIRAL PROTEIN; 3C PROTEASES; CYSTEINE PROTEINASE;

EID: 85021098349     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2017.06.023     Document Type: Article
Times cited : (41)

References (44)
  • 3
    • 0033988512 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
    • Belsham, G.J., McInerney, G.M., Ross-Smith, N., Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells. J. Virol. 74 (2000), 272–280.
    • (2000) J. Virol. , vol.74 , pp. 272-280
    • Belsham, G.J.1    McInerney, G.M.2    Ross-Smith, N.3
  • 6
    • 0024593159 scopus 로고
    • The cellular 68,000-Mr protein kinase is highly autophosphorylated and activated yet significantly degraded during poliovirus infection: implications for translational regulation
    • Black, T.L., Safer, B., Hovanessian, A., Katze, M.G., The cellular 68,000-Mr protein kinase is highly autophosphorylated and activated yet significantly degraded during poliovirus infection: implications for translational regulation. J. Virol. 63 (1989), 2244–2251.
    • (1989) J. Virol. , vol.63 , pp. 2244-2251
    • Black, T.L.1    Safer, B.2    Hovanessian, A.3    Katze, M.G.4
  • 7
    • 0035010933 scopus 로고    scopus 로고
    • Inhibition of L-deleted foot-and-mouth disease virus replication by alpha/beta interferon involves double-stranded RNA-dependent protein kinase
    • Chinsangaram, J., Koster, M., Grubman, M.J., Inhibition of L-deleted foot-and-mouth disease virus replication by alpha/beta interferon involves double-stranded RNA-dependent protein kinase. J. Virol. 75 (2001), 5498–5503.
    • (2001) J. Virol. , vol.75 , pp. 5498-5503
    • Chinsangaram, J.1    Koster, M.2    Grubman, M.J.3
  • 8
    • 33749649170 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus 3C protease: recent structural and functional insights into an antiviral target
    • Curry, S., Roqué-Rosell, N., Zunszain, P.A., Leatherbarrow, R.J., Foot-and-mouth disease virus 3C protease: recent structural and functional insights into an antiviral target. Int. J. Biochem. Cell Biol. 39 (2007), 1–6.
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1-6
    • Curry, S.1    Roqué-Rosell, N.2    Zunszain, P.A.3    Leatherbarrow, R.J.4
  • 9
    • 84870623251 scopus 로고    scopus 로고
    • dsRNA-dependent protein kinase PKR and its role in stress, signaling and HCV infection
    • Dabo, S., Meurs, E.F., dsRNA-dependent protein kinase PKR and its role in stress, signaling and HCV infection. Virus.-Basel 4 (2012), 2598–2635.
    • (2012) Virus.-Basel , vol.4 , pp. 2598-2635
    • Dabo, S.1    Meurs, E.F.2
  • 12
    • 0025223793 scopus 로고
    • Modified subcellular localization of interferon-induced p68 kinase during encephalomyocarditis virus infection
    • Dubois, M.F., Hovanessian, A.G., Modified subcellular localization of interferon-induced p68 kinase during encephalomyocarditis virus infection. Virology 179 (1990), 591–598.
    • (1990) Virology , vol.179 , pp. 591-598
    • Dubois, M.F.1    Hovanessian, A.G.2
  • 15
    • 34347225099 scopus 로고    scopus 로고
    • The dsRNA protein kinase PKR: virus and cell control
    • Garcia, M.A., Meurs, E.F., Esteban, M., The dsRNA protein kinase PKR: virus and cell control. Biochimie 89 (2007), 799–811.
    • (2007) Biochimie , vol.89 , pp. 799-811
    • Garcia, M.A.1    Meurs, E.F.2    Esteban, M.3
  • 17
    • 0028802290 scopus 로고
    • Identification of the active-site residues of the 3c proteinase of foot-and-mouth-disease virus
    • Grubman, M.J., Zellner, M., Bablanian, G., Mason, P.W., Piccone, M.E., Identification of the active-site residues of the 3c proteinase of foot-and-mouth-disease virus. Virology 213 (1995), 581–589.
    • (1995) Virology , vol.213 , pp. 581-589
    • Grubman, M.J.1    Zellner, M.2    Bablanian, G.3    Mason, P.W.4    Piccone, M.E.5
  • 18
  • 19
    • 84889032990 scopus 로고    scopus 로고
    • Foot-and-mouth disease: past, present and future
    • Jamal, S.M., Belsham, G.J., Foot-and-mouth disease: past, present and future. Vet. Res., 44, 2013, 116.
    • (2013) Vet. Res. , vol.44 , pp. 116
    • Jamal, S.M.1    Belsham, G.J.2
  • 21
    • 10644276047 scopus 로고    scopus 로고
    • Global epidemiology and prospects for control of foot-and-mouth disease
    • Kitching, R.P., Global epidemiology and prospects for control of foot-and-mouth disease. Curr. Top. Microbiol. Immunol. 288 (2005), 133–148.
    • (2005) Curr. Top. Microbiol. Immunol. , vol.288 , pp. 133-148
    • Kitching, R.P.1
  • 23
    • 84856575654 scopus 로고    scopus 로고
    • The nuclear protein Sam68 is cleaved by the FMDV 3C protease redistributing Sam68 to the cytoplasm during FMDV infection of host cells
    • Lawrence, P., Schafer, E.A., Rieder, E., The nuclear protein Sam68 is cleaved by the FMDV 3C protease redistributing Sam68 to the cytoplasm during FMDV infection of host cells. Virology 425 (2012), 40–52.
    • (2012) Virology , vol.425 , pp. 40-52
    • Lawrence, P.1    Schafer, E.A.2    Rieder, E.3
  • 24
    • 84966393533 scopus 로고    scopus 로고
    • The VP3 structural protein of foot-and-mouth disease virus inhibits the IFN-β signaling pathway
    • (fj. 15-281410)
    • Li, D., Yang, W., Yang, F., Liu, H., Zhu, Z., Lian, K., Lei, C., Li, S., Liu, X., Zheng, H., The VP3 structural protein of foot-and-mouth disease virus inhibits the IFN-β signaling pathway. FASEB J., 2016 (fj. 15-281410).
    • (2016) FASEB J.
    • Li, D.1    Yang, W.2    Yang, F.3    Liu, H.4    Zhu, Z.5    Lian, K.6    Lei, C.7    Li, S.8    Liu, X.9    Zheng, H.10
  • 25
    • 33646517711 scopus 로고    scopus 로고
    • Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA
    • Li, S., Min, J.-Y., Krug, R.M., Sen, G.C., Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA. Virology 349 (2006), 13–21.
    • (2006) Virology , vol.349 , pp. 13-21
    • Li, S.1    Min, J.-Y.2    Krug, R.M.3    Sen, G.C.4
  • 26
    • 84979300806 scopus 로고    scopus 로고
    • Esterase D enhances type I interferon signal transduction to suppress foot-and-mouth disease virus replication
    • Li, W., Zhu, Z., Cao, W., Yang, F., Zhang, X., Li, D., Zhang, K., Li, P., Mao, R., Liu, X., Zheng, H., Esterase D enhances type I interferon signal transduction to suppress foot-and-mouth disease virus replication. Mol. Immunol. 75 (2016), 112–121.
    • (2016) Mol. Immunol. , vol.75 , pp. 112-121
    • Li, W.1    Zhu, Z.2    Cao, W.3    Yang, F.4    Zhang, X.5    Li, D.6    Zhang, K.7    Li, P.8    Mao, R.9    Liu, X.10    Zheng, H.11
  • 27
    • 84945295942 scopus 로고    scopus 로고
    • Multifunctional roles of leader protein of foot-and-mouth disease viruses in suppressing host antiviral responses
    • Liu, Y., Zhu, Z., Zhang, M., Zheng, H., Multifunctional roles of leader protein of foot-and-mouth disease viruses in suppressing host antiviral responses. Vet. Res., 46, 2015, 127.
    • (2015) Vet. Res. , vol.46 , pp. 127
    • Liu, Y.1    Zhu, Z.2    Zhang, M.3    Zheng, H.4
  • 28
    • 0028847292 scopus 로고
    • Binding of the Influenza-Virus Ns1 Protein to Double-Stranded-Rna Inhibits the Activation of the Protein-Kinase That Phosphorylates the Elf-2 Translation Initiation-Factor
    • Lu, Y., Wambach, M., Katze, M.G., Krug, R.M., Binding of the Influenza-Virus Ns1 Protein to Double-Stranded-Rna Inhibits the Activation of the Protein-Kinase That Phosphorylates the Elf-2 Translation Initiation-Factor. Virology 214 (1995), 222–228.
    • (1995) Virology , vol.214 , pp. 222-228
    • Lu, Y.1    Wambach, M.2    Katze, M.G.3    Krug, R.M.4
  • 29
    • 84874210142 scopus 로고    scopus 로고
    • The herpes simplex virus 1 Us11 protein inhibits autophagy through its interaction with the protein kinase PKR
    • Lussignol, M., Queval, C., Bernet-Camard, M.F., Cotte-Laffitte, J., Beau, I., Codogno, P., Esclatine, A., The herpes simplex virus 1 Us11 protein inhibits autophagy through its interaction with the protein kinase PKR. J. Virol. 87 (2013), 859–871.
    • (2013) J. Virol. , vol.87 , pp. 859-871
    • Lussignol, M.1    Queval, C.2    Bernet-Camard, M.F.3    Cotte-Laffitte, J.4    Beau, I.5    Codogno, P.6    Esclatine, A.7
  • 30
    • 75749108288 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis
    • Nakamura, T., Furuhashi, M., Li, P., Cao, H.M., Tuncman, G., Sonenberg, N., Gorgun, C.Z., Hotamisligil, G.S., Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis. Cell 140 (2010), 338–U341.
    • (2010) Cell , vol.140 , pp. 338-U341
    • Nakamura, T.1    Furuhashi, M.2    Li, P.3    Cao, H.M.4    Tuncman, G.5    Sonenberg, N.6    Gorgun, C.Z.7    Hotamisligil, G.S.8
  • 31
    • 79551687500 scopus 로고    scopus 로고
    • Regulation of innate immunity through RNA structure and the protein kinase PKR
    • Nallagatla, S.R., Toroney, R., Bevilacqua, P.C., Regulation of innate immunity through RNA structure and the protein kinase PKR. Curr. Opin. Struct. Biol. 21 (2011), 119–127.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 119-127
    • Nallagatla, S.R.1    Toroney, R.2    Bevilacqua, P.C.3
  • 33
    • 84907466617 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus leader proteinase: structural insights into the mechanism of intermolecular cleavage
    • Steinberger, J., Grishkovskaya, I., Cencic, R., Juliano, L., Juliano, M.A., Skern, T., Foot-and-mouth disease virus leader proteinase: structural insights into the mechanism of intermolecular cleavage. Virology 468–470 (2014), 397–408.
    • (2014) Virology , vol.468-470 , pp. 397-408
    • Steinberger, J.1    Grishkovskaya, I.2    Cencic, R.3    Juliano, L.4    Juliano, M.A.5    Skern, T.6
  • 34
    • 84926474776 scopus 로고    scopus 로고
    • The leader proteinase of foot-and-mouth disease virus: structure-function relationships in a proteolytic virulence factor
    • Steinberger, J., Skern, T., The leader proteinase of foot-and-mouth disease virus: structure-function relationships in a proteolytic virulence factor. Biol. Chem. 395 (2014), 1179–1185.
    • (2014) Biol. Chem. , vol.395 , pp. 1179-1185
    • Steinberger, J.1    Skern, T.2
  • 36
    • 33845759346 scopus 로고    scopus 로고
    • Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease reveals the role of the beta-ribbon in proteolysis
    • Sweeney, T.R., Roque-Rosell, N., Birtley, J.R., Leatherbarrow, R.J., Curry, S., Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease reveals the role of the beta-ribbon in proteolysis. J. Virol. 81 (2007), 115–124.
    • (2007) J. Virol. , vol.81 , pp. 115-124
    • Sweeney, T.R.1    Roque-Rosell, N.2    Birtley, J.R.3    Leatherbarrow, R.J.4    Curry, S.5
  • 37
    • 0031897318 scopus 로고    scopus 로고
    • Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor
    • Tan, S.-L., Gale, M.J., Katze, M.G., Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor. Mol. Cell. Biol. 18 (1998), 2431–2443.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2431-2443
    • Tan, S.-L.1    Gale, M.J.2    Katze, M.G.3
  • 38
    • 0038719944 scopus 로고    scopus 로고
    • Inhibition of the protein kinase PKR by the internal ribosome entry site of hepatitis C virus genomic RNA
    • Vyas, J., Elia, A., Clemens, M.J., Inhibition of the protein kinase PKR by the internal ribosome entry site of hepatitis C virus genomic RNA. Rna-a Publ. Rna Soc. 9 (2003), 858–870.
    • (2003) Rna-a Publ. Rna Soc. , vol.9 , pp. 858-870
    • Vyas, J.1    Elia, A.2    Clemens, M.J.3
  • 40
    • 84903888416 scopus 로고    scopus 로고
    • Influenza A Virus-Induced Degradation of Eukaryotic Translation Initiation Factor 4B Contributes to Viral Replication by Suppressing IFITM3 Protein Expression
    • Wang, S., Chi, X.J., Wei, H.T., Chen, Y.H., Chen, Z.L., Huang, S.L., Chen, J.L., Influenza A Virus-Induced Degradation of Eukaryotic Translation Initiation Factor 4B Contributes to Viral Replication by Suppressing IFITM3 Protein Expression. J. Virol. 88 (2014), 8375–8385.
    • (2014) J. Virol. , vol.88 , pp. 8375-8385
    • Wang, S.1    Chi, X.J.2    Wei, H.T.3    Chen, Y.H.4    Chen, Z.L.5    Huang, S.L.6    Chen, J.L.7
  • 41
    • 84861565298 scopus 로고    scopus 로고
    • Stabilization of p53 in Influenza A Virus-infected Cells Is Associated with Compromised MDM2-mediated Ubiquitination of p53
    • Wang, X.D., Deng, X.F., Yan, W.J., Zhu, Z.X., Shen, Y., Qiu, Y.F., Shi, Z.X., Shao, D.H., Wei, J.C., Xia, X.Z., Ma, Z.Y., Stabilization of p53 in Influenza A Virus-infected Cells Is Associated with Compromised MDM2-mediated Ubiquitination of p53. J. Biol. Chem. 287 (2012), 18366–18375.
    • (2012) J. Biol. Chem. , vol.287 , pp. 18366-18375
    • Wang, X.D.1    Deng, X.F.2    Yan, W.J.3    Zhu, Z.X.4    Shen, Y.5    Qiu, Y.F.6    Shi, Z.X.7    Shao, D.H.8    Wei, J.C.9    Xia, X.Z.10    Ma, Z.Y.11
  • 42
    • 84960387555 scopus 로고    scopus 로고
    • Downregulation of protein kinase PKR activation by porcine reproductive and respiratory syndrome virus at its early stage infection
    • Xiao, Y.Q., Ma, Z.X., Wang, R., Yang, L.P., Nan, Y.C., Zhang, Y.J., Downregulation of protein kinase PKR activation by porcine reproductive and respiratory syndrome virus at its early stage infection. Vet. Microbiol. 187 (2016), 1–7.
    • (2016) Vet. Microbiol. , vol.187 , pp. 1-7
    • Xiao, Y.Q.1    Ma, Z.X.2    Wang, R.3    Yang, L.P.4    Nan, Y.C.5    Zhang, Y.J.6
  • 43
    • 85000925772 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus viroporin 2B antagonizes RIG-I mediated antiviral effects by inhibition of its protein expression
    • Zhu, Z., Wang, G., Yang, F., Cao, W., Mao, R., Du, X., Zhang, X., Li, C., Li, D., Zhang, K., Foot-and-mouth disease virus viroporin 2B antagonizes RIG-I mediated antiviral effects by inhibition of its protein expression. J. Virol., JVI, 2016, 01310–01316.
    • (2016) J. Virol., JVI , pp. 01310-01316
    • Zhu, Z.1    Wang, G.2    Yang, F.3    Cao, W.4    Mao, R.5    Du, X.6    Zhang, X.7    Li, C.8    Li, D.9    Zhang, K.10
  • 44
    • 84873529276 scopus 로고    scopus 로고
    • Nonstructural Protein 1 of Influenza A Virus Interacts with Human Guanylate-Binding Protein 1 to Antagonize Antiviral Activity
    • Zhu, Z.X., Shi, Z.X., Yan, W.J., Wei, J.C., Shao, D.H., Deng, X.F., Wang, S.H., Li, B.B., Tong, G.Z., Ma, Z.Y., Nonstructural Protein 1 of Influenza A Virus Interacts with Human Guanylate-Binding Protein 1 to Antagonize Antiviral Activity. PloS One, 8(2), 2013, e0055920.
    • (2013) PloS One , vol.8 , Issue.2 , pp. e0055920
    • Zhu, Z.X.1    Shi, Z.X.2    Yan, W.J.3    Wei, J.C.4    Shao, D.H.5    Deng, X.F.6    Wang, S.H.7    Li, B.B.8    Tong, G.Z.9    Ma, Z.Y.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.