메뉴 건너뛰기




Volumn 88, Issue 17, 2014, Pages 10252-10258

Hepatitis a virus 3C protease cleaves NEMO to impair induction of beta interferon

Author keywords

[No Author keywords available]

Indexed keywords

3C PROTEASES; BETA INTERFERON; CYSTEINE PROTEINASE; I KAPPA B KINASE; IKBKG PROTEIN, HUMAN; VIRUS PROTEIN;

EID: 84921522079     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00869-14     Document Type: Article
Times cited : (72)

References (22)
  • 1
    • 31344461659 scopus 로고    scopus 로고
    • Innate immune recognition of viral infection
    • Kawai T, Akira S. 2006. Innate immune recognition of viral infection. Nat. Immunol. 7:131-137. http://dx.doi.org/10.1038/ni1303.
    • (2006) Nat. Immunol , vol.7 , pp. 131-137
    • Kawai, T.1    Akira, S.2
  • 2
    • 33744791510 scopus 로고    scopus 로고
    • Essential role of mda-5 in type I IFN responses to polyriboinosinic:polyribocytidylic acid and encephalomyocarditis picornavirus
    • Gitlin L, Barchet W, Gilfillan S, Cella M, Beutler B, Flavell RA, Diamond MS, Colonna M. 2006. Essential role of mda-5 in type I IFN responses to polyriboinosinic:polyribocytidylic acid and encephalomyocarditis picornavirus. Proc. Natl. Acad. Sci. U. S. A. 103:8459-8464. http://dx.doi.org/10.1073/pnas.0603082103.
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 8459-8464
    • Gitlin, L.1    Barchet, W.2    Gilfillan, S.3    Cella, M.4    Beutler, B.5    Flavell, R.A.6    Diamond, M.S.7    Colonna, M.8
  • 3
    • 79957604087 scopus 로고    scopus 로고
    • Identification of the role of RIG-I, MDA-5 and TLR3 in sensing RNA viruses in porcine epithelial cells using lentivirus-driven RNA interference
    • Husser L, Alves MP, Ruggli N, Summerfield A. 2011. Identification of the role of RIG-I, MDA-5 and TLR3 in sensing RNA viruses in porcine epithelial cells using lentivirus-driven RNA interference. Virus Res. 159: 9-16. http://dx.doi.org/10.1016/j.virusres.2011.04.005.
    • (2011) Virus Res , vol.159 , pp. 9-16
    • Husser, L.1    Alves, M.P.2    Ruggli, N.3    Summerfield, A.4
  • 5
    • 70349807812 scopus 로고    scopus 로고
    • The viral RNA recognition sensor RIG-I is degraded during encephalomyocarditis virus (EMCV) infection
    • Papon L, Oteiza A, Imaizumi T, Kato H, Brocchi E, Lawson TG, Akira S, Mechti N. 2009. The viral RNA recognition sensor RIG-I is degraded during encephalomyocarditis virus (EMCV) infection. Virology 393:311-318. http://dx.doi.org/10.1016/j.virol.2009.08.009.
    • (2009) Virology , vol.393 , pp. 311-318
    • Papon, L.1    Oteiza, A.2    Imaizumi, T.3    Kato, H.4    Brocchi, E.5    Lawson, T.G.6    Akira, S.7    Mechti, N.8
  • 6
    • 81455141907 scopus 로고    scopus 로고
    • The TLR3/TICAM-1 pathway is mandatory for innate immune responses to poliovirus infection
    • Oshiumi H, Okamoto M, Fujii K, Kawanishi T, Matsumoto M, Koike S, Seya T. 2011. The TLR3/TICAM-1 pathway is mandatory for innate immune responses to poliovirus infection. J. Immunol. 187:5320-5327. http://dx.doi.org/10.4049/jimmunol.1101503.
    • (2011) J. Immunol , vol.187 , pp. 5320-5327
    • Oshiumi, H.1    Okamoto, M.2    Fujii, K.3    Kawanishi, T.4    Matsumoto, M.5    Koike, S.6    Seya, T.7
  • 9
    • 34249855382 scopus 로고    scopus 로고
    • Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor
    • Yang Y, Liang Y, Qu L, Chen Z, Yi M, Li K, Lemon SM. 2007. Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor. Proc. Natl. Acad. Sci. U. S. A. 104:7253-7258. http://dx.doi.org/10.1073/pnas.0611506104.
    • (2007) Proc. Natl. Acad. Sci. U. S. A , vol.104 , pp. 7253-7258
    • Yang, Y.1    Liang, Y.2    Qu, L.3    Chen, Z.4    Yi, M.5    Li, K.6    Lemon, S.M.7
  • 10
    • 79960598740 scopus 로고    scopus 로고
    • Disruption of TLR3 signaling due to cleavage of TRIF by the hepatitis A virus protease-polymerase processing intermediate, 3CD
    • Qu L, Feng Z, Yamane D, Liang Y, Lanford RE, Li K, Lemon SM. 2011. Disruption of TLR3 signaling due to cleavage of TRIF by the hepatitis A virus protease-polymerase processing intermediate, 3CD. PLoS Pathog. 7:e1002169. http://dx.doi.org/10.1371/journal.ppat.1002169.
    • (2011) PLoS Pathog , vol.7
    • Qu, L.1    Feng, Z.2    Yamane, D.3    Liang, Y.4    Lanford, R.E.5    Li, K.6    Lemon, S.M.7
  • 11
    • 0028364693 scopus 로고
    • Proteinase 3C of hepatitis A virus (HAV) cleaves the HAV polyprotein P2-P3 at all sites including VP1/2A and 2A/2B
    • Schultheiss T, Kusov YY, Gauss-Muller V. 1994. Proteinase 3C of hepatitis A virus (HAV) cleaves the HAV polyprotein P2-P3 at all sites including VP1/2A and 2A/2B. Virology 198:275-281. http://dx.doi.org/10.1006/viro.1994.1030.
    • (1994) Virology , vol.198 , pp. 275-281
    • Schultheiss, T.1    Kusov, Y.Y.2    Gauss-Muller, V.3
  • 12
    • 0028851295 scopus 로고
    • Cleavage specificity of purified recombinant hepatitis A virus 3C proteinase on natural substrates
    • Schultheiss T, Sommergruber W, Kusov Y, Gauss-Muller V. 1995. Cleavage specificity of purified recombinant hepatitis A virus 3C proteinase on natural substrates. J. Virol. 69:1727-1733.
    • (1995) J. Virol , vol.69 , pp. 1727-1733
    • Schultheiss, T.1    Sommergruber, W.2    Kusov, Y.3    Gauss-Muller, V.4
  • 13
    • 0031047974 scopus 로고    scopus 로고
    • The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition
    • Bergmann EM, Mosimann SC, Chernaia MM, Malcolm BA, James MN. 1997. The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition. J. Virol. 71:2436-2448.
    • (1997) J. Virol , vol.71 , pp. 2436-2448
    • Bergmann, E.M.1    Mosimann, S.C.2    Chernaia, M.M.3    Malcolm, B.A.4    James, M.N.5
  • 14
    • 34249058119 scopus 로고    scopus 로고
    • The NEMO adaptor bridges the nuclear factor-kappaB and interferon regulatory factor signaling pathways
    • Zhao T, Yang L, Sun Q, Arguello M, Ballard DW, Hiscott J, Lin R. 2007. The NEMO adaptor bridges the nuclear factor-kappaB and interferon regulatory factor signaling pathways. Nat. Immunol. 8:592-600. http://dx.doi.org/10.1038/ni1465.
    • (2007) Nat. Immunol , vol.8 , pp. 592-600
    • Zhao, T.1    Yang, L.2    Sun, Q.3    Arguello, M.4    Ballard, D.W.5    Hiscott, J.6    Lin, R.7
  • 16
    • 26244443472 scopus 로고    scopus 로고
    • Linkage map of protein-protein interactions of porcine teschovirus
    • Zell R, Seitz S, Henke A, Munder T, Wutzler P. 2005. Linkage map of protein-protein interactions of porcine teschovirus. J. Gen. Virol. 86: 2763-2768. http://dx.doi.org/10.1099/vir.0.81144-0.
    • (2005) J. Gen. Virol , vol.86 , pp. 2763-2768
    • Zell, R.1    Seitz, S.2    Henke, A.3    Munder, T.4    Wutzler, P.5
  • 17
    • 38149020712 scopus 로고    scopus 로고
    • Picornavirus genome replicati. Identification of the surface of the poliovirus (PV) 3C dimer that interacts withPV3Dpol during VPg uridylylation and construction of a structural model for the PV 3C2-3Dpol complex
    • Shen M, Reitman ZJ, Zhao Y, Moustafa I, Wang Q, Arnold JJ, Pathak HB, Cameron CE. 2008. Picornavirus genome replication. Identification of the surface of the poliovirus (PV) 3C dimer that interacts withPV3Dpol during VPg uridylylation and construction of a structural model for the PV 3C2-3Dpol complex. J. Biol. Chem. 283:875-888. http://dx.doi.org/10.1074/jbc.M707907200.
    • (2008) J. Biol. Chem , vol.283 , pp. 875-888
    • Shen, M.1    Reitman, Z.J.2    Zhao, Y.3    Moustafa, I.4    Wang, Q.5    Arnold, J.J.6    Pathak, H.B.7    Cameron, C.E.8
  • 18
    • 34447536284 scopus 로고    scopus 로고
    • Picornavirus genome replication: assembly and organization of the VPg uridylylation ribonucleoprotein (initiation) complex
    • Pathak HB, Arnold JJ, Wiegand PN, Hargittai MR, Cameron CE. 2007. Picornavirus genome replication: assembly and organization of the VPg uridylylation ribonucleoprotein (initiation) complex. J. Biol. Chem. 282: 16202-16213. http://dx.doi.org/10.1074/jbc.M610608200.
    • (2007) J. Biol. Chem , vol.282 , pp. 16202-16213
    • Pathak, H.B.1    Arnold, J.J.2    Wiegand, P.N.3    Hargittai, M.R.4    Cameron, C.E.5
  • 21
    • 84878354921 scopus 로고    scopus 로고
    • Comparative evaluation of a novel TaqMan real-time reverse transcription-polymerase chain reaction assay for hepatitis A virus detection
    • Qiu F, Zheng H, Yi Y, Jia Z, Cao J, Bi S. 2013. Comparative evaluation of a novel TaqMan real-time reverse transcription-polymerase chain reaction assay for hepatitis A virus detection. J. Int. Med. Res. 41:427-434. http://dx.doi.org/10.1177/0300060513476434.
    • (2013) J. Int. Med. Res , vol.41 , pp. 427-434
    • Qiu, F.1    Zheng, H.2    Yi, Y.3    Jia, Z.4    Cao, J.5    Bi, S.6
  • 22
    • 84873053639 scopus 로고    scopus 로고
    • Cleavage of interferon regulatory factor 7 by enterovirus 71 3C suppresses cellular responses
    • Lei X, Xiao X, Xue Q, Jin Q, He B, Wang J. 2013. Cleavage of interferon regulatory factor 7 by enterovirus 71 3C suppresses cellular responses. J. Virol. 87:1690-1698. http://dx.doi.org/10.1128/JVI.01855-12.
    • (2013) J. Virol , vol.87 , pp. 1690-1698
    • Lei, X.1    Xiao, X.2    Xue, Q.3    Jin, Q.4    He, B.5    Wang, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.