메뉴 건너뛰기




Volumn 88, Issue 23, 2014, Pages 13821-13835

Overlapping and distinct molecular determinants dictating the antiviral activities of TRIM56 against flaviviruses and coronavirus

Author keywords

[No Author keywords available]

Indexed keywords

TRIPARTITE MOTIF PROTEIN 56; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VIRUS PROTEIN; MUTANT PROTEIN; TRIM56 PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE;

EID: 84911361751     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02505-14     Document Type: Article
Times cited : (75)

References (37)
  • 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
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors
    • Kawai T, Akira S. 2010. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat. Immunol. 11:373-384http://dx.doi.org/10.1038/ni.1863.
    • (2010) Nat. Immunol. , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 3
    • 75749089555 scopus 로고    scopus 로고
    • Recognition of viral nucleic acids in innate immunity
    • Yoneyama M, Fujita T. 2010. Recognition of viral nucleic acids in innate immunity. Rev. Med. Virol. 20:4-22. http://dx.doi.org/10.1002/rmv.633.
    • (2010) Rev. Med. Virol. , vol.20 , pp. 4-22
    • Yoneyama, M.1    Fujita, T.2
  • 4
    • 84894585119 scopus 로고    scopus 로고
    • Toll-Like receptors in antiviral innate immunity
    • Lester SN, Li K. 2014. Toll-Like receptors in antiviral innate immunity. J. Mol. Biol. 426:1246-1264. http://dx.doi.org/10.1016/j.jmb.2013.11.024.
    • (2014) J. Mol. Biol. , vol.426 , pp. 1246-1264
    • Lester, S.N.1    Li, K.2
  • 5
    • 33646166525 scopus 로고    scopus 로고
    • Intracellular restriction factors in mammalian cells-an ancient defense system finds a modern foe
    • Baumann JG. 2006. Intracellular restriction factors in mammalian cells-an ancient defense system finds a modern foe. Curr. HIV. Res. 4:141-168. http://dx.doi.org/10.2174/157016206776055093.
    • (2006) Curr. HIV. Res. , vol.4 , pp. 141-168
    • Baumann, J.G.1
  • 6
    • 77953855867 scopus 로고    scopus 로고
    • TRIM proteins: another class of viral victims
    • Munir M. 2010. TRIM proteins: another class of viral victims. Sci. Signal. 3:jc2. http://dx.doi.org/10.1126/scisignal.3118jc2.
    • (2010) Sci. Signal. , vol.3 , pp. jc2
    • Munir, M.1
  • 7
    • 84894515095 scopus 로고    scopus 로고
    • TRIMmunity: the roles of the TRIM E3-ubiquitin ligase family in innate antiviral immunity
    • Rajsbaum R, García-Sastre A, Versteeg GA. 2014. TRIMmunity: the roles of the TRIM E3-ubiquitin ligase family in innate antiviral immunity. J. Mol. Biol. 426:1265-1284. http://dx.doi.org/10.1016/j.jmb.2013.12.005.
    • (2014) J. Mol. Biol. , vol.426 , pp. 1265-1284
    • Rajsbaum, R.1    García-Sastre, A.2    Versteeg, G.A.3
  • 8
    • 80052289447 scopus 로고    scopus 로고
    • Regulation of innate immune signalling pathways by the tripartite motif (TRIM) family proteins
    • Kawai T, Akira S. 2011. Regulation of innate immune signalling pathways by the tripartite motif (TRIM) family proteins. EMBO Mol. Med. 3:513-527http://dx.doi.org/10.1002/emmm.201100160.
    • (2011) EMBO Mol. Med. , vol.3 , pp. 513-527
    • Kawai, T.1    Akira, S.2
  • 9
    • 54949126675 scopus 로고    scopus 로고
    • TRIM family proteins and their emerging roles in innate immunity
    • Ozato K, Shin DM, Chang TH, Morse HC, III. 2008. TRIM family proteins and their emerging roles in innate immunity. Nat. Rev. Immunol. 8:849-860. http://dx.doi.org/10.1038/nri2413.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 849-860
    • Ozato, K.1    Shin, D.M.2    Chang, T.H.3    Morse III, H.C.4
  • 10
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys
    • Stremlau M, Owens CM, Perron MJ, Kiessling M, Autissier P, Sodroski J. 2004. The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. Nature 427:848-853. Http://dx.doi.org /10.1038/nature02343.
    • (2004) Nature , vol.427 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3    Kiessling, M.4    Autissier, P.5    Sodroski, J.6
  • 11
    • 80053004397 scopus 로고    scopus 로고
    • TRIM79α an interferon-stimulated gene product, restricts tick-borne encephalitis virus replication by degrading the viral RNA polymerase
    • Taylor RT, Lubick KJ, Robertson SJ, Broughton JP, Bloom ME, Bresnahan WA, Best SM. 2011. TRIM79α, an interferon-stimulated gene product, restricts tick-borne encephalitis virus replication by degrading the viral RNA polymerase. Cell Host Microbe 10:185-196. Http://dx.doi .org/10.1016/j.chom.2011.08.004.
    • (2011) Cell Host Microbe , vol.10 , pp. 185-196
    • Taylor, R.T.1    Lubick, K.J.2    Robertson, S.J.3    Broughton, J.P.4    Bloom, M.E.5    Bresnahan, W.A.6    Best, S.M.7
  • 12
    • 79952856821 scopus 로고    scopus 로고
    • TRIM56 is a virusand interferon-inducible E3 ubiquitin ligase that restricts pestivirus infection
    • Wang J, Liu B, Wang N, Lee YM, Liu C, Li K. 2011. TRIM56 is a virusand interferon-inducible E3 ubiquitin ligase that restricts pestivirus infection. J. Virol. 85:3733-3745. http://dx.doi.org/10.1128/JVI.02546-10.
    • (2011) J. Virol. , vol.85 , pp. 3733-3745
    • Wang, J.1    Liu, B.2    Wang, N.3    Lee, Y.M.4    Liu, C.5    Li, K.6
  • 13
    • 84861978036 scopus 로고    scopus 로고
    • Flaviviruses and flavivirus vaccines
    • Heinz FX, Stiasny K. 2012. Flaviviruses and flavivirus vaccines. Vaccine 30:4301-4306. http://dx.doi.org/10.1016/j.vaccine.2011.09.114.
    • (2012) Vaccine , vol.30 , pp. 4301-4306
    • Heinz, F.X.1    Stiasny, K.2
  • 14
    • 84867801015 scopus 로고    scopus 로고
    • TRIM56 is an essential component of the TLR3 antiviral signaling pathway
    • Shen Y, Li NL, Wang J, Liu B, Lester S, Li K. 2012. TRIM56 is an essential component of the TLR3 antiviral signaling pathway. J. Biol. Chem. 287:36404-36413. http://dx.doi.org/10.1074/jbc.M112.397075.
    • (2012) J. Biol. Chem. , vol.287 , pp. 36404-36413
    • Shen, Y.1    Li, N.L.2    Wang, J.3    Liu, B.4    Lester, S.5    Li, K.6
  • 16
    • 80055106240 scopus 로고    scopus 로고
    • Inhibition of dengue virus by targeting viral NS4B protein
    • Xie X, Wang QY, Xu HY, Qing M, Kramer L, Yuan Z, Shi PY. 2011. Inhibition of dengue virus by targeting viral NS4B protein. J. Virol. 85: 11183-11195. http://dx.doi.org/10.1128/JVI.05468-11.
    • (2011) J. Virol. , vol.85 , pp. 11183-11195
    • Xie, X.1    Wang, Q.Y.2    Xu, H.Y.3    Qing, M.4    Kramer, L.5    Yuan, Z.6    Shi, P.Y.7
  • 19
    • 70349278409 scopus 로고    scopus 로고
    • Toll-like receptor 3 mediates establishment of an antiviral state against hepatitis C virus in hepatoma cells
    • Wang N, Liang Y, Devaraj S, Wang J, Lemon SM, Li K. 2009. Toll-like receptor 3 mediates establishment of an antiviral state against hepatitis C virus in hepatoma cells. J. Virol. 83:9824-9834. Http://dx.doi.org/10.1128 /JVI.01125-09.
    • (2009) J. Virol. , vol.83 , pp. 9824-9834
    • Wang, N.1    Liang, Y.2    Devaraj, S.3    Wang, J.4    Lemon, S.M.5    Li, K.6
  • 20
    • 20444442721 scopus 로고    scopus 로고
    • Distinct poly(I-C) and virus-activated signaling pathways leading to interferon-beta production in hepatocytes
    • Li K, Chen Z, Kato N, Gale M, Jr, Lemon SM. 2005. Distinct poly(I-C) and virus-activated signaling pathways leading to interferon-beta production in hepatocytes. J. Biol. Chem. 280:16739-16747. Http://dx.doi.org/10 .1074/jbc.M414139200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16739-16747
    • Li, K.1    Chen, Z.2    Kato, N.3    Gale Jr., M.4    Lemon, S.M.5
  • 22
    • 77949899515 scopus 로고    scopus 로고
    • Viral induction of the zinc-finger antiviral protein is IRF3-dependent but NF-kappa B-independent
    • Wang N, Dong Q, Li J, Jangra RK, Fan M, Brasier AR, Lemon SM, Pfeffer LM, Li K. 2010. Viral induction of the zinc-finger antiviral protein is IRF3-dependent but NF-kappa B-independent. J. Biol. Chem. 285: 6080-6090. http://dx.doi.org/10.1074/jbc.M109.054486.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6080-6090
    • Wang, N.1    Dong, Q.2    Li, J.3    Jangra, R.K.4    Fan, M.5    Brasier, A.R.6    Lemon, S.M.7    Pfeffer, L.M.8    Li, K.9
  • 23
    • 10744225794 scopus 로고    scopus 로고
    • Frequent detection of human coronaviruses in clinical specimens from patients with respiratory tract infection by use of a novel realtime reverse-transcriptase polymerase chain reaction
    • van Elden LJ, van Loon AM, van Alphen F, Hendriksen KA, Hoepelman AI, van Kraaij MG, Oosterheert JJ, Schipper P, Schuurman R, Nijhuis M. 2004. Frequent detection of human coronaviruses in clinical specimens from patients with respiratory tract infection by use of a novel realtime reverse-transcriptase polymerase chain reaction. J. Infect. Dis. 189: 652-657. http://dx.doi.org/10.1086/381207.
    • (2004) J. Infect. Dis. , vol.189 , pp. 652-657
    • van Elden, L.J.1    van Loon, A.M.2    van Alphen, F.3    Hendriksen, K.A.4    Hoepelman, A.I.5    van Kraaij, M.G.6    Oosterheert, J.J.7    Schipper, P.8    Schuurman, R.9    Nijhuis, M.10
  • 24
    • 84860656208 scopus 로고    scopus 로고
    • Host factors in the replication of positive-strand RNA viruses
    • Wang RY, Li K. 2012. Host factors in the replication of positive-strand RNA viruses. Chang Gung Med. J. 35:111-124.
    • (2012) Chang Gung Med. J. , vol.35 , pp. 111-124
    • Wang, R.Y.1    Li, K.2
  • 25
    • 78650214109 scopus 로고    scopus 로고
    • The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA
    • Tsuchida T, Zou J, Saitoh T, Kumar H, Abe T, Matsuura Y, Kawai T, Akira S. 2010. The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA. Immunity 33:765-776. http://dx.doi.org/10.1016/j.immuni.2010.10.013.
    • (2010) Immunity , vol.33 , pp. 765-776
    • Tsuchida, T.1    Zou, J.2    Saitoh, T.3    Kumar, H.4    Abe, T.5    Matsuura, Y.6    Kawai, T.7    Akira, S.8
  • 27
    • 38849194747 scopus 로고    scopus 로고
    • Identification of three interferon-inducible cellular enzymes that inhibit the replication of hepatitis C virus
    • Jiang D, Guo H, Xu C, Chang J, Gu B, Wang L, Block TM, Guo JT. Identification of three interferon-inducible cellular enzymes that inhibit the replication of hepatitis C virus. J. Virol. 82:1665-1678. Http: //dx.doi.org/10.1128/JVI.02113-07.
    • J. Virol. , vol.82 , pp. 1665-1678
    • Jiang, D.1    Guo, H.2    Xu, C.3    Chang, J.4    Gu, B.5    Wang, L.6    Block, T.M.7    Guo, J.T.8
  • 29
    • 79951679142 scopus 로고    scopus 로고
    • Innate immune DNA sensing pathways: STING AIMII and the regulation of interferon production and inflammatory responses
    • Barber GN. 2011. Innate immune DNA sensing pathways: STING, AIMII and the regulation of interferon production and inflammatory responses. Curr. Opin. Immunol. 23:10-20. Http://dx.doi.org/10.1016/j.coi.2010.12 .015.
    • (2011) Curr. Opin. Immunol. , vol.23 , pp. 10-20
    • Barber, G.N.1
  • 30
    • 84899131835 scopus 로고    scopus 로고
    • The cGAS-cGAMP-STING pathway of cytosolic DNA sensing and signaling
    • Cai X, Chiu YH, Chen ZJ. 2014. The cGAS-cGAMP-STING pathway of cytosolic DNA sensing and signaling. Mol. Cell 54:289-296. Http://dx.doi .org/10.1016/j.molcel.2014.03.040.
    • (2014) Mol. Cell , vol.54 , pp. 289-296
    • Cai, X.1    Chiu, Y.H.2    Chen, Z.J.3
  • 31
    • 84875797273 scopus 로고    scopus 로고
    • TRIM22 inhibits influenza A virus infection by targeting the viral nucleoprotein for degradation
    • Di Pietro A, Kajaste-Rudnitski A, Oteiza A, Nicora L, Towers GJ, Mechti N, Vicenzi E. 2013. TRIM22 inhibits influenza A virus infection by targeting the viral nucleoprotein for degradation. J. Virol. 87:4523-4533 http://dx.doi.org/10.1128/JVI.02548-12.
    • (2013) J. Virol. , vol.87 , pp. 4523-4533
    • Di Pietro, A.1    Kajaste-Rudnitski, A.2    Oteiza, A.3    Nicora, L.4    Towers, G.J.5    Mechti, N.6    Vicenzi, E.7
  • 32
    • 40349116307 scopus 로고    scopus 로고
    • TRIM E3 ligases interfere with early and late stages of the retroviral life cycle
    • Uchil PD, Quinlan BD, Chan WT, Luna JM, Mothes W. 2008. TRIM E3 ligases interfere with early and late stages of the retroviral life cycle. PLoS Pathog. 4:e16. http://dx.doi.org/10.1371/journal.ppat.0040016.
    • (2008) PLoS Pathog , vol.4
    • Uchil, P.D.1    Quinlan, B.D.2    Chan, W.T.3    Luna, J.M.4    Mothes, W.5
  • 33
    • 79951540682 scopus 로고    scopus 로고
    • Functional interactions between ubiquitin E2 enzymes and TRIM proteins
    • Napolitano LM, Jaffray EG, Hay RT, Meroni G. 2011. Functional interactions between ubiquitin E2 enzymes and TRIM proteins. Biochem. J. 434:309-319. http://dx.doi.org/10.1042/BJ20101487.
    • (2011) Biochem. J. , vol.434 , pp. 309-319
    • Napolitano, L.M.1    Jaffray, E.G.2    Hay, R.T.3    Meroni, G.4
  • 36
    • 80555133291 scopus 로고    scopus 로고
    • Tripartite motif-containing protein 28 is a small ubiquitin-related modifier E3 ligase and negative regulator of IFN regulatory factor 7
    • Liang Q, Deng H, Li X, Wu X, Tang Q, Chang TH, Peng H, Rauscher FJ, III, Ozato K, Zhu F. 2011. Tripartite motif-containing protein 28 is a small ubiquitin-related modifier E3 ligase and negative regulator of IFN regulatory factor 7. J. Immunol. 187:4754-4763. Http://dx.doi.org/10 .4049/jimmunol.1101704.
    • (2011) J. Immunol. , vol.187 , pp. 4754-4763
    • Liang, Q.1    Deng, H.2    Li, X.3    Wu, X.4    Tang, Q.5    Chang, T.H.6    Peng, H.7    Rauscher III, F.J.8    Ozato, K.9    Zhu, F.10
  • 37
    • 33645217490 scopus 로고    scopus 로고
    • The interferon-inducible ubiquitin-protein isopeptide ligase (E3) EFP also functions as an ISG15 E3 ligase
    • Zou W, Zhang DE. 2006. The interferon-inducible ubiquitin-protein isopeptide ligase (E3) EFP also functions as an ISG15 E3 ligase. J. Biol. Chem. 281:3989-3994. http://dx.doi.org/10.1074/jbc.M510787200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3989-3994
    • Zou, W.1    Zhang, D.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.