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Volumn 7, Issue , 2016, Pages

Influenza B virus non-structural protein 1 counteracts ISG15 antiviral activity by sequestering ISGylated viral proteins

Author keywords

[No Author keywords available]

Indexed keywords

BETA INTERFERON; NONSTRUCTURAL PROTEIN 1; RIBONUCLEOPROTEIN; SMALL INTERFERING RNA; UBIQUITIN; UBIQUITIN LIKE PROTEIN ISG15; UNCLASSIFIED DRUG; VIRUS NUCLEOPROTEIN; VIRUS RNA; CYTOKINE; INS1 PROTEIN, INFLUENZA VIRUS; ISG15 PROTEIN, HUMAN; PROTEIN BINDING; PROTEINASE; USP18 PROTEIN, HUMAN; VIRAL PROTEIN;

EID: 84986182412     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms12754     Document Type: Article
Times cited : (75)

References (39)
  • 1
    • 0026722530 scopus 로고
    • The interferon-inducible 15-kDa ubiquitin homolog conjugates to intracellular proteins
    • Loeb, K. R. & Haas, A. L. The interferon-inducible 15-kDa ubiquitin homolog conjugates to intracellular proteins. J. Biol. Chem. 267, 7806-7813 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 7806-7813
    • Loeb, K.R.1    Haas, A.L.2
  • 2
    • 77950873763 scopus 로고    scopus 로고
    • Species specificity of the NS1 protein of influenza B virus: NS1 binds only human and non-human primate ubiquitinlike ISG15 proteins
    • Sridharan, H., Zhao, C. & Krug, R. M. Species specificity of the NS1 protein of influenza B virus: NS1 binds only human and non-human primate ubiquitinlike ISG15 proteins. J. Biol. Chem. 285, 7852-7856 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 7852-7856
    • Sridharan, H.1    Zhao, C.2    Krug, R.M.3
  • 3
    • 77957785465 scopus 로고    scopus 로고
    • Emerging role of ISG15 in antiviral immunity
    • Skaug, B. & Chen, Z. J. Emerging role of ISG15 in antiviral immunity. Cell 143, 187-190 (2010).
    • (2010) Cell , vol.143 , pp. 187-190
    • Skaug, B.1    Chen, Z.J.2
  • 5
    • 84875854073 scopus 로고    scopus 로고
    • Interferon-induced ISG15 pathway: An ongoing virus-host battle
    • Zhao, C., Collins, M. N., Hsiang, T. Y. & Krug, R. M. Interferon-induced ISG15 pathway: an ongoing virus-host battle. Trends Microbiol. 21, 181-186 (2013).
    • (2013) Trends Microbiol , vol.21 , pp. 181-186
    • Zhao, C.1    Collins, M.N.2    Hsiang, T.Y.3    Krug, R.M.4
  • 6
    • 0035253852 scopus 로고    scopus 로고
    • Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein
    • Yuan, W. & Krug, R. M. Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein. EMBO J. 20, 362-371 (2001).
    • (2001) EMBO J. , vol.20 , pp. 362-371
    • Yuan, W.1    Krug, R.M.2
  • 7
    • 48249105524 scopus 로고    scopus 로고
    • Vaccinia virus E3 protein prevents the antiviral action of ISG15
    • Guerra, S., Caceres, A., Knobeloch, K. P., Horak, I. & Esteban, M. Vaccinia virus E3 protein prevents the antiviral action of ISG15. PLoS Pathog. 4, e1000096 (2008).
    • (2008) PLoS Pathog , vol.4 , pp. e1000096
    • Guerra, S.1    Caceres, A.2    Knobeloch, K.P.3    Horak, I.4    Esteban, M.5
  • 8
    • 36749007273 scopus 로고    scopus 로고
    • Ovarian tumor domain-containing viral proteases evade ubiquitin-and ISG15-dependent innate immune responses
    • Frias-Staheli, N. et al. Ovarian tumor domain-containing viral proteases evade ubiquitin-and ISG15-dependent innate immune responses. Cell Host Microbe 2, 404-416 (2007).
    • (2007) Cell Host Microbe , vol.2 , pp. 404-416
    • Frias-Staheli, N.1
  • 9
    • 33846603312 scopus 로고    scopus 로고
    • IFN-stimulated gene 15 functions as a critical antiviral molecule against influenza, herpes, Sindbis viruses
    • Lenschow, D. J. et al. IFN-stimulated gene 15 functions as a critical antiviral molecule against influenza, herpes, Sindbis viruses. Proc. Natl Acad. Sci. USA 104, 1371-1376 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 1371-1376
    • Lenschow, D.J.1
  • 10
    • 58149502576 scopus 로고    scopus 로고
    • Mice lacking the ISG15 E1 enzyme UbE1L demonstrate increased susceptibility to both mouse-adapted and non-mouse-adapted influenza B virus infection
    • Lai, C. et al. Mice lacking the ISG15 E1 enzyme UbE1L demonstrate increased susceptibility to both mouse-adapted and non-mouse-adapted influenza B virus infection. J. Virol. 83, 1147-1151 (2009).
    • (2009) J. Virol. , vol.83 , pp. 1147-1151
    • Lai, C.1
  • 11
    • 84919429658 scopus 로고    scopus 로고
    • Novel mode of ISG15-mediated protection against influenza A virus and Sendai virus in mice
    • Morales, D. J. et al. Novel mode of ISG15-mediated protection against influenza A virus and Sendai virus in mice. J. Virol. 89, 337-349 (2015).
    • (2015) J. Virol. , vol.89 , pp. 337-349
    • Morales, D.J.1
  • 12
    • 66149152602 scopus 로고    scopus 로고
    • Interferon-induced ISG15 conjugation inhibits influenza A virus gene expression and replication in human cells
    • Hsiang, T. Y., Zhao, C. & Krug, R. M. Interferon-induced ISG15 conjugation inhibits influenza A virus gene expression and replication in human cells. J. Virol. 83, 5971-5977 (2009).
    • (2009) J. Virol. , vol.83 , pp. 5971-5977
    • Hsiang, T.Y.1    Zhao, C.2    Krug, R.M.3
  • 13
    • 76649140147 scopus 로고    scopus 로고
    • ISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cells
    • Zhao, C., Hsiang, T. Y., Kuo, R. L. & Krug, R. M. ISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cells. Proc. Natl Acad. Sci. USA 107, 2253-2258 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 2253-2258
    • Zhao, C.1    Hsiang, T.Y.2    Kuo, R.L.3    Krug, R.M.4
  • 14
    • 77954753259 scopus 로고    scopus 로고
    • Herc5 attenuates influenza A virus by catalyzing ISGylation of viral NS1 protein
    • Tang, Y. et al. Herc5 attenuates influenza A virus by catalyzing ISGylation of viral NS1 protein. J. Immunol. 184, 5777-5790 (2010).
    • (2010) J. Immunol. , vol.184 , pp. 5777-5790
    • Tang, Y.1
  • 15
    • 77953114765 scopus 로고    scopus 로고
    • The ISG15 conjugation system broadly targets newly synthesized proteins: Implications for the antiviral function of ISG15
    • Durfee, L. A., Lyon, N., Seo, K. & Huibregtse, J. M. The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15. Mol. Cell 38, 722-732 (2010).
    • (2010) Mol. Cell , vol.38 , pp. 722-732
    • Durfee, L.A.1    Lyon, N.2    Seo, K.3    Huibregtse, J.M.4
  • 16
    • 80055100405 scopus 로고    scopus 로고
    • ISG15 is critical in the control of Chikungunya virus infection independent of UbE1L mediated conjugation
    • Werneke, S. W. et al. ISG15 is critical in the control of Chikungunya virus infection independent of UbE1L mediated conjugation. PLoS Pathog. 7, e1002322 (2011).
    • (2011) PLoS Pathog. , vol.7 , pp. 1002322
    • Werneke, S.W.1
  • 17
    • 84866748115 scopus 로고    scopus 로고
    • Mycobacterial disease and impaired IFN-gamma immunity in humans with inherited ISG15 deficiency
    • Bogunovic, D. et al. Mycobacterial disease and impaired IFN-gamma immunity in humans with inherited ISG15 deficiency. Science 337, 1684-1688 (2012).
    • (2012) Science , vol.337 , pp. 1684-1688
    • Bogunovic, D.1
  • 18
    • 84922880395 scopus 로고    scopus 로고
    • Human intracellular ISG15 prevents interferon-alpha/beta over-amplification and auto-inflammation
    • Zhang, X. et al. Human intracellular ISG15 prevents interferon-alpha/beta over-amplification and auto-inflammation. Nature 517, 89-93 (2015).
    • (2015) Nature , vol.517 , pp. 89-93
    • Zhang, X.1
  • 19
    • 33745761009 scopus 로고    scopus 로고
    • UBP43 is a novel regulator of interferon signaling independent of its ISG15 isopeptidase activity
    • Malakhova, O. A. et al. UBP43 is a novel regulator of interferon signaling independent of its ISG15 isopeptidase activity. EMBO J. 25, 2358-2367 (2006).
    • (2006) EMBO J. , vol.25 , pp. 2358-2367
    • Malakhova, O.A.1
  • 20
    • 84970959689 scopus 로고    scopus 로고
    • ISG15 deficiency and increased viral resistance in humans but not mice
    • Speer, S. D. et al. ISG15 deficiency and increased viral resistance in humans but not mice. Nat. Commun. 7, 11496 (2016).
    • (2016) Nat. Commun. , vol.7 , pp. 11496
    • Speer, S.D.1
  • 21
    • 0004250834 scopus 로고    scopus 로고
    • (eds Knipe, D. & Howley, P. ) Lippincott Williams & Wilkins
    • Wright, P., Neumann, G. & Kawaoka, Y. Fields Virology 6th edn (eds Knipe, D. & Howley, P. ) 1186-1243 (Lippincott, Williams & Wilkins, 2013).
    • (2013) Fields Virology 6th Edn , pp. 1186-1243
    • Wright, P.1    Neumann, G.2    Kawaoka, Y.3
  • 22
    • 77951480439 scopus 로고    scopus 로고
    • Species-specific antagonism of host ISGylation by the influenza B virus NS1 protein
    • Versteeg, G. A. et al. Species-specific antagonism of host ISGylation by the influenza B virus NS1 protein. J. Virol. 84, 5423-5430 (2010).
    • (2010) J. Virol. , vol.84 , pp. 5423-5430
    • Versteeg, G.A.1
  • 23
    • 80051970948 scopus 로고    scopus 로고
    • Structural basis for the sequence-specific recognition of human ISG15 by the NS1 protein of influenza B virus
    • Guan, R. et al. Structural basis for the sequence-specific recognition of human ISG15 by the NS1 protein of influenza B virus. Proc. Natl Acad. Sci. USA 108, 13468-13473 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 13468-13473
    • Guan, R.1
  • 24
    • 84864007807 scopus 로고    scopus 로고
    • Structural basis for RNA binding and homo-oligomer formation by influenza B virus nucleoprotein
    • Ng, A. K. et al. Structural basis for RNA binding and homo-oligomer formation by influenza B virus nucleoprotein. J. Virol. 86, 6758-6767 (2012).
    • (2012) J. Virol. , vol.86 , pp. 6758-6767
    • Ng, A.K.1
  • 25
    • 84907990560 scopus 로고    scopus 로고
    • The N terminus of the influenza B virus nucleoprotein is essential for virus viability, nuclear localization, optimal transcription and replication of the viral genome
    • Sherry, L., Smith, M., Davidson, S. & Jackson, D. The N terminus of the influenza B virus nucleoprotein is essential for virus viability, nuclear localization, optimal transcription and replication of the viral genome. J. Virol. 88, 12326-12338 (2014).
    • (2014) J. Virol. , vol.88 , pp. 12326-12338
    • Sherry, L.1    Smith, M.2    Davidson, S.3    Jackson, D.4
  • 26
    • 84922326351 scopus 로고    scopus 로고
    • Selective inactivation of USP18 isopeptidase activity in vivo enhances ISG15 conjugation and viral resistance
    • Ketscher, L. et al. Selective inactivation of USP18 isopeptidase activity in vivo enhances ISG15 conjugation and viral resistance. Proc. Natl Acad. Sci. USA 112, 1577-1582 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 1577-1582
    • Ketscher, L.1
  • 27
    • 84924970829 scopus 로고    scopus 로고
    • At the centre: Influenza A virus ribonucleoproteins
    • Eisfeld, A. J., Neumann, G. & Kawaoka, Y. At the centre: influenza A virus ribonucleoproteins. Nat. Rev. Microbiol. 13, 28-41 (2015).
    • (2015) Nat. Rev. Microbiol. , vol.13 , pp. 28-41
    • Eisfeld, A.J.1    Neumann, G.2    Kawaoka, Y.3
  • 28
    • 84922245983 scopus 로고    scopus 로고
    • Structural insight into cap-snatching and RNA synthesis by influenza polymerase
    • Reich, S. et al. Structural insight into cap-snatching and RNA synthesis by influenza polymerase. Nature 516, 361-366 (2014).
    • (2014) Nature , vol.516 , pp. 361-366
    • Reich, S.1
  • 29
    • 84876033771 scopus 로고    scopus 로고
    • Structure and assembly of the influenza A virus ribonucleoprotein complex
    • Zheng, W. & Tao, Y. J. Structure and assembly of the influenza A virus ribonucleoprotein complex. FEBS Lett. 587, 1206-1214 (2013).
    • (2013) FEBS Lett. , vol.587 , pp. 1206-1214
    • Zheng, W.1    Tao, Y.J.2
  • 30
    • 33845890539 scopus 로고    scopus 로고
    • The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA
    • Ye, Q., Krug, R. M. & Tao, Y. J. The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA. Nature 444, 1078-1082 (2006).
    • (2006) Nature , vol.444 , pp. 1078-1082
    • Ye, Q.1    Krug, R.M.2    Tao, Y.J.3
  • 31
    • 84929494280 scopus 로고    scopus 로고
    • Phosphorylation at the homotypic interface regulates nucleoprotein oligomerization and assembly of the influenza virus replication machinery
    • Mondal, A., Potts, G. K., Dawson, A. R., Coon, J. J. & Mehle, A. Phosphorylation at the homotypic interface regulates nucleoprotein oligomerization and assembly of the influenza virus replication machinery. PLoS Pathog. 11, e1004826 (2015).
    • (2015) PLoS Pathog. , vol.11 , pp. 1004826
    • Mondal, A.1    Potts, G.K.2    Dawson, A.R.3    Coon, J.J.4    Mehle, A.5
  • 32
    • 84875829625 scopus 로고    scopus 로고
    • The role and assembly mechanism of nucleoprotein in influenza A virus ribonucleoprotein complexes
    • Turrell, L., Lyall, J. W., Tiley, L. S., Fodor, E. & Vreede, F. T. The role and assembly mechanism of nucleoprotein in influenza A virus ribonucleoprotein complexes. Nat. Commun. 4, 1591 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 1591
    • Turrell, L.1    Lyall, J.W.2    Tiley, L.S.3    Fodor, E.4    Vreede, F.T.5
  • 33
    • 80053650056 scopus 로고    scopus 로고
    • E339. R416 salt bridge of nucleoprotein as a feasible target for influenza virus inhibitors
    • Shen, Y. F. et al. E339. . . R416 salt bridge of nucleoprotein as a feasible target for influenza virus inhibitors. Proc. Natl Acad. Sci . USA 108, 16515-16520 (2011).
    • (2011) Proc. Natl Acad. Sci . USA , vol.108 , pp. 16515-16520
    • Shen, Y.F.1
  • 34
    • 58149517735 scopus 로고    scopus 로고
    • Analysis of influenza B Virus NS1 protein trafficking reveals a novel interaction with nuclear speckle domains
    • Schneider, J., Dauber, B., Melen, K., Julkunen, I. & Wolff, T. Analysis of influenza B Virus NS1 protein trafficking reveals a novel interaction with nuclear speckle domains. J. Virol. 83, 701-711 (2009).
    • (2009) J. Virol. , vol.83 , pp. 701-711
    • Schneider, J.1    Dauber, B.2    Melen, K.3    Julkunen, I.4    Wolff, T.5
  • 35
    • 84874584098 scopus 로고    scopus 로고
    • Biochemical and structural evidence in support of a coherent model for the formation of the double-helical influenza A virus ribonucleoprotein
    • Ye, Q. et al. Biochemical and structural evidence in support of a coherent model for the formation of the double-helical influenza A virus ribonucleoprotein. mBio. 4, e00467-12 (2012).
    • (2012) MBio. , vol.4 , pp. 00467-00512
    • Ye, Q.1
  • 36
    • 0037143718 scopus 로고    scopus 로고
    • Rescue of influenza B virus from eight plasmids
    • Hoffmann, E. et al. Rescue of influenza B virus from eight plasmids. Proc. Natl Acad. Sci. USA 99, 11411-11416 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11411-11416
    • Hoffmann, E.1
  • 38
    • 51549108484 scopus 로고    scopus 로고
    • Attenuated influenza virus (LAIV) vehicles are strong inducers of immunity toward influenza B virus
    • Huber, V. C., Kleimeyer, L. H. & McCullers, J. A. Live, attenuated influenza virus (LAIV) vehicles are strong inducers of immunity toward influenza B virus. Vaccine 26, 5381-5388 (2008).
    • (2008) Vaccine , vol.26 , pp. 5381-5388
    • Huber, V.C.1    Kleimeyer, L.H.2    Live, A.M.J.3
  • 39
    • 0036720769 scopus 로고    scopus 로고
    • A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs
    • Fodor, E. et al. A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs. J. Virol. 76, 8989-9001 (2002).
    • (2002) J. Virol. , vol.76 , pp. 8989-9001
    • Fodor, E.1


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