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Volumn 88, Issue 20, 2014, Pages 12146-12151

A single amino acid substitution in the novel H7N9 influenza a virus NS1 protein increases CPSF30 binding and virulence

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR; CPSF30 PROTEIN; NONSTRUCTURAL PROTEIN 1; UNCLASSIFIED DRUG; INS1 PROTEIN, INFLUENZA VIRUS; VIRUS PROTEIN;

EID: 84907915259     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01567-14     Document Type: Article
Times cited : (65)

References (33)
  • 1
    • 84907911134 scopus 로고    scopus 로고
    • Center for Infectious Disease Research and Policy, University of Minnesota, Minneapolis, MN. Accessed June 2014.
    • Center for Infectious Disease Research and Policy. 2014. H7N9 avian influenza: resources and literature. Center for Infectious Disease Research and Policy, University of Minnesota, Minneapolis, MN. http://www.cidrap.umn.edu/infectious-disease-topics/h7n9-avian-influenza#literature. Accessed June 2014.
    • (2014) H7N9 avian influenza: resources and literature
  • 2
    • 84894546931 scopus 로고    scopus 로고
    • Amino acid substitutions in polymerase basic protein 2 gene contributes to the pathogenicity of the novel A/H7N9 influenza virus in mammalian hosts
    • Mok CK, Lee HH, Lestra M, Nicholls JM, Chan CW, Sia SF, Zhu H, Poon LL, Guan Y, Peiris JM. 2014. Amino acid substitutions in polymerase basic protein 2 gene contributes to the pathogenicity of the novel A/H7N9 influenza virus in mammalian hosts. J. Virol. 88:3568-3576. http://dx.doi.org/10.1128/JVI.02740-13.
    • (2014) J. Virol. , vol.88 , pp. 3568-3576
    • Mok, C.K.1    Lee, H.H.2    Lestra, M.3    Nicholls, J.M.4    Chan, C.W.5    Sia, S.F.6    Zhu, H.7    Poon, L.L.8    Guan, Y.9    Peiris, J.M.10
  • 3
    • 84896671181 scopus 로고    scopus 로고
    • The PB2 E627K mutation contributes to the high polymerase activity and enhanced replication of H7N9 influenza virus
    • Zhang H, Li X, Guo J, Li L, Chang C, Li Y, Bian C, Xu K, Chen H, Sun B. 2014. The PB2 E627K mutation contributes to the high polymerase activity and enhanced replication of H7N9 influenza virus. J. Gen. Virol. 95(Part 4):779-786. http://dx.doi.org/10.1099/vir.0.061721-0.
    • (2014) J. Gen. Virol. , vol.95 , pp. 779-786
    • Zhang, H.1    Li, X.2    Guo, J.3    Li, L.4    Chang, C.5    Li, Y.6    Bian, C.7    Xu, K.8    Chen, H.9    Sun, B.10
  • 6
    • 84876494442 scopus 로고    scopus 로고
    • Genetic analysis of novel avian A(H7N9) influenza viruses isolated from patients in China, February to April 2013
    • Kageyama T, Fujisaki S, Takashita E, Xu H, Yamada S, Uchida Y, Neumann G, Saito T, Kawaoka Y, Tashiro M. 2013. Genetic analysis of novel avian A(H7N9) influenza viruses isolated from patients in China, February to April 2013. Euro Surveill. 18:20453. http://www.eurosurveillance.org/ViewArticle.aspx?ArticleId=20453.
    • (2013) Euro Surveill. , vol.18 , pp. 20453
    • Kageyama, T.1    Fujisaki, S.2    Takashita, E.3    Xu, H.4    Yamada, S.5    Uchida, Y.6    Neumann, G.7    Saito, T.8    Kawaoka, Y.9    Tashiro, M.10
  • 7
    • 84885598343 scopus 로고    scopus 로고
    • H7N9 influenza viruses interact preferentially with alpha2,3-linked sialic acids and bind weakly to alpha2,6-linked sialic acids
    • Ramos I, Krammer F, Hai R, Aguilera D, Bernal-Rubio D, Steel J, García-Sastre A, Fernandez-Sesma A. 2013. H7N9 influenza viruses interact preferentially with alpha2,3-linked sialic acids and bind weakly to alpha2,6-linked sialic acids. J. Gen. Virol. 94:2417-2423. http://dx.doi.org /10.1099/vir.0.056184-0.
    • (2013) J. Gen. Virol. , vol.94 , pp. 2417-2423
    • Ramos, I.1    Krammer, F.2    Hai, R.3    Aguilera, D.4    Bernal-Rubio, D.5    Steel, J.6    García-Sastre, A.7    Fernandez-Sesma, A.8
  • 10
    • 84889243391 scopus 로고    scopus 로고
    • Preferential recognition of avian-like receptors in human influenza A H7N9 viruses
    • Xu R, de Vries RP, Zhu X, Nycholat CM, McBride R, Yu W, Paulson JC, Wilson IA. 2013. Preferential recognition of avian-like receptors in human influenza A H7N9 viruses. Science 342:1230-1235. http://dx.doi.org/10.1126/science.1243761.
    • (2013) Science , vol.342 , pp. 1230-1235
    • Xu, R.1    de Vries, R.P.2    Zhu, X.3    Nycholat, C.M.4    McBride, R.5    Yu, W.6    Paulson, J.C.7    Wilson, I.A.8
  • 11
    • 54449099369 scopus 로고    scopus 로고
    • The multifunctional NS1 protein of influenza A viruses
    • Hale BG, Randall RE, Ortin J, Jackson D. 2008. The multifunctional NS1 protein of influenza A viruses. J. Gen. Virol. 89:2359-2376. http://dx.doi.org/10.1099/vir.0.2008/004606-0.
    • (2008) J. Gen. Virol. , vol.89 , pp. 2359-2376
    • Hale, B.G.1    Randall, R.E.2    Ortin, J.3    Jackson, D.4
  • 13
    • 33645037542 scopus 로고    scopus 로고
    • Variation in the ability of human influenza A viruses to induce and inhibit the IFN-beta pathway
    • Hayman A, Comely S, Lackenby A, Murphy S, McCauley J, Goodbourn S, Barclay W. 2006. Variation in the ability of human influenza A viruses to induce and inhibit the IFN-beta pathway. Virology 347:52-64. http: //dx.doi.org/10.1016/j.virol.2005.11.024.
    • (2006) Virology , vol.347 , pp. 52-64
    • Hayman, A.1    Comely, S.2    Lackenby, A.3    Murphy, S.4    McCauley, J.5    Goodbourn, S.6    Barclay, W.7
  • 14
    • 34250810666 scopus 로고    scopus 로고
    • Multiple antiinterferon actions of the influenza A virus NS1 protein
    • Kochs G, García-Sastre A, Martínez-Sobrido L. 2007. Multiple antiinterferon actions of the influenza A virus NS1 protein. J. Virol. 81:7011-7021. http://dx.doi.org/10.1128/JVI.02581-06.
    • (2007) J. Virol. , vol.81 , pp. 7011-7021
    • Kochs, G.1    García-Sastre, A.2    Martínez-Sobrido, L.3
  • 15
    • 78149413053 scopus 로고    scopus 로고
    • Influenza A virus strains that circulate in humans differ in the ability of their NS1 proteins to block the activation of IRF3 and interferon-beta transcription
    • Kuo RL, Zhao C, Malur M, Krug RM. 2010. Influenza A virus strains that circulate in humans differ in the ability of their NS1 proteins to block the activation of IRF3 and interferon-beta transcription. Virology 408:146-158. http://dx.doi.org/10.1016/j.virol.2010.09.012.
    • (2010) Virology , vol.408 , pp. 146-158
    • Kuo, R.L.1    Zhao, C.2    Malur, M.3    Krug, R.M.4
  • 17
  • 18
    • 33846061693 scopus 로고    scopus 로고
    • Inhibition of retinoic acid-inducible gene I-mediated induction of beta interferon by the NS1 protein of influenza A virus
    • Mibayashi M, Martínez-Sobrido L, Loo YM, Cárdenas WB, Gale M, Jr, García-Sastre A. 2007. Inhibition of retinoic acid-inducible gene I-mediated induction of beta interferon by the NS1 protein of influenza A virus. J. Virol. 81:514-524. http://dx.doi.org/10.1128/JVI.01265-06.
    • (2007) J. Virol. , vol.81 , pp. 514-524
    • Mibayashi, M.1    Martínez-Sobrido, L.2    Loo, Y.M.3    Cárdenas, W.B.4    Gale, M.5    García-Sastre, A.6
  • 21
    • 0032086357 scopus 로고    scopus 로고
    • Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs
    • Nemeroff ME, Barabino SM, Li Y, Keller W, Krug RM. 1998. Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs. Mol. Cell 1:991-1000. http://dx.doi.org/10.1016/S1097-2765(00)80099-4.
    • (1998) Mol. Cell , vol.1 , pp. 991-1000
    • Nemeroff, M.E.1    Barabino, S.M.2    Li, Y.3    Keller, W.4    Krug, R.M.5
  • 22
    • 0037444193 scopus 로고    scopus 로고
    • Cellular antiviral responses against influenza A virus are countered at the posttranscriptional level by the viral NS1A protein via its binding to a cellular protein required for the 3' end processing of cellular pre-mRNAS
    • Noah DL, Twu KY, Krug RM. 2003. Cellular antiviral responses against influenza A virus are countered at the posttranscriptional level by the viral NS1A protein via its binding to a cellular protein required for the 3' end processing of cellular pre-mRNAS. Virology 307:386-395. http://dx.doi.org/10.1016/S0042-6822(02)00127-7.
    • (2003) Virology , vol.307 , pp. 386-395
    • Noah, D.L.1    Twu, K.Y.2    Krug, R.M.3
  • 23
    • 34547110101 scopus 로고    scopus 로고
    • The H5N1 influenza virus NS genes selected after 1998 enhance virus replication in mammalian cells
    • Twu KY, Kuo RL, Marklund J, Krug RM. 2007. The H5N1 influenza virus NS genes selected after 1998 enhance virus replication in mammalian cells. J. Virol. 81:8112-8121. http://dx.doi.org/10.1128/JVI.00006-07.
    • (2007) J. Virol. , vol.81 , pp. 8112-8121
    • Twu, K.Y.1    Kuo, R.L.2    Marklund, J.3    Krug, R.M.4
  • 24
    • 84857425220 scopus 로고    scopus 로고
    • Multifunctional adaptive NS1 mutations are selected upon human influenza virus evolution in the mouse
    • Forbes NE, Ping J, Dankar SK, Jia JJ, Selman M, Keleta L, Zhou Y, Brown EG. 2012. Multifunctional adaptive NS1 mutations are selected upon human influenza virus evolution in the mouse. PLoS One 7:e31839. http://dx.doi.org/10.1371/journal.pone.0031839.
    • (2012) PLoS One , vol.7 , pp. e31839
    • Forbes, N.E.1    Ping, J.2    Dankar, S.K.3    Jia, J.J.4    Selman, M.5    Keleta, L.6    Zhou, Y.7    Brown, E.G.8
  • 26
    • 79960403406 scopus 로고    scopus 로고
    • The virulence of 1997 H5N1 influenza viruses in the mouse model is increased by correcting a defect in their NS1 proteins
    • Spesock A, Malur M, Hossain MJ, Chen LM, Njaa BL, Davis CT, Lipatov AS, York IA, Krug RM, Donis RO. 2011. The virulence of 1997 H5N1 influenza viruses in the mouse model is increased by correcting a defect in their NS1 proteins. J. Virol. 85:7048-7058. http://dx.doi.org/10.1128/JVI.00417-11.
    • (2011) J. Virol. , vol.85 , pp. 7048-7058
    • Spesock, A.1    Malur, M.2    Hossain, M.J.3    Chen, L.M.4    Njaa, B.L.5    Davis, C.T.6    Lipatov, A.S.7    York, I.A.8    Krug, R.M.9    Donis, R.O.10
  • 27
    • 84880865579 scopus 로고    scopus 로고
    • Influenza A/Hong Kong/156/1997(H5N1) virus NS1 gene mutations F103L and M106I both increase IFN antagonism, virulence and cytoplasmic localization but differ in binding to RIG-I and CPSF30
    • Dankar SK, Miranda E, Forbes NE, Pelchat M, Tavassoli A, Selman M, Ping J, Jia J, Brown EG. 2013. Influenza A/Hong Kong/156/1997(H5N1) virus NS1 gene mutations F103L and M106I both increase IFN antagonism, virulence and cytoplasmic localization but differ in binding to RIG-I and CPSF30. Virol. J. 10:243. http://dx.doi.org/10.1186/1743-422X-10-243.
    • (2013) Virol. J. , vol.10 , pp. 243
    • Dankar, S.K.1    Miranda, E.2    Forbes, N.E.3    Pelchat, M.4    Tavassoli, A.5    Selman, M.6    Ping, J.7    Jia, J.8    Brown, E.G.9
  • 28
    • 78649414629 scopus 로고    scopus 로고
    • Glycine 184 in nonstructural protein NS1 determines the virulence of influenza A virus strain PR8 without affecting the host interferon response
    • Steidle S, Martínez-Sobrido L, Mordstein M, Lienenklaus S, García-Sastre A, Staheli P, Kochs G. 2010. Glycine 184 in nonstructural protein NS1 determines the virulence of influenza A virus strain PR8 without affecting the host interferon response. J. Virol. 84:12761-12770. http://dx.doi.org/10.1128/JVI.00701-10.
    • (2010) J. Virol. , vol.84 , pp. 12761-12770
    • Steidle, S.1    Martínez-Sobrido, L.2    Mordstein, M.3    Lienenklaus, S.4    García-Sastre, A.5    Staheli, P.6    Kochs, G.7
  • 31
    • 55249118428 scopus 로고    scopus 로고
    • Influenza B virus NS1-truncated mutants: live-attenuated vaccine approach
    • Hai R, Martinez-Sobrido L, Fraser KA, Ayllon J, García-Sastre A, Palese P. 2008. Influenza B virus NS1-truncated mutants: live-attenuated vaccine approach. J. Virol. 82:10580-10590. http://dx.doi.org/10.1128/JVI.01213-08.
    • (2008) J. Virol. , vol.82 , pp. 10580-10590
    • Hai, R.1    Martinez-Sobrido, L.2    Fraser, K.A.3    Ayllon, J.4    García-Sastre, A.5    Palese, P.6
  • 32
    • 79960384534 scopus 로고    scopus 로고
    • Influenza A viruses: new research developments
    • Medina RA, García-Sastre A. 2011. Influenza A viruses: new research developments. Nat. Rev. Microbiol. 9:590-603. http://dx.doi.org/10.1038 /nrmicro2613.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 590-603
    • Medina, R.A.1    García-Sastre, A.2
  • 33
    • 59649123636 scopus 로고    scopus 로고
    • Influenza a virus polymerase is an integral component of the CPSF30-NS1A protein complex in infected cells
    • Kuo RL, Krug RM. 2009. Influenza a virus polymerase is an integral component of the CPSF30-NS1A protein complex in infected cells. J. Virol. 83:1611-1616. http://dx.doi.org/10.1128/JVI.01491-08.
    • (2009) J. Virol. , vol.83 , pp. 1611-1616
    • Kuo, R.L.1    Krug, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.