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Volumn 39, Issue 3, 2007, Pages 155-162

Structure and function of the NS1 protein of influenza A virus

Author keywords

Influenza A virus; NS1A protein; RNA binding domain; effector domain; dimer; resistance; antiviral response

Indexed keywords

AVES; INFLUENZA A VIRUS; INFLUENZAVIRUS A;

EID: 33947210422     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1111/j.1745-7270.2007.00263.x     Document Type: Article
Times cited : (48)

References (41)
  • 1
    • 0035956970 scopus 로고    scopus 로고
    • Sequence of the 1918 pandemic influenza virus nonstructural gene (NS) segment and characterization of recombinant viruses bearing the 1918 NS genes
    • Basler CF, Reid AH, Dybing JK, Janczewski TA, Fanning TG, Zheng H, Salvatore M et al. Sequence of the 1918 pandemic influenza virus nonstructural gene (NS) segment and characterization of recombinant viruses bearing the 1918 NS genes. Proc Natl Acad Sci USA 2001, 98: 2746-2751
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2746-2751
    • Basler, C.F.1    Reid, A.H.2    Dybing, J.K.3    Janczewski, T.A.4    Fanning, T.G.5    Zheng, H.6    Salvatore, M.7
  • 3
    • 0036734038 scopus 로고    scopus 로고
    • Lethal H5N1 influenza viruses escape host anti-viral cytokine responses
    • Seo SH, Hoffmann E, Webster RG. Lethal H5N1 influenza viruses escape host anti-viral cytokine responses. Nat Med 2002, 8: 950-954
    • (2002) Nat Med , vol.8 , pp. 950-954
    • Seo, S.H.1    Hoffmann, E.2    Webster, R.G.3
  • 4
    • 33947287231 scopus 로고    scopus 로고
    • Influenza virus pathogenicity
    • Digard P, Nash AA, Randall RE, eds, 27-30 September, Bergen, Norway. Cambridge: Cambridge University Press
    • Webster RG, Lipatov AS, Hoffmann E. Influenza virus pathogenicity. In: Digard P, Nash AA, Randall RE, eds. SGM Symposium 64: Molecular Pathogenesis of Virus Infections. 27-30 September 2005, Bergen, Norway. Cambridge: Cambridge University Press 2005
    • (2005) SGM Symposium 64: Molecular Pathogenesis of Virus Infections
    • Webster, R.G.1    Lipatov, A.S.2    Hoffmann, E.3
  • 5
    • 3142579867 scopus 로고    scopus 로고
    • Genesis of a highly pathogenic and potentially pandemic H5N1 influenza virus in eastern Asia
    • Li KS, Guan Y, Wang J, Smith GJ, Xu KM, Duan L, Rahardjo AP et al. Genesis of a highly pathogenic and potentially pandemic H5N1 influenza virus in eastern Asia. Nature 2004, 430: 209-213
    • (2004) Nature , vol.430 , pp. 209-213
    • Li, K.S.1    Guan, Y.2    Wang, J.3    Smith, G.J.4    Xu, K.M.5    Duan, L.6    Rahardjo, A.P.7
  • 6
    • 33645958859 scopus 로고    scopus 로고
    • Early diagnosis of avian influenza
    • Lu PS. Early diagnosis of avian influenza. Science 2006, 312: 337
    • (2006) Science , vol.312 , pp. 337
    • Lu, P.S.1
  • 7
    • 33947200230 scopus 로고    scopus 로고
    • Bird flu developments stoke fears
    • Williams N. Bird flu developments stoke fears. Curr Biol 2006, 16: R65-R66
    • (2006) Curr Biol , vol.16
    • Williams, N.1
  • 8
    • 22944457912 scopus 로고    scopus 로고
    • Influenza: Lessons from past pandemics, warnings from current incidents
    • Horimoto T, Kawaoka Y. Influenza: Lessons from past pandemics, warnings from current incidents. Nat Rev Microbiol 2005, 3: 591-600
    • (2005) Nat Rev Microbiol , vol.3 , pp. 591-600
    • Horimoto, T.1    Kawaoka, Y.2
  • 9
    • 33644841402 scopus 로고    scopus 로고
    • Influenza virus virulence and its molecular determinants
    • Noah DL, Krug RM. Influenza virus virulence and its molecular determinants. Adv Virus Res 2005, 65: 121-145
    • (2005) Adv Virus Res , vol.65 , pp. 121-145
    • Noah, D.L.1    Krug, R.M.2
  • 10
    • 19944419799 scopus 로고    scopus 로고
    • Mutations in the NS1 protein of swine influenza virus impair anti-interferon activity and confer attenuation in pigs
    • Solorzano A, Webby RJ, Lager KM, Janke BH, Oarcia-Sastre A, Rieht JA. Mutations in the NS1 protein of swine influenza virus impair anti-interferon activity and confer attenuation in pigs. J Virol 2005, 79: 7535-7543
    • (2005) J Virol , vol.79 , pp. 7535-7543
    • Solorzano, A.1    Webby, R.J.2    Lager, K.M.3    Janke, B.H.4    Oarcia-Sastre, A.5    Rieht, J.A.6
  • 11
    • 2442446901 scopus 로고    scopus 로고
    • The NS1 gene of H5N1 influenza viruses circumvents the host anti-viral cytokine responses
    • Seo SH, Hoffmann E, Webster RG. The NS1 gene of H5N1 influenza viruses circumvents the host anti-viral cytokine responses. Virus Res 2004, 103: 107-113
    • (2004) Virus Res , vol.103 , pp. 107-113
    • Seo, S.H.1    Hoffmann, E.2    Webster, R.G.3
  • 12
    • 20144387310 scopus 로고    scopus 로고
    • Fathogenesis of Hong Kong H5N1 influenza virus NS gene reassortants in mice: The role of cytokines and B- and T-cell responses
    • Lipatov AS, Andreansky S, Webby RJ, Hulse DJ, Rehg JE, Krauss S, Perez DR et al. Fathogenesis of Hong Kong H5N1 influenza virus NS gene reassortants in mice: The role of cytokines and B- and T-cell responses. J Gen Virol 2005, 86(Pt 4): 1121-1130
    • (2005) J Gen Virol , vol.86 , Issue.PART 4 , pp. 1121-1130
    • Lipatov, A.S.1    Andreansky, S.2    Webby, R.J.3    Hulse, D.J.4    Rehg, J.E.5    Krauss, S.6    Perez, D.R.7
  • 14
    • 0037565268 scopus 로고    scopus 로고
    • Intracellular warfare between human influenza viruses and human cells: The roles of the viral NS1 protein
    • Krug RM, Yuan W, Noah DL, Latham AG. Intracellular warfare between human influenza viruses and human cells: The roles of the viral NS1 protein. Virology 2003, 309: 181-189
    • (2003) Virology , vol.309 , pp. 181-189
    • Krug, R.M.1    Yuan, W.2    Noah, D.L.3    Latham, A.G.4
  • 15
    • 0036891842 scopus 로고    scopus 로고
    • Functional replacement of the carboxy-terminal two-thirds of the influenza A virus NS1 protein with short heterologous dimerization domains
    • Wang X, Basler CF, Williams BR, Silverman RH, Palese P, Garcia-Sastre A. Functional replacement of the carboxy-terminal two-thirds of the influenza A virus NS1 protein with short heterologous dimerization domains. J Virol 2002, 76: 12951-12962
    • (2002) J Virol , vol.76 , pp. 12951-12962
    • Wang, X.1    Basler, C.F.2    Williams, B.R.3    Silverman, R.H.4    Palese, P.5    Garcia-Sastre, A.6
  • 16
    • 33744925682 scopus 로고    scopus 로고
    • X-ray structure of influenza virus NS1 effector domain
    • Bornholdt ZA, Prasad BV. X-ray structure of influenza virus NS1 effector domain. Nat Struct Mol Biol 2006, 13: 559-560
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 559-560
    • Bornholdt, Z.A.1    Prasad, B.V.2
  • 17
    • 0035042067 scopus 로고    scopus 로고
    • Influenza A virus NEP (NS2 protein) downregulates RNA synthesis of model template RNAs
    • Bullido R, Gomez-Puertas P, Saiz MJ, Portela A. Influenza A virus NEP (NS2 protein) downregulates RNA synthesis of model template RNAs. J Virol 2001, 75: 4912-4917
    • (2001) J Virol , vol.75 , pp. 4912-4917
    • Bullido, R.1    Gomez-Puertas, P.2    Saiz, M.J.3    Portela, A.4
  • 19
    • 0029400032 scopus 로고
    • An amino-terminal polypeptide fragment of the influenza virus NS1 protein possesses specific RNA-binding activity and largely helical backbone structure
    • Qian XY, Chien CY, Lu Y, Montelione GT, Krug RM. An amino-terminal polypeptide fragment of the influenza virus NS1 protein possesses specific RNA-binding activity and largely helical backbone structure. RNA 1995, 1: 948-956
    • (1995) RNA , vol.1 , pp. 948-956
    • Qian, X.Y.1    Chien, C.Y.2    Lu, Y.3    Montelione, G.T.4    Krug, R.M.5
  • 20
    • 1242307789 scopus 로고    scopus 로고
    • Biophysical characterization of the complex between double-stranded RNA and the N-terminal domain of the NS1 protein from influenza A virus: Evidence for a novel RNA-binding mode
    • Chien CY, Xu Y, Xiao R, Aramini JM, Sahasrabudhe PV, Krug RM, Montelione GT. Biophysical characterization of the complex between double-stranded RNA and the N-terminal domain of the NS1 protein from influenza A virus: Evidence for a novel RNA-binding mode. Biochemistry 2004, 43: 1950-1962
    • (2004) Biochemistry , vol.43 , pp. 1950-1962
    • Chien, C.Y.1    Xu, Y.2    Xiao, R.3    Aramini, J.M.4    Sahasrabudhe, P.V.5    Krug, R.M.6    Montelione, G.T.7
  • 21
    • 0032995665 scopus 로고    scopus 로고
    • RNA binding by the novel helical domain of the influenza virus NS1 protein requires its dimer structure and a small number of specific basic amino acids
    • Wang W, Riedel K, Lynch P, Chien CY, Montelione GT, Krug RM. RNA binding by the novel helical domain of the influenza virus NS1 protein requires its dimer structure and a small number of specific basic amino acids. RNA 1999, 5: 195-205
    • (1999) RNA , vol.5 , pp. 195-205
    • Wang, W.1    Riedel, K.2    Lynch, P.3    Chien, C.Y.4    Montelione, G.T.5    Krug, R.M.6
  • 23
    • 0028847292 scopus 로고
    • Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase thatphosphorylates the elF-2 translation initiation factor
    • Lu Y, Wambach M, Katze MG, Krug RM. Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase thatphosphorylates the elF-2 translation initiation factor. Virology 1995, 214: 222-228
    • (1995) Virology , vol.214 , pp. 222-228
    • Lu, Y.1    Wambach, M.2    Katze, M.G.3    Krug, R.M.4
  • 24
    • 0032980412 scopus 로고    scopus 로고
    • Mutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cells
    • Hatada E, Saito S, Fukuda R. Mutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cells. J Virol 1999, 73: 2425-2433
    • (1999) J Virol , vol.73 , pp. 2425-2433
    • Hatada, E.1    Saito, S.2    Fukuda, R.3
  • 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 JY, Krug RM, Sen GC. Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA. Virology 2006, 349: 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
    • 0345167006 scopus 로고    scopus 로고
    • A recombinant influenza A virus expressing an RNA-binding-defective NS 1 protein induces high levels of beta interferon and is attenuated in mice
    • Donelan NR, Basler CF, Garcia-Sastre A. A recombinant influenza A virus expressing an RNA-binding-defective NS 1 protein induces high levels of beta interferon and is attenuated in mice. J Virol 2003, 77: 13257-13266
    • (2003) J Virol , vol.77 , pp. 13257-13266
    • Donelan, N.R.1    Basler, C.F.2    Garcia-Sastre, A.3
  • 27
    • 0034466776 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein prevents activation of NF-κB and induction of alpha/beta Interferon
    • Wang X, Li M, Zheng H, Muster T, Palese P, Beg AA, Garcia-Sastre A. Influenza A virus NS1 protein prevents activation of NF-κB and induction of alpha/beta Interferon. J Virol 2000, 74: 11566-11573
    • (2000) J Virol , vol.74 , pp. 11566-11573
    • Wang, X.1    Li, M.2    Zheng, H.3    Muster, T.4    Palese, P.5    Beg, A.A.6    Garcia-Sastre, A.7
  • 28
    • 33646478272 scopus 로고    scopus 로고
    • The primary function of RNA binding by the influenza A virus NS1 protein in infected cells: Inhibiting the 2′-5′ oligo (A) synthetase/ RNase L pathway
    • Min JY, Krug RM. The primary function of RNA binding by the influenza A virus NS1 protein in infected cells: Inhibiting the 2′-5′ oligo (A) synthetase/ RNase L pathway. Proc Natl Acad Sci USA 2006, 103: 7100-7105
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7100-7105
    • Min, J.Y.1    Krug, R.M.2
  • 29
    • 11444262203 scopus 로고    scopus 로고
    • Influenza A mutant viruses with altered NS1 protein function provoke caspase-1 activation in primary human macrophages, resulting in fast apoptosis and release of high levels of interleukins 1β and 18
    • Stasakova J, Ferko B, Kittel C, Sereinig S, Romanova J, Katinger H, Egorov A. Influenza A mutant viruses with altered NS1 protein function provoke caspase-1 activation in primary human macrophages, resulting in fast apoptosis and release of high levels of interleukins 1β and 18. J Gen Virol 2005, 86: 185-195
    • (2005) J Gen Virol , vol.86 , pp. 185-195
    • Stasakova, J.1    Ferko, B.2    Kittel, C.3    Sereinig, S.4    Romanova, J.5    Katinger, H.6    Egorov, A.7
  • 30
    • 0031985445 scopus 로고    scopus 로고
    • U6atac snRNA, the highly divergent counterpart of U6 snRNA, is the specific target that mediates inhibition of AT-AC splicing by the influenza virus NS1 protein
    • Wang W, Krug RM. U6atac snRNA, the highly divergent counterpart of U6 snRNA, is the specific target that mediates inhibition of AT-AC splicing by the influenza virus NS1 protein. RNA 1998, 4: 55-64
    • (1998) RNA , vol.4 , pp. 55-64
    • Wang, W.1    Krug, R.M.2
  • 31
    • 0346121589 scopus 로고    scopus 로고
    • PABP1 and eIF4GI associate with influenza virus NS1 protein in viral mRNA translation initiation complexes
    • Burgui I, Aragon T, Ortin J, Nieto A. PABP1 and eIF4GI associate with influenza virus NS1 protein in viral mRNA translation initiation complexes. J Gen Virol 2003, 84: 3263-3274
    • (2003) J Gen Virol , vol.84 , pp. 3263-3274
    • Burgui, I.1    Aragon, T.2    Ortin, J.3    Nieto, A.4
  • 32
  • 33
    • 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. 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 2003, 307: 386-395
    • (2003) Virology , vol.307 , pp. 386-395
    • Noah, D.L.1    Twu, K.Y.2    Krug, R.M.3
  • 34
    • 33645792617 scopus 로고    scopus 로고
    • The CPSF30 binding site on the NS1A protein of influenza A virus is a potential antiviral target
    • Twu KY, Noah DL, Rao P, Kuo RL, Krug RM. The CPSF30 binding site on the NS1A protein of influenza A virus is a potential antiviral target. J Virol 2006, 80: 3957-3965
    • (2006) J Virol , vol.80 , pp. 3957-3965
    • Twu, K.Y.1    Noah, D.L.2    Rao, P.3    Kuo, R.L.4    Krug, R.M.5
  • 35
    • 0034743629 scopus 로고    scopus 로고
    • The 3 -end-processing factor CPSF is required for the splicing of single-intron pre-mRNAs in vivo
    • Li Y, Chen ZY, Wang W, Baker CC, Krug RM. The 3 -end-processing factor CPSF is required for the splicing of single-intron pre-mRNAs in vivo. RNA 2001, 7: 920-931
    • (2001) RNA , vol.7 , pp. 920-931
    • Li, Y.1    Chen, Z.Y.2    Wang, W.3    Baker, C.C.4    Krug, R.M.5
  • 36
    • 0033560753 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3 -end processing machinery
    • Chen Z, Li Y, Krug RM. Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3 -end processing machinery. EMBO J 1999, 18: 2273-2283
    • (1999) EMBO J , vol.18 , pp. 2273-2283
    • Chen, Z.1    Li, Y.2    Krug, R.M.3
  • 37
    • 10744225684 scopus 로고    scopus 로고
    • Interferon antagonist proteins of influenza and vaccinia viruses are suppressors of RNA silencing
    • Li WX, Li H, Lu R, Li F, Dus M, Atkinson P, Brydon EW et al. Interferon antagonist proteins of influenza and vaccinia viruses are suppressors of RNA silencing. Proc Natl Acad Sci USA 2004, 101: 1350-1355
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1350-1355
    • Li, W.X.1    Li, H.2    Lu, R.3    Li, F.4    Dus, M.5    Atkinson, P.6    Brydon, E.W.7
  • 38
    • 2442426044 scopus 로고    scopus 로고
    • Characterization of NS1 gene of influenza A virus in southern China
    • Zhang ZZ, Duan L, Li KS. Characterization of NS1 gene of influenza A virus in southern China. Prog Biochem Biophys 2004, 31: 237-243
    • (2004) Prog Biochem Biophys , vol.31 , pp. 237-243
    • Zhang, Z.Z.1    Duan, L.2    Li, K.S.3
  • 39
    • 1842536901 scopus 로고    scopus 로고
    • Defective RNA replication and late gene expression in temperature-sensitive influenza viruses expressing deleted forms of the NS1 protein
    • Falcon AM, Marion RM, Zurcher T, Gomez P, Portela A, Nieto A, Ortin J. Defective RNA replication and late gene expression in temperature-sensitive influenza viruses expressing deleted forms of the NS1 protein. J Virol 2004, 78: 3880-3888
    • (2004) J Virol , vol.78 , pp. 3880-3888
    • Falcon, A.M.1    Marion, R.M.2    Zurcher, T.3    Gomez, P.4    Portela, A.5    Nieto, A.6    Ortin, J.7
  • 40
    • 26244458739 scopus 로고    scopus 로고
    • Attenuation and immunogenicity in mice of temperature-sensitive influenza viruses expressing truncated NS1 proteins
    • Falcon AM, Fernandez-Sesma A, Nakaya Y, Moran TM, Ortin J, Garcia-Sastre A. Attenuation and immunogenicity in mice of temperature-sensitive influenza viruses expressing truncated NS1 proteins. J Gen Virol 2005, 86: 2817-2821
    • (2005) J Gen Virol , vol.86 , pp. 2817-2821
    • Falcon, A.M.1    Fernandez-Sesma, A.2    Nakaya, Y.3    Moran, T.M.4    Ortin, J.5    Garcia-Sastre, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.