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Volumn 7, Issue 5, 2012, Pages

Influenza polymerase activity correlates with the strength of interaction between nucleoprotein and PB2 through the host-specific residue K/E627

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; LYSINE; NUCLEOPROTEIN; PROTEIN PA; PROTEIN PB1; PROTEIN PB2; RIBONUCLEOPROTEIN; RNA DIRECTED RNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 84860526518     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0036415     Document Type: Article
Times cited : (44)

References (44)
  • 1
    • 31344448218 scopus 로고    scopus 로고
    • Influenza pandemics of the 20th century
    • Kilbourne ED, (2006) Influenza pandemics of the 20th century. Emerg Infect Dis 12: 9-14.
    • (2006) Emerg Infect Dis , vol.12 , pp. 9-14
    • Kilbourne, E.D.1
  • 2
    • 71149117904 scopus 로고    scopus 로고
    • Pandemic (H1N1) 2009 - update 112
    • World Health Organization, Available:. Accessed 12 November 2012
    • World Health Organization (2010) Pandemic (H1N1) 2009 - update 112. Available: http://www.who.int/csr/don/2010_08_06/en/index.html. Accessed 12 November 2012.
    • (2010)
  • 3
    • 0032515589 scopus 로고    scopus 로고
    • Clinical features and rapid viral diagnosis of human disease associated with avian influenza A H5N1 virus
    • Yuen KY, Chan PK, Peiris M, Tsang DN, Que TL, et al. (1998) Clinical features and rapid viral diagnosis of human disease associated with avian influenza A H5N1 virus. Lancet 351: 467-471.
    • (1998) Lancet , vol.351 , pp. 467-471
    • Yuen, K.Y.1    Chan, P.K.2    Peiris, M.3    Tsang, D.N.4    Que, T.L.5
  • 4
    • 33645421057 scopus 로고    scopus 로고
    • Cumulative Number of Confirmed Human Cases of Avian Influenza A/(H5N1) Reported to WHO
    • World Health Organization, Available: Accessed 12 April 2012
    • World Health Organization (2012) Cumulative Number of Confirmed Human Cases of Avian Influenza A/(H5N1) Reported to WHO. Available: http://www.who.int/influenza/human_animal_interface/H5N1_cumulative_table_archives/en/index.html Accessed 12 April 2012.
    • (2012)
  • 5
    • 79960384534 scopus 로고    scopus 로고
    • Influenza A viruses: new research developments
    • Medina RA, Garcia-Sastre A, (2011) Influenza A viruses: new research developments. Nat Rev Microbiol 9: 590-603.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 590-603
    • Medina, R.A.1    Garcia-Sastre, A.2
  • 6
    • 0024990401 scopus 로고
    • Determination of influenza virus proteins required for genome replication
    • Huang TS, Palese P, Krystal M, (1990) Determination of influenza virus proteins required for genome replication. J Virol 64: 5669-5673.
    • (1990) J Virol , vol.64 , pp. 5669-5673
    • Huang, T.S.1    Palese, P.2    Krystal, M.3
  • 7
    • 0019394947 scopus 로고
    • A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription
    • Plotch SJ, Bouloy M, Ulmanen I, Krug RM, (1981) A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription. Cell 23: 847-858.
    • (1981) Cell , vol.23 , pp. 847-858
    • Plotch, S.J.1    Bouloy, M.2    Ulmanen, I.3    Krug, R.M.4
  • 9
    • 67249130012 scopus 로고    scopus 로고
    • The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit
    • Dias A, Bouvier D, Crepin T, McCarthy AA, Hart DJ, et al. (2009) The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit. Nature 458: 914-918.
    • (2009) Nature , vol.458 , pp. 914-918
    • Dias, A.1    Bouvier, D.2    Crepin, T.3    McCarthy, A.A.4    Hart, D.J.5
  • 10
    • 67249100913 scopus 로고    scopus 로고
    • Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site
    • Yuan P, Bartlam M, Lou Z, Chen S, Zhou J, et al. (2009) Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site. Nature 458: 909-913.
    • (2009) Nature , vol.458 , pp. 909-913
    • Yuan, P.1    Bartlam, M.2    Lou, Z.3    Chen, S.4    Zhou, J.5
  • 11
    • 0028176691 scopus 로고
    • Rift Valley fever virus L segment: correction of the sequence and possible functional role of newly identified regions conserved in RNA-dependent polymerases
    • Muller R, Poch O, Delarue M, Bishop DH, Bouloy M, (1994) Rift Valley fever virus L segment: correction of the sequence and possible functional role of newly identified regions conserved in RNA-dependent polymerases. J Gen Virol 75 (Pt 6): 1345-1352.
    • (1994) J Gen Virol , vol.75 , Issue.Pt 6 , pp. 1345-1352
    • Muller, R.1    Poch, O.2    Delarue, M.3    Bishop, D.H.4    Bouloy, M.5
  • 12
    • 0024784519 scopus 로고
    • Identification of four conserved motifs among the RNA-dependent polymerase encoding elements
    • Poch O, Sauvaget I, Delarue M, Tordo N, (1989) Identification of four conserved motifs among the RNA-dependent polymerase encoding elements. Embo J 8: 3867-3874.
    • (1989) Embo J , vol.8 , pp. 3867-3874
    • Poch, O.1    Sauvaget, I.2    Delarue, M.3    Tordo, N.4
  • 13
    • 0036210827 scopus 로고    scopus 로고
    • The influenza virus nucleoprotein: a multifunctional RNA-binding protein pivotal to virus replication
    • Portela A, Digard P, (2002) The influenza virus nucleoprotein: a multifunctional RNA-binding protein pivotal to virus replication. J Gen Virol 83: 723-734.
    • (2002) J Gen Virol , vol.83 , pp. 723-734
    • Portela, A.1    Digard, P.2
  • 14
    • 31444441789 scopus 로고    scopus 로고
    • Architecture of ribonucleoprotein complexes in influenza A virus particles
    • Noda T, Sagara H, Yen A, Takada A, Kida H, et al. (2006) Architecture of ribonucleoprotein complexes in influenza A virus particles. Nature 439: 490-492.
    • (2006) Nature , vol.439 , pp. 490-492
    • Noda, T.1    Sagara, H.2    Yen, A.3    Takada, A.4    Kida, H.5
  • 15
    • 0015414910 scopus 로고
    • Structure of the ribonucleoprotein of influenza virus
    • Compans RW, Content J, Duesberg PH, (1972) Structure of the ribonucleoprotein of influenza virus. J Virol 10: 795-800.
    • (1972) J Virol , vol.10 , pp. 795-800
    • Compans, R.W.1    Content, J.2    Duesberg, P.H.3
  • 16
    • 0014591650 scopus 로고
    • Isolation and characterization of the ribonucleoprotein of influenza virus
    • Pons MW, Schulze IT, Hirst GK, Hauser R, (1969) Isolation and characterization of the ribonucleoprotein of influenza virus. Virology 39: 250-259.
    • (1969) Virology , vol.39 , pp. 250-259
    • Pons, M.W.1    Schulze, I.T.2    Hirst, G.K.3    Hauser, R.4
  • 17
    • 0035033091 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of a recombinant influenza virus ribonucleoprotein particle
    • Martin-Benito J, Area E, Ortega J, Llorca O, Valpuesta JM, et al. (2001) Three-dimensional reconstruction of a recombinant influenza virus ribonucleoprotein particle. EMBO Rep 2: 313-317.
    • (2001) EMBO Rep , vol.2 , pp. 313-317
    • Martin-Benito, J.1    Area, E.2    Ortega, J.3    Llorca, O.4    Valpuesta, J.M.5
  • 19
    • 67650917906 scopus 로고    scopus 로고
    • The structure of a biologically active influenza virus ribonucleoprotein complex
    • Coloma R, Valpuesta JM, Arranz R, Carrascosa JL, Ortin J, et al. (2009) The structure of a biologically active influenza virus ribonucleoprotein complex. PLoS Pathog 5: e1000491.
    • (2009) PLoS Pathog , vol.5
    • Coloma, R.1    Valpuesta, J.M.2    Arranz, R.3    Carrascosa, J.L.4    Ortin, J.5
  • 20
    • 77956536783 scopus 로고    scopus 로고
    • Influenza A virus polymerase: structural insights into replication and host adaptation mechanisms
    • Boivin S, Cusack S, Ruigrok RW, Hart DJ, (2010) Influenza A virus polymerase: structural insights into replication and host adaptation mechanisms. J Biol Chem 285: 28411-28417.
    • (2010) J Biol Chem , vol.285 , pp. 28411-28417
    • Boivin, S.1    Cusack, S.2    Ruigrok, R.W.3    Hart, D.J.4
  • 21
    • 54049146687 scopus 로고    scopus 로고
    • Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design
    • Ng AK, Zhang H, Tan K, Li Z, Liu JH, et al. (2008) Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design. Faseb J 22: 3638-3647.
    • (2008) Faseb J , vol.22 , pp. 3638-3647
    • Ng, A.K.1    Zhang, H.2    Tan, K.3    Li, Z.4    Liu, J.H.5
  • 22
    • 33845890539 scopus 로고    scopus 로고
    • The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA
    • Ye Q, Krug RM, Tao YJ, (2006) The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA. Nature 444: 1078-1082.
    • (2006) Nature , vol.444 , pp. 1078-1082
    • Ye, Q.1    Krug, R.M.2    Tao, Y.J.3
  • 23
    • 50849137828 scopus 로고    scopus 로고
    • Host determinant residue lysine 627 lies on the surface of a discrete, folded domain of influenza virus polymerase PB2 subunit
    • Tarendeau F, Crepin T, Guilligay D, Ruigrok RW, Cusack S, et al. (2008) Host determinant residue lysine 627 lies on the surface of a discrete, folded domain of influenza virus polymerase PB2 subunit. PLoS Pathog 4: e1000136.
    • (2008) PLoS Pathog , vol.4
    • Tarendeau, F.1    Crepin, T.2    Guilligay, D.3    Ruigrok, R.W.4    Cusack, S.5
  • 24
    • 65449163086 scopus 로고    scopus 로고
    • Structural basis of the influenza A virus RNA polymerase PB2 RNA-binding domain containing the pathogenicity-determinant lysine 627 residue
    • Kuzuhara T, Kise D, Yoshida H, Horita T, Murazaki Y, et al. (2009) Structural basis of the influenza A virus RNA polymerase PB2 RNA-binding domain containing the pathogenicity-determinant lysine 627 residue. J Biol Chem 284: 6855-6860.
    • (2009) J Biol Chem , vol.284 , pp. 6855-6860
    • Kuzuhara, T.1    Kise, D.2    Yoshida, H.3    Horita, T.4    Murazaki, Y.5
  • 26
    • 0027468737 scopus 로고
    • A single amino acid in the PB2 gene of influenza A virus is a determinant of host range
    • Subbarao EK, London W, Murphy BR, (1993) A single amino acid in the PB2 gene of influenza A virus is a determinant of host range. J Virol 67: 1761-1764.
    • (1993) J Virol , vol.67 , pp. 1761-1764
    • Subbarao, E.K.1    London, W.2    Murphy, B.R.3
  • 27
    • 0034054170 scopus 로고    scopus 로고
    • Genetic analysis of the compatibility between polymerase proteins from human and avian strains of influenza A viruses
    • Naffakh N, Massin P, Escriou N, Crescenzo-Chaigne B, van der Werf S, (2000) Genetic analysis of the compatibility between polymerase proteins from human and avian strains of influenza A viruses. J Gen Virol 81: 1283-1291.
    • (2000) J Gen Virol , vol.81 , pp. 1283-1291
    • Naffakh, N.1    Massin, P.2    Escriou, N.3    Crescenzo-Chaigne, B.4    van der Werf, S.5
  • 28
    • 75849136881 scopus 로고    scopus 로고
    • Adaptive strategies of the influenza virus polymerase for replication in humans
    • Mehle A, Doudna JA, (2009) Adaptive strategies of the influenza virus polymerase for replication in humans. Proc Natl Acad Sci U S A 106: 21312-21316.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 21312-21316
    • Mehle, A.1    Doudna, J.A.2
  • 29
    • 43149095780 scopus 로고    scopus 로고
    • Identification of human-to-human transmissibility factors in PB2 proteins of influenza A by large-scale mutual information analysis
    • Miotto O, Heiny A, Tan TW, August JT, Brusic V, (2008) Identification of human-to-human transmissibility factors in PB2 proteins of influenza A by large-scale mutual information analysis. BMC Bioinformatics 9 (Suppl 1): S18.
    • (2008) BMC Bioinformatics , vol.9 , Issue.SUPPL. 1
    • Miotto, O.1    Heiny, A.2    Tan, T.W.3    August, J.T.4    Brusic, V.5
  • 30
    • 48649085166 scopus 로고    scopus 로고
    • An inhibitory activity in human cells restricts the function of an avian-like influenza virus polymerase
    • Mehle A, Doudna JA, (2008) An inhibitory activity in human cells restricts the function of an avian-like influenza virus polymerase. Cell Host Microbe 4: 111-122.
    • (2008) Cell Host Microbe , vol.4 , pp. 111-122
    • Mehle, A.1    Doudna, J.A.2
  • 31
    • 77956839458 scopus 로고    scopus 로고
    • Evidence for avian and human host cell factors that affect the activity of influenza virus polymerase
    • Moncorge O, Mura M, Barclay WS, (2010) Evidence for avian and human host cell factors that affect the activity of influenza virus polymerase. J Virol 84: 9978-9986.
    • (2010) J Virol , vol.84 , pp. 9978-9986
    • Moncorge, O.1    Mura, M.2    Barclay, W.S.3
  • 32
    • 0035823083 scopus 로고    scopus 로고
    • Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses
    • Hatta M, Gao P, Halfmann P, Kawaoka Y, (2001) Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses. Science 293: 1840-1842.
    • (2001) Science , vol.293 , pp. 1840-1842
    • Hatta, M.1    Gao, P.2    Halfmann, P.3    Kawaoka, Y.4
  • 33
    • 33751438303 scopus 로고    scopus 로고
    • Recent H5N1 avian influenza A virus increases rapidly in virulence to mice after a single passage in mice
    • Mase M, Tanimura N, Imada T, Okamatsu M, Tsukamoto K, et al. (2006) Recent H5N1 avian influenza A virus increases rapidly in virulence to mice after a single passage in mice. J Gen Virol 87: 3655-3659.
    • (2006) J Gen Virol , vol.87 , pp. 3655-3659
    • Mase, M.1    Tanimura, N.2    Imada, T.3    Okamatsu, M.4    Tsukamoto, K.5
  • 34
    • 0035026051 scopus 로고    scopus 로고
    • Residue 627 of PB2 is a determinant of cold sensitivity in RNA replication of avian influenza viruses
    • Massin P, van der Werf S, Naffakh N, (2001) Residue 627 of PB2 is a determinant of cold sensitivity in RNA replication of avian influenza viruses. J Virol 75: 5398-5404.
    • (2001) J Virol , vol.75 , pp. 5398-5404
    • Massin, P.1    van der Werf, S.2    Naffakh, N.3
  • 35
    • 0031778876 scopus 로고    scopus 로고
    • Influenza virus nucleoprotein interacts with influenza virus polymerase proteins
    • Biswas SK, Boutz PL, Nayak DP, (1998) Influenza virus nucleoprotein interacts with influenza virus polymerase proteins. J Virol 72: 5493-5501.
    • (1998) J Virol , vol.72 , pp. 5493-5501
    • Biswas, S.K.1    Boutz, P.L.2    Nayak, D.P.3
  • 36
    • 0032837329 scopus 로고    scopus 로고
    • Temperature-sensitive lesions in two influenza A viruses defective for replicative transcription disrupt RNA binding by the nucleoprotein
    • Medcalf L, Poole E, Elton D, Digard P, (1999) Temperature-sensitive lesions in two influenza A viruses defective for replicative transcription disrupt RNA binding by the nucleoprotein. J Virol 73: 7349-7356.
    • (1999) J Virol , vol.73 , pp. 7349-7356
    • Medcalf, L.1    Poole, E.2    Elton, D.3    Digard, P.4
  • 37
    • 1642325300 scopus 로고    scopus 로고
    • Functional domains of the influenza A virus PB2 protein: identification of NP- and PB1-binding sites
    • Poole E, Elton D, Medcalf L, Digard P, (2004) Functional domains of the influenza A virus PB2 protein: identification of NP- and PB1-binding sites. Virology 321: 120-133.
    • (2004) Virology , vol.321 , pp. 120-133
    • Poole, E.1    Elton, D.2    Medcalf, L.3    Digard, P.4
  • 38
    • 34247565021 scopus 로고    scopus 로고
    • Host-range determinants on the PB2 protein of influenza A viruses control the interaction between the viral polymerase and nucleoprotein in human cells
    • Labadie K, Dos Santos Afonso E, Rameix-Welti MA, van der Werf S, Naffakh N, (2007) Host-range determinants on the PB2 protein of influenza A viruses control the interaction between the viral polymerase and nucleoprotein in human cells. Virology 362: 271-282.
    • (2007) Virology , vol.362 , pp. 271-282
    • Labadie, K.1    Dos Santos Afonso, E.2    Rameix-Welti, M.A.3    van der Werf, S.4    Naffakh, N.5
  • 39
    • 59749097063 scopus 로고    scopus 로고
    • Avian Influenza A virus polymerase association with nucleoprotein, but not polymerase assembly, is impaired in human cells during the course of infection
    • Rameix-Welti MA, Tomoiu A, Dos Santos Afonso E, van der Werf S, Naffakh N, (2009) Avian Influenza A virus polymerase association with nucleoprotein, but not polymerase assembly, is impaired in human cells during the course of infection. J Virol 83: 1320-1331.
    • (2009) J Virol , vol.83 , pp. 1320-1331
    • Rameix-Welti, M.A.1    Tomoiu, A.2    Dos Santos Afonso, E.3    van der Werf, S.4    Naffakh, N.5
  • 40
    • 66249092809 scopus 로고    scopus 로고
    • Full factorial analysis of mammalian and avian influenza polymerase subunits suggests a role of an efficient polymerase for virus adaptation
    • Li OT, Chan MC, Leung CS, Chan RW, Guan Y, et al. (2009) Full factorial analysis of mammalian and avian influenza polymerase subunits suggests a role of an efficient polymerase for virus adaptation. PLoS One 4: e5658.
    • (2009) PLoS One , vol.4
    • Li, O.T.1    Chan, M.C.2    Leung, C.S.3    Chan, R.W.4    Guan, Y.5
  • 42
    • 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, Crow M, Mingay LJ, Deng T, Sharps J, et al. (2002) 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) J Virol , vol.76 , pp. 8989-9001
    • Fodor, E.1    Crow, M.2    Mingay, L.J.3    Deng, T.4    Sharps, J.5
  • 43
    • 4143153932 scopus 로고    scopus 로고
    • Model suggesting that replication of influenza virus is regulated by stabilization of replicative intermediates
    • Vreede FT, Jung TE, Brownlee GG, (2004) Model suggesting that replication of influenza virus is regulated by stabilization of replicative intermediates. J Virol 78: 9568-9572.
    • (2004) J Virol , vol.78 , pp. 9568-9572
    • Vreede, F.T.1    Jung, T.E.2    Brownlee, G.G.3
  • 44
    • 77953794395 scopus 로고    scopus 로고
    • Functional analysis of the influenza virus H5N1 nucleoprotein tail loop reveals amino acids that are crucial for oligomerization and ribonucleoprotein activities
    • Chan WH, Ng AK, Robb NC, Lam MK, Chan PK, et al. Functional analysis of the influenza virus H5N1 nucleoprotein tail loop reveals amino acids that are crucial for oligomerization and ribonucleoprotein activities. J Virol 84: 7337-7345.
    • J Virol , vol.84 , pp. 7337-7345
    • Chan, W.H.1    Ng, A.K.2    Robb, N.C.3    Lam, M.K.4    Chan, P.K.5


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