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Volumn 22, Issue 10, 2008, Pages 3638-3647

Structure of the influenza virus A H5N1 nucleoprotein: Implications for RNA binding, oligomerization, and vaccine design

Author keywords

Crystal structure; Protein RNA interaction; Trimerization

Indexed keywords

VIRUS NUCLEOPROTEIN; ANTIVIRUS AGENT; CORE PROTEIN; INFLUENZA VACCINE; NUCLEOPROTEIN; RNA;

EID: 54049146687     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.08-112110     Document Type: Article
Times cited : (182)

References (40)
  • 1
    • 0036514779 scopus 로고    scopus 로고
    • Updating the accounts: Global mortality of the 1918-1920 "Spanish" influenza pandemic
    • Johnson, N. P., and Mueller, J. (2002) Updating the accounts: global mortality of the 1918-1920 "Spanish" influenza pandemic. Bull. Hist. Med. 76, 105-115
    • (2002) Bull. Hist. Med , vol.76 , pp. 105-115
    • Johnson, N.P.1    Mueller, J.2
  • 2
    • 31144473845 scopus 로고    scopus 로고
    • Avian influenza. WHO proposes plan to stop pandemic in its tracks
    • Normile, D. (2006) Avian influenza. WHO proposes plan to stop pandemic in its tracks. Science 311, 315-316
    • (2006) Science , vol.311 , pp. 315-316
    • Normile, D.1
  • 3
    • 27644544183 scopus 로고    scopus 로고
    • Protection against multiple influenza A subtypes by vaccination with highly conserved nucleoprotein
    • Epstein, S. L., Kong, W. P., Misplon, J. A., Lo, C. Y., Tumpey, T. M., Xu, L., and Nabel, G. J. (2005) Protection against multiple influenza A subtypes by vaccination with highly conserved nucleoprotein. Vaccine 23, 5404-5410
    • (2005) Vaccine , vol.23 , pp. 5404-5410
    • Epstein, S.L.1    Kong, W.P.2    Misplon, J.A.3    Lo, C.Y.4    Tumpey, T.M.5    Xu, L.6    Nabel, G.J.7
  • 4
    • 0027471186 scopus 로고
    • Analysis of the evolution and variation of the human influenza A virus nucleoprotein gene from 1933 to 1990
    • Shu, L. L., Bean, W. J., and Webster, R. G. (1993) Analysis of the evolution and variation of the human influenza A virus nucleoprotein gene from 1933 to 1990. J. Virol. 67, 2723-2729
    • (1993) J. Virol , vol.67 , pp. 2723-2729
    • Shu, L.L.1    Bean, W.J.2    Webster, R.G.3
  • 6
    • 0015090930 scopus 로고
    • Transcription of the influenza ribonucleic acid genome by a virion polymerase. I. Optimal conditions for in vitro activity of the ribonucleic acid-dependent ribonucleic acid polymerase
    • Bishop, D. H., Obijeski, J. F., and Simpson, R. W. (1971) Transcription of the influenza ribonucleic acid genome by a virion polymerase. I. Optimal conditions for in vitro activity of the ribonucleic acid-dependent ribonucleic acid polymerase. J. Virol. 8, 66-73
    • (1971) J. Virol , vol.8 , pp. 66-73
    • Bishop, D.H.1    Obijeski, J.F.2    Simpson, R.W.3
  • 7
    • 0036210827 scopus 로고    scopus 로고
    • The influenza virus nucleoprotein: A multifunctional RNA-binding protein pivotal to virus replication
    • Portela, A., and 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
  • 8
    • 0025970779 scopus 로고
    • Influenza A virus in vitro transcription: Roles of NS1 and NP proteins in regulating RNA synthesis
    • Skorko, R., Summers, D. F., and Galarza, J. M. (1991) Influenza A virus in vitro transcription: roles of NS1 and NP proteins in regulating RNA synthesis. Virology 180, 668-677
    • (1991) Virology , vol.180 , pp. 668-677
    • Skorko, R.1    Summers, D.F.2    Galarza, J.M.3
  • 9
    • 0028131905 scopus 로고
    • Molecular dissection of influenza virus nucleoprotein: Deletion mapping of the RNA binding domain
    • Kobayashi, M., Toyoda, T., Adyshev, D. M., Azuma, Y., and Ishihama, A. (1994) Molecular dissection of influenza virus nucleoprotein: deletion mapping of the RNA binding domain. J. Virol. 68, 8433-8436
    • (1994) J. Virol , vol.68 , pp. 8433-8436
    • Kobayashi, M.1    Toyoda, T.2    Adyshev, D.M.3    Azuma, Y.4    Ishihama, A.5
  • 10
    • 0030246992 scopus 로고    scopus 로고
    • Intracellular oligomerization of influenza virus nucleoprotein
    • Prokudina-Kantorovich, E. N., and Semenova, N. P. (1996) Intracellular oligomerization of influenza virus nucleoprotein. Virology 223, 51-56
    • (1996) Virology , vol.223 , pp. 51-56
    • Prokudina-Kantorovich, E.N.1    Semenova, N.P.2
  • 11
    • 0031778876 scopus 로고    scopus 로고
    • Influenza virus nucleoprotein interacts with influenza virus polymerase proteins
    • Biswas, S. K., Boutz, P. L., and Nayak, D. P. (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
  • 14
    • 33845890539 scopus 로고    scopus 로고
    • The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA
    • Ye, Q., Krug, R. M., and Tao, Y. J. (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
  • 15
    • 2342662152 scopus 로고    scopus 로고
    • Negative staining and image classification - powerful tools in modern electron microscopy
    • Ohi, M., Li, Y., Cheng, Y., and Walz, T. (2004) Negative staining and image classification - powerful tools in modern electron microscopy. Biol. Proced. Online 6, 23-34
    • (2004) Biol. Proced. Online , vol.6 , pp. 23-34
    • Ohi, M.1    Li, Y.2    Cheng, Y.3    Walz, T.4
  • 16
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution - from diffraction images to an initial model in minutes
    • Minor, W., Cymborowski, M., Otwinowski, Z., and Chruszcz, M. (2006) HKL-3000: the integration of data reduction and structure solution - from diffraction images to an initial model in minutes. Acta Crystallogr. D Biol. Crystallogr. 62, 859-866
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 17
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
  • 18
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 20
  • 21
    • 33747863016 scopus 로고    scopus 로고
    • ArchPRED: A template based loop structure prediction server
    • Fernandez-Fuentes, N., Zhai, J., and Fiser, A. (2006) ArchPRED: a template based loop structure prediction server. Nucleic Acids Res. 34, W173-W176
    • (2006) Nucleic Acids Res , vol.34
    • Fernandez-Fuentes, N.1    Zhai, J.2    Fiser, A.3
  • 22
    • 0033587599 scopus 로고    scopus 로고
    • Oligomerization of the influenza virus nucleoprotein: Identification of positive and negative sequence elements
    • Elton, D., Medcalf, E., Bishop, K., and Digard, P. (1999) Oligomerization of the influenza virus nucleoprotein: identification of positive and negative sequence elements. Virology 260, 190-200
    • (1999) Virology , vol.260 , pp. 190-200
    • Elton, D.1    Medcalf, E.2    Bishop, K.3    Digard, P.4
  • 23
    • 1642494835 scopus 로고    scopus 로고
    • Transient disulfide bonds formation in conformational maturation of influenza virus nucleocapsid protein (NP)
    • Prokudina, E. N., Semenova, N. P., Chumakov, V. M., and Rudneva, I. A. (2004) Transient disulfide bonds formation in conformational maturation of influenza virus nucleocapsid protein (NP). Virus Res. 99, 169-175
    • (2004) Virus Res , vol.99 , pp. 169-175
    • Prokudina, E.N.1    Semenova, N.P.2    Chumakov, V.M.3    Rudneva, I.A.4
  • 25
    • 33746516378 scopus 로고    scopus 로고
    • Structure of the vesicular stomatitis virus nucleoprotein-RNA complex
    • Green, T. J., Zhang, X., Wertz, G. W., and Luo, M. (2006) Structure of the vesicular stomatitis virus nucleoprotein-RNA complex. Science 313, 357-360
    • (2006) Science , vol.313 , pp. 357-360
    • Green, T.J.1    Zhang, X.2    Wertz, G.W.3    Luo, M.4
  • 26
    • 35348886782 scopus 로고    scopus 로고
    • Structural comparisons of the nucleoprotein from three negative strand RNA virus families
    • Luo, M., Green, T. J., Zhang, X., Tsao, J., and Qiu, S. (2007) Structural comparisons of the nucleoprotein from three negative strand RNA virus families. Virol. J. 4, 72
    • (2007) Virol. J , vol.4 , pp. 72
    • Luo, M.1    Green, T.J.2    Zhang, X.3    Tsao, J.4    Qiu, S.5
  • 28
    • 0031003878 scopus 로고    scopus 로고
    • Roles of the influenza virus polymerase and nucleoprotein in forming a functional RNP structure
    • Klumpp, K., Ruigrok, R. W., and Baudin, F. (1997) Roles of the influenza virus polymerase and nucleoprotein in forming a functional RNP structure. EMBO J. 16, 1248-1257
    • (1997) EMBO J , vol.16 , pp. 1248-1257
    • Klumpp, K.1    Ruigrok, R.W.2    Baudin, F.3
  • 29
    • 0032854172 scopus 로고    scopus 로고
    • Identification of amino acid residues of influenza virus nucleoprotein essential for RNA binding
    • Elton, D., Medcalf, L., Bishop, K., Harrison, D., and Digard, P. (1999) Identification of amino acid residues of influenza virus nucleoprotein essential for RNA binding. J. Virol. 73, 7357-7367
    • (1999) J. Virol , vol.73 , pp. 7357-7367
    • Elton, D.1    Medcalf, L.2    Bishop, K.3    Harrison, D.4    Digard, P.5
  • 30
    • 0028275669 scopus 로고
    • Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent
    • Baudin, F., Bach, C., Cusack, S., and Ruigrok, R. W. (1994) Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent. EMBO J. 13, 3158-3165
    • (1994) EMBO J , vol.13 , pp. 3158-3165
    • Baudin, F.1    Bach, C.2    Cusack, S.3    Ruigrok, R.W.4
  • 31
    • 0028228459 scopus 로고
    • Sequence-specific binding of the influenza virus RNA polymerase to sequences located at the 5′ ends of the viral RNAs
    • Tiley, L. S., Hagen, M., Matthews, J. T., and Krystal, M. (1994) Sequence-specific binding of the influenza virus RNA polymerase to sequences located at the 5′ ends of the viral RNAs. J. Virol. 68, 5108-5116
    • (1994) J. Virol , vol.68 , pp. 5108-5116
    • Tiley, L.S.1    Hagen, M.2    Matthews, J.T.3    Krystal, M.4
  • 32
    • 17644443084 scopus 로고    scopus 로고
    • Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification
    • Ortega, J., Martin-Benito, J., Zurcher, T., Valpuesta, J. M., Carrascosa, J. L., and Ortin, J. (2000) Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification. J. Virol. 74, 156-163
    • (2000) J. Virol , vol.74 , pp. 156-163
    • Ortega, J.1    Martin-Benito, J.2    Zurcher, T.3    Valpuesta, J.M.4    Carrascosa, J.L.5    Ortin, J.6
  • 34
    • 33846124632 scopus 로고    scopus 로고
    • Evolving strategies for the prevention of influenza infection: Potential for multistrain targeting
    • Livingston, B. D., Higgins, D., and Van Nest, G. (2006) Evolving strategies for the prevention of influenza infection: potential for multistrain targeting. BioDrugs. 20, 335-340
    • (2006) BioDrugs , vol.20 , pp. 335-340
    • Livingston, B.D.1    Higgins, D.2    Van Nest, G.3
  • 35
    • 43949096181 scopus 로고    scopus 로고
    • Cross-recognition of avian H5N1 influenza virus by human cytotoxic T lymphocyte populations directed to human influenza A virus
    • Kreijtz, J. H. C. M., de Mutsert, G., van Baalen, C. A., Fouchier, R. A. M., Osterhaus, A. D. M. E., and Rimmelzwaan, G. F. (2008) Cross-recognition of avian H5N1 influenza virus by human cytotoxic T lymphocyte populations directed to human influenza A virus. J. Virol. 82, 5161-5166
    • (2008) J. Virol , vol.82 , pp. 5161-5166
    • Kreijtz, J.H.C.M.1    de Mutsert, G.2    van Baalen, C.A.3    Fouchier, R.A.M.4    Osterhaus, A.D.M.E.5    Rimmelzwaan, G.F.6
  • 36
    • 41149170727 scopus 로고    scopus 로고
    • Age-associated decline in T cell repertoire diversity leads to holes in the repertoire and impaired immunity to influenza virus
    • Yager, E. J., Ahmed, M., Lanzer, K., Randall, T. D., Woodland, D. L., and Blackman, M. A. (2008) Age-associated decline in T cell repertoire diversity leads to holes in the repertoire and impaired immunity to influenza virus. J. Exp. Med. 205, 711-723
    • (2008) J. Exp. Med , vol.205 , pp. 711-723
    • Yager, E.J.1    Ahmed, M.2    Lanzer, K.3    Randall, T.D.4    Woodland, D.L.5    Blackman, M.A.6
  • 38
    • 33744913792 scopus 로고    scopus 로고
    • The hypervariable immunodominant NP418-426 epitope from the influenza A virus nucleoprotein is recognized by cytotoxic T lymphocytes with high functional avidity
    • Boon, A. C., de Mutsert, G., Fouchier, R. A., Osterhaus, A. D., and Rimmelzwaan, G. F. (2006) The hypervariable immunodominant NP418-426 epitope from the influenza A virus nucleoprotein is recognized by cytotoxic T lymphocytes with high functional avidity. J. Virol. 80, 6024-6032
    • (2006) J. Virol , vol.80 , pp. 6024-6032
    • Boon, A.C.1    de Mutsert, G.2    Fouchier, R.A.3    Osterhaus, A.D.4    Rimmelzwaan, G.F.5
  • 39
    • 2442519025 scopus 로고    scopus 로고
    • Sequence variation in the influenza A virus nucleoprotein associated with escape from cytotoxic T lymphocytes
    • Rimmelzwaan, G. F., Boon, A. C., Voeten, J. T., Berkhoff, E. G., Fouchier, R. A., and Osterhaus, A. D. (2004) Sequence variation in the influenza A virus nucleoprotein associated with escape from cytotoxic T lymphocytes. Virus. Res. 103, 97-100
    • (2004) Virus. Res , vol.103 , pp. 97-100
    • Rimmelzwaan, G.F.1    Boon, A.C.2    Voeten, J.T.3    Berkhoff, E.G.4    Fouchier, R.A.5    Osterhaus, A.D.6
  • 40
    • 40749139110 scopus 로고    scopus 로고
    • Healthy human subjects have CD4 T cells directed against H5N1 influenza virus
    • Roti, M., Yang, J., Berger, D., Huston, L., James, E. A., and Kwok, W. W. (2008) Healthy human subjects have CD4 T cells directed against H5N1 influenza virus. J. Immunol. 180, 1758-1768
    • (2008) J. Immunol , vol.180 , pp. 1758-1768
    • Roti, M.1    Yang, J.2    Berger, D.3    Huston, L.4    James, E.A.5    Kwok, W.W.6


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