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Volumn 4, Issue , 2014, Pages

Structural analysis of H1N1 and H7N9 influenza A virus PA in the absence of PB1

Author keywords

[No Author keywords available]

Indexed keywords

INFLUENZA VIRUS POLYMERASE BASIC PROTEIN 1; PA PROTEIN, INFLUENZA VIRUSES; PROTEIN BINDING; RECOMBINANT PROTEIN; RNA DIRECTED RNA POLYMERASE; VIRAL PROTEIN;

EID: 84905454525     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep05944     Document Type: Article
Times cited : (12)

References (35)
  • 1
    • 79954499474 scopus 로고    scopus 로고
    • The influenza virus RNA synthesis machine: Advances in its structure and function
    • Resa-Infante, P., Jorba, N., Coloma, R. & Ortin, J. The influenza virus RNA synthesis machine: advances in its structure and function. RNA Biol. 8, 207-215 (2011).
    • (2011) RNA Biol. , vol.8 , pp. 207-215
    • Resa-Infante, P.1    Jorba, N.2    Coloma, R.3    Ortin, J.4
  • 2
    • 47649116956 scopus 로고    scopus 로고
    • Host factors for replication and transcription of the influenza virus genome
    • DOI 10.1002/rmv.575
    • Nagata, K., Kawaguchi, A. & Naito, T. Host factors for replication and transcription of the influenza virus genome. Rev. Med. Virol. 18, 247-260 (2008). (Pubitemid 352018848)
    • (2008) Reviews in Medical Virology , vol.18 , Issue.4 , pp. 247-260
    • Nagata, K.1    Kawaguchi, A.2    Naito, T.3
  • 3
    • 0019958063 scopus 로고
    • Sequence analysis of the polymerase 1 gene and the secondary structure prediction of polymerase 1 protein of human influenza virus A/WSN/33
    • Sivasubramanian, N. & Nayak, D. P. Sequence analysis of the polymerase 1 gene and the secondary structure prediction of polymerase 1 protein of human influenza virus A/WSN/33. J. Virol. 44, 321-329 (1982). (Pubitemid 12020924)
    • (1982) Journal of Virology , vol.44 , Issue.1 , pp. 321-329
    • Sivasubramanian, N.1    Nayak, D.P.2
  • 4
    • 0032518374 scopus 로고    scopus 로고
    • A mechanism for all polymerases
    • Steitz, T. A. A mechanism for all polymerases. Nature 391, 231-232 (1998).
    • (1998) Nature , vol.391 , pp. 231-232
    • Steitz, T.A.1
  • 5
    • 84892159576 scopus 로고    scopus 로고
    • The N-terminal region of influenza virus polymerase PB1 adjacent to the PA binding site is involved in replication but not transcription of the viral genome
    • Binh, N. T., Wakai, C., Kawaguchi, A. & Nagata, K. The N-terminal region of influenza virus polymerase PB1 adjacent to the PA binding site is involved in replication but not transcription of the viral genome. Frontiers in Microbiol. 4, 398 (2013).
    • (2013) Frontiers in Microbiol. , vol.4 , pp. 398
    • Binh, N.T.1    Wakai, C.2    Kawaguchi, A.3    Nagata, K.4
  • 6
    • 64049093748 scopus 로고    scopus 로고
    • Detection and characterization of influenza A virus PA-PB2 interaction through a bimolecular fluorescence complementation assay
    • Hemerka, J. N. et al. Detection and characterization of influenza A virus PA-PB2 interaction through a bimolecular fluorescence complementation assay. J. Virol. 83, 3944-3955 (2009).
    • (2009) J. Virol. , vol.83 , pp. 3944-3955
    • Hemerka, J.N.1
  • 7
    • 84869136079 scopus 로고    scopus 로고
    • Evolutionary conservation of the PA-X open reading frame in segment 3 of influenza A virus
    • Shi, M. et al. Evolutionary conservation of the PA-X open reading frame in segment 3 of influenza A virus. J. Virol. 86, 12411-12413 (2012).
    • (2012) J. Virol. , vol.86 , pp. 12411-12413
    • Shi, M.1
  • 8
    • 67249130012 scopus 로고    scopus 로고
    • The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit
    • Dias, A. et al. The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit. Nature 458, 914-918 (2009).
    • (2009) Nature , vol.458 , pp. 914-918
    • Dias, A.1
  • 9
    • 67249100913 scopus 로고    scopus 로고
    • Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site
    • Yuan, P. et al. Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site. Nature 458, 909-913 (2009).
    • (2009) Nature , vol.458 , pp. 909-913
    • Yuan, P.1
  • 10
    • 69449096816 scopus 로고    scopus 로고
    • Nucleoside monophosphate complex structures of the endonuclease domain from the influenza virus polymerase PA subunit reveal the substrate binding site inside the catalytic center
    • Zhao, C. et al. Nucleoside monophosphate complex structures of the endonuclease domain from the influenza virus polymerase PA subunit reveal the substrate binding site inside the catalytic center. J. Virol. 83, 9024-9030 (2009).
    • (2009) J. Virol. , vol.83 , pp. 9024-9030
    • Zhao, C.1
  • 11
    • 84885181482 scopus 로고    scopus 로고
    • Crystallographic fragment screening and structure-based optimization yields a new class of influenza endonuclease inhibitors
    • Bauman, J. D. et al. Crystallographic fragment screening and structure-based optimization yields a new class of influenza endonuclease inhibitors. ACS Chem. Biol. 8, 2501-2508 (2013).
    • (2013) ACS Chem. Biol. , vol.8 , pp. 2501-2508
    • Bauman, J.D.1
  • 12
    • 84866177810 scopus 로고    scopus 로고
    • Structural analysis of specific metal chelating inhibitor binding to the endonuclease domain of influenza pH1N1 (2009) polymerase
    • Kowalinski, E. et al. Structural analysis of specific metal chelating inhibitor binding to the endonuclease domain of influenza pH1N1 (2009) polymerase. PLoS Pathog. 8, e1002831 (2012).
    • (2012) PLoS Pathog. , vol.8
    • Kowalinski, E.1
  • 13
    • 50649089174 scopus 로고    scopus 로고
    • Crystal structure of the polymerase PA(C)-PB1(N) complex from an avian influenza H5N1 virus
    • He, X. et al. Crystal structure of the polymerase PA(C)-PB1(N) complex from an avian influenza H5N1 virus. Nature 454, 1123-1126 (2008).
    • (2008) Nature , vol.454 , pp. 1123-1126
    • He, X.1
  • 14
    • 50649122962 scopus 로고    scopus 로고
    • The structural basis for an essential subunit interaction in influenza virus RNA polymerase
    • Obayashi, E. et al. The structural basis for an essential subunit interaction in influenza virus RNA polymerase. Nature 454, 1127-1131 (2008).
    • (2008) Nature , vol.454 , pp. 1127-1131
    • Obayashi, E.1
  • 15
    • 67649552964 scopus 로고    scopus 로고
    • Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase
    • Sugiyama, K. et al. Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase. EMBO J. 28, 1803-1811 (2009).
    • (2009) EMBO J. , vol.28 , pp. 1803-1811
    • Sugiyama, K.1
  • 16
    • 84892608509 scopus 로고    scopus 로고
    • Computation-guided discovery of influenza endonuclease inhibitors
    • Chen, E. et al. Computation-guided discovery of influenza endonuclease inhibitors. ACS Med. Chem. Lett. 5, 61-64 (2014).
    • (2014) ACS Med. Chem. Lett. , vol.5 , pp. 61-64
    • Chen, E.1
  • 17
    • 80055072231 scopus 로고    scopus 로고
    • Identification of influenza virus inhibitors which disrupt of viral polymerase protein-protein interactions
    • Chase, G., Wunderlich, K., Reuther, P. & Schwemmle, M. Identification of influenza virus inhibitors which disrupt of viral polymerase protein-protein interactions. Methods 55, 188-191 (2011).
    • (2011) Methods , vol.55 , pp. 188-191
    • Chase, G.1    Wunderlich, K.2    Reuther, P.3    Schwemmle, M.4
  • 18
    • 78751681564 scopus 로고    scopus 로고
    • Identification of high-affinity PB1-derived peptides with enhanced affinity to the PA protein of influenza A virus polymerase
    • Wunderlich, K. et al. Identification of high-affinity PB1-derived peptides with enhanced affinity to the PA protein of influenza A virus polymerase. Antimicrob. Agents Chemother. 55, 696-702 (2011).
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 696-702
    • Wunderlich, K.1
  • 19
    • 84859986406 scopus 로고    scopus 로고
    • Small molecule inhibitors of influenza A and B viruses that act by disrupting subunit interactions of the viral polymerase
    • Muratore, G. et al. Small molecule inhibitors of influenza A and B viruses that act by disrupting subunit interactions of the viral polymerase. Proc. Natl. Acad. Sci. USA 109, 6247-6252 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 6247-6252
    • Muratore, G.1
  • 20
    • 84891744967 scopus 로고    scopus 로고
    • The fight against the influenza A virus H1N1: Synthesis molecular modeling, and biological evaluation of benzofurazan derivatives as viral RNA polymerase inhibitors
    • Pagano, M. et al. The fight against the influenza A virus H1N1: synthesis, molecular modeling, and biological evaluation of benzofurazan derivatives as viral RNA polymerase inhibitors. ChemMedChem 9, 129-150 (2014).
    • (2014) ChemMedChem , vol.9 , pp. 129-150
    • Pagano, M.1
  • 21
    • 84891492237 scopus 로고    scopus 로고
    • High-throughput docking for the identification of new influenza A virus polymerase inhibitors targeting the PA-PB1 protein-protein interaction
    • Tintori, C. et al. High-throughput docking for the identification of new influenza A virus polymerase inhibitors targeting the PA-PB1 protein-protein interaction. Bioorg. Med. Chem. Lett. 24, 280-282 (2014).
    • (2014) Bioorg. Med. Chem. Lett. , vol.24 , pp. 280-282
    • Tintori, C.1
  • 22
    • 65649112893 scopus 로고    scopus 로고
    • Gene composer: Database software for protein construct design, codon engineering, and gene synthesis
    • Lorimer, D. et al. Gene composer: database software for protein construct design, codon engineering, and gene synthesis. BMC Biotechnol. 9, 36 (2009).
    • (2009) BMC Biotechnol. , vol.9 , pp. 36
    • Lorimer, D.1
  • 23
    • 65649096202 scopus 로고    scopus 로고
    • Combined protein construct and synthetic gene engineering for heterologous protein expression and crystallization using Gene Composer
    • Raymond, A. et al. Combined protein construct and synthetic gene engineering for heterologous protein expression and crystallization using Gene Composer. BMC Biotechnol. 9, 37 (2009).
    • (2009) BMC Biotechnol. , vol.9 , pp. 37
    • Raymond, A.1
  • 24
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • DOI 10.1038/nprot.2007.321, PII NPROT.2007.321
    • Niesen, F. H., Berglund, H. & Vedadi, M. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nature Protoc. 2, 2212-2221 (2007). (Pubitemid 351565860)
    • (2007) Nature Protocols , vol.2 , Issue.9 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 25
    • 84857098515 scopus 로고    scopus 로고
    • Reassortment and mutation of the avian influenza virus polymerase PA subunit overcome species barriers
    • Mehle, A., Dugan, V. G., Taubenberger, J. K. & Doudna, J. A. Reassortment and mutation of the avian influenza virus polymerase PA subunit overcome species barriers. J. Virol. 86, 1750-1757 (2012).
    • (2012) J. Virol. , vol.86 , pp. 1750-1757
    • Mehle, A.1    Dugan, V.G.2    Taubenberger, J.K.3    Doudna, J.A.4
  • 26
    • 85003322320 scopus 로고    scopus 로고
    • Multi-target parallel processing approach for gene-to-structure determination of the influenza polymerase PB2 subunit
    • DOI: 10.3791/4225
    • Armour, B. L. et al. Multi-target parallel processing approach for gene-to-structure determination of the influenza polymerase PB2 subunit. J. Vis. Exp. June 26, 76; DOI: 10.3791/4225 (2013).
    • (2013) J. Vis. Exp. June , vol.26 , pp. 76
    • Armour, B.L.1
  • 27
    • 80052615275 scopus 로고    scopus 로고
    • The Protein Maker: An automated system for high-throughput parallel purification
    • Smith, E. R. et al. The Protein Maker: an automated system for high-throughput parallel purification. Acta Cryst. F 67, 1015-1021 (2011).
    • (2011) Acta Cryst. F , vol.67 , pp. 1015-1021
    • Smith, E.R.1
  • 28
    • 77958149212 scopus 로고    scopus 로고
    • Biological and structural characterization of a host-adapting amino acid in influenza virus
    • Yamada, S. et al. Biological and structural characterization of a host-adapting amino acid in influenza virus. PLoS Pathog. 6, e1001034 (2010).
    • (2010) PLoS Pathog. , vol.6
    • Yamada, S.1
  • 29
    • 70449768051 scopus 로고    scopus 로고
    • The MORPHEUS protein crystallization screen
    • Gorrec, F. The MORPHEUS protein crystallization screen. J Appl. Crystallogr. 42, 1035-1042 (2009).
    • (2009) J Appl. Crystallogr. , vol.42 , pp. 1035-1042
    • Gorrec, F.1
  • 34
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Cryst. D 66, 12-21 (2010).
    • (2010) Acta Cryst. D , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 35
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Cryst. D 66, 213-221 (2010).
    • (2010) Acta Cryst. D , vol.66 , pp. 213-221
    • Adams, P.D.1


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