The structural basis for an essential subunit interaction in influenza virus RNA polymerase

Nature

Volumn 454, Issue 7208, 2008, Pages 1127-1131

  Obayashi, Eiji ^a   Yoshida, Hisashi ^a   Kawai, Fumihiro ^a   Shibayama, Naoya ^b   Kawaguchi, Atsushi ^c   Nagata, Kyosuke ^c   Tame, Jeremy R H ^a   Park, Sam Yong ^a  

^a YOKOHAMA CITY UNIVERSITY   (Japan)

^b JICHI MEDICAL UNIVERSITY   (Japan)

^c UNIVERSITY OF TSUKUBA   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE ANTIGEN; RNA POLYMERASE;

ENZYME; INFLUENZA; RNA; VIRUS;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME BINDING; HYDROGEN BOND; INFLUENZA VIRUS; MOLECULAR INTERACTION; NONHUMAN; PB1 GENE; PRIORITY JOURNAL; VIRUS GENOME; VIRUS REPLICATION;

BINDING SITES; CELL LINE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; HUMANS; INFLUENZA A VIRUS, H1N1 SUBTYPE; PROTEIN BINDING; PROTEIN SUBUNITS; RNA REPLICASE; VIRAL PROTEINS; VIRUS REPLICATION;

ANIMALIA; AVES; INFLUENZA A VIRUS; ORTHOMYXOVIRIDAE;

EID: 50649122962     PISSN: 00280836     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/nature07225     Document Type: Article

References (42)

1. Peiris, J. S., de Jong, M. D. & Guan, Y. Avian influenza virus (H5N1): a threat to human health. Clin. Microbiol. Rev. 20, 243-267 (2007).
2. Horisberger, M. A. The large P proteins of influenza A viruses are composed of one acidic and two basic polypeptides. Virology 107, 302-305 (1980).
3. Braam, J., Ulmanen, I. & Krug, R. M. Molecular model of a eucaryotic transcription complex: functions and movements of influenza P proteins during capped RNA-primed transcription. Cell 34, 611-618 (1983).
4. Nagata, K., Kawaguchi, A. & Naito, T. Host factors for replication and transcription of the influenza virus genome. Rev. Med. Virol. 18, 247-260 (2008).
5. Fodor, E., Mingay, L. J., Crow, M., Deng, T. & Brownlee, G. G. A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase promotes the generation of defective interfering RNAs. J. Virol. 77, 5017-5020 (2003).
6. Kawaguchi, A., Naito, T. & Nagata, K. Involvement of influenza virus PA subunit in assembly of functional RNA polymerase complexes. J. Virol. 79, 732-744 (2005).
7. Deng, T., Sharps, J. L. & Brownlee, G. G. Role of the influenza virus heterotrimeric RNA polymerase complex in the initiation of replication. J. Gen. Virol. 87, 3373-3377 (2006).
8. Area, E. et al. 3D structure of the influenza virus polymerase complex: localization of subunit domains. Proc. Natl Acad. Sci. USA 101, 308-313 (2004).
9. Torreira, E. et al. Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer. Nucleic Acids Res. 35, 3774-3783 (2007).
10. Tarendeau, F. et al. Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit. Nature Struct. Mol. Biol. 14, 229-233 (2007).
11. Guilligay, D. et al. The structural basis for cap binding by influenza virus polymerase subunit PB2. Nature Struct. Mol. Biol. 15, 500-506 (2008).
12. Elton, D., Digard, P., Tiley, L. & Ortin, J. in Current Topics in Influenza Virology (ed. Kawaoka, Y.) 1-92 (Horizon Scientific Press, 2005).
13. 7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription. Cell 23, 847-858 (1981).
14. Taubenberger, J. K. et al. Characterization of the 1918 influenza virus polymerase genes. Nature 437, 889-893 (2005).
15. Zurcher, T., de la Luna, S., Sanz-Ezquerro, J. J., Nieto, A. & Ortin, J. Mutational analysis of the influenza virus A/Victoria/3/75 PA protein: studies of interaction with PB1 protein and identification of a dominant negative mutant. J. Gen. Virol. 77, 1745-1749 (1996).
16. Perez, D. R. & Donis, R. O. Functional analysis of PA binding by influenza A virus PB1: effects on polymerase activity and viral infectivity. J. Virol. 75, 8127-8136 (2001).
17. Ohtsu, Y., Honda, Y., Sakata, Y., Kato, H. & Toyoda, T. Fine mapping of the subunit binding sites of influenza virus RNA polymerase. Microbiol. Immunol. 46, 167-175 (2002).
18. Ghanem, A. et al. Peptide-mediated interference with influenza A virus polymerase. J. Virol. 81, 7801-7804 (2007).
19. Hara, K., Schmidt, F. I., Crow, M. & Brownlee, G. G. Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding. J. Virol. 80, 7789-7798 (2006).
20. Fodor, E. et al. 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).
21. Huarte, M. et al. Threonine 157 of influenza virus PA polymerase subunit modulates RNA replication in infectious viruses. J. Virol. 77, 6007-6013 (2003).
22. Regan, J. F., Liang, Y. & Parslow, T. G. Defective assembly of influenza A virus due to a mutation in the polymerase subunit PA. J. Virol. 80, 252-261 (2006).
23. Hsieh, H. P. & Hsu, J. T. Strategies of development of antiviral agents directed against influenza virus replication. Curr. Pharm. Des. 13, 3531-3542 (2007).
24. World Health Organization.. A revision of the system of nomenclature for influenza viruses: a WHO memorandum. Bull. World Health Organ. 58, 585-591 (1980).
25. Kim, C. U. et al. Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: Design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity. J. Am. Chem. Soc. 119, 681-690 (1997).
26. von Itzstein, M. et al. Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature 363, 418-423 (1993).
27. Russell, R. J. et al. The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature 443, 45-49 (2006).
28. Liu, Y., Zhang, J. & Xu, W. Recent progress in rational drug design of neuraminidase inhibitors. Curr. Med. Chem. 14, 2872-2891 (2007).
29. Wang, C., Takeuchi, K., Pinto, L. H. & Lamb, R. A. Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block. J. Virol. 67, 5585-5594 (1993).
30. Stouffer, A. L. et al. Structural basis for the function and inhibition of an influenza virus proton channel. Nature 451, 596-599 (2008).
31. Kawaguchi, A. & Nagata, K. De novo replication of the influenza virus RNA genome is regulated by DNA replicative helicase, MCM. EMBO J. 26, 4566-4575 (2007).
32. Turan, K. et al. Nuclear MxA proteins form a complex with influenza virus NP and inhibit the transcription of the engineered influenza virus genome. Nucleic Acids Res. 32, 643-652 (2004).
33. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
34. Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
35. Sheldrick, G. M. A short history of SHELX. Acta Crystallogr. A 64, 112-122 (2008).
36. Terwilliger, T. C. & Berendzen, J. Automated MAD and MIR structure solution. Acta Crystallogr. D 55, 849-861 (1999).
37. Terwilliger, T. C. SOLVE and RESOLVE: Automated structure solution and density modification. Methods Enzymol. 374, 22-37 (2003).
38. Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
39. Roussel, A. & Cambillau, C. in Silicon Graphics Geometry Partner Directory 77-78 (Silicon Graphics, 1989).
40. Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
41. Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
42. Laskowski, R. A., Moss, D. S. & Thornton, J. M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231, 1049-1067 (1993).