Evidence that the C-terminal PB2-binding region of the influenza A virus PB1 protein is a discrete α-helical domain

FEBS Letters

Volumn 581, Issue 27, 2007, Pages 5300-5306

  Poole, Emma L ^a   Medcalf, Liz ^a   Elton, Debra ^a   Digard, Paul ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Drug design; Orthomyxovirus; Polymerase; Protein protein

Indexed keywords

PROTEIN PB1; RNA DIRECTED RNA POLYMERASE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ALPHA HELIX; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME STRUCTURE; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; INFLUENZA VIRUS A; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; VIRUS REPLICATION;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL LINE; FEMALE; HUMANS; INFLUENZA A VIRUS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OOCYTES; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID; VIRAL PROTEINS; XENOPUS;

INFLUENZA A VIRUS; ORTHOMYXOVIRIDAE;

EID: 35549006262     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.10.025     Document Type: Article

References (38)

1. Peiris J.S., de Jong M.D., and Guan Y. Avian influenza virus (H5N1): a threat to human health. Clin. Microbiol. Rev. 20 (2007) 243-267
2. Portela A., and Digard P. The influenza virus nucleoprotein: a multifunctional RNA-binding protein pivotal to virus replication. J. Gen. Virol. 83 (2002) 723-734
3. Braam J., Ulmanen I., and Krug R.M. Molecular model of a eucaryotic transcription complex: functions and movements of influenza P proteins during capped RNA-primed transcription. Cell 34 (1983) 609-618
4. Digard P., Blok V.C., and Inglis S.C. Complex formation between influenza virus polymerase proteins expressed in Xenopus oocytes. Virology 171 (1989) 162-169
5. Elton D., Digard P., Tiley L., and Ortin J. Structure and function of the influenza virus RNP. In: Kawaoka Y. (Ed). Influenza Virology; Current Topics (2006), Caister Academic Press, Wymondham 1-36
6. Gonzalez S., Zurcher T., and Ortin J. Identification of two separate domains in the influenza virus PB1 protein involved in the interaction with the PB2 and PA subunits: a model for the viral RNA polymerase structure. Nucleic Acids Res. 24 (1996) 4456-4463
7. Perez D.R., and Donis R.O. A 48-amino-acid region of influenza A virus PB1 protein is sufficient for complex formation with PA. J. Virol. 69 (1995) 6932-6939
8. Toyoda T., Adyshev D.M., Kobayashi M., Iwata A., and Ishihama A. Molecular assembly of the influenza virus RNA polymerase: determination of the subunit-subunit contact sites. J. Gen. Virol. 77 Pt 9 (1996) 2149-2157
9. Zurcher T., de la Luna S., Sanz-Ezquerro J.J., Nieto A., and 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 Pt 8 (1996) 1745-1749
10. Area E., Martin-Benito J., Gastaminza P., Torreira E., Valpuesta J.M., Carrascosa J.L., and Ortin J. 3D structure of the influenza virus polymerase complex: localization of subunit domains. Proc. Natl. Acad. Sci. USA 101 (2004) 308-313
11. Martin-Benito J., Area E., Ortega J., Llorca O., Valpuesta J.M., Carrascosa J.L., and Ortin J. Three-dimensional reconstruction of a recombinant influenza virus ribonucleoprotein particle. EMBO Rep. 2 (2001) 313-317
12. Torreira E., Schoehn G., Fernandez Y., Jorba N., Ruigrok R.W., Cusack S., Ortin J., and Llorca O. Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer. Nucleic Acids Res. 35 (2007) 3774-3783
13. Biswas S.K., and Nayak D.P. Influenza virus polymerase basic protein 1 interacts with influenza virus polymerase basic protein 2 at multiple sites. J. Virol. 70 (1996) 6716-6722
14. Poole E., Elton D., Medcalf L., and Digard P. Functional domains of the influenza A virus PB2 protein: identification of NP- and PB1-binding sites. Virology 321 (2004) 120-133
15. Ghanem A., Mayer D., Chase G., Tegge W., Frank R., Kochs G., Garcia-Sastre A., and Schwemmle M. Peptide-mediated interference with influenza a virus polymerase. J. Virol. 81 (2007) 7801-7804
16. Perez D.R., and Donis R.O. Functional analysis of PA binding by influenza a virus PB1: effects on polymerase activity and viral infectivity. J. Virol. 75 (2001) 8127-8136
17. Tsai C.H., Lee P.Y., Stollar V., and Li M.L. Antiviral therapy targeting viral polymerase. Curr. Pharm. Des. 12 (2006) 1339-1355
18. Tarendeau F., et al. Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit. Nat. Struct. Mol. Biol. 14 (2007) 229-233
19. Hara K., Schmidt F.I., Crow M., and 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 (2006) 7789-7798
20. Blok V., Cianci C., Tibbles K.W., Inglis S.C., Krystal M., and Digard P. Inhibition of the influenza virus RNA-dependent RNA polymerase by antisera directed against the carboxy-terminal region of the PB2 subunit. J. Gen. Virol. 77 Pt 5 (1996) 1025-1033
21. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
22. Mullin A.E., Dalton R.M., Amorim M.J., Elton D., and Digard P. Increased amounts of the influenza virus nucleoprotein do not promote higher levels of viral genome replication. J. Gen. Virol. 85 (2004) 3689-3698
23. Ohtsu Y., Honda Y., Sakata Y., Kato H., and Toyoda T. Fine mapping of the subunit binding sites of influenza virus RNA polymerase. Microbiol. Immunol. 46 (2002) 167-175
24. Chen Y.H., Yang J.T., and Martinez H.M. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11 (1972) 4120-4131
25. Cuff J.A., and Barton G.J. Evaluation and improvement of multiple sequence methods for protein secondary structure prediction. Proteins 34 (1999) 508-519
26. Cheng J., Randall A.Z., Sweredoski M.J., and Baldi P. SCRATCH: a protein structure and structural feature prediction server. Nucleic Acids Res. 33 (2005) W72-W76
27. Holm L., and Sander C. Database algorithm for generating protein backbone and side-chain co-ordinates from a C alpha trace application to model building and detection of co-ordinate errors. J. Mol. Biol. 218 (1991) 183-194
28. Deng T., Sharps J.L., and Brownlee G.G. Role of the influenza virus heterotrimeric RNA polymerase complex in the initiation of replication. J. Gen. Virol. 87 (2006) 3373-3377
29. Gastaminza P., Perales B., Falcon A.M., and Ortin J. Mutations in the N-terminal region of influenza virus PB2 protein affect virus RNA replication but not transcription. J. Virol. 77 (2003) 5098-5108
30. Lee M.T., Bishop K., Medcalf L., Elton D., Digard P., and Tiley L. Definition of the minimal viral components required for the initiation of unprimed RNA synthesis by influenza virus RNA polymerase. Nucleic Acids Res. 30 (2002) 429-438
31. Perales B., and Ortin J. The influenza A virus PB2 polymerase subunit is required for the replication of viral RNA. J. Virol. 71 (1997) 1381-1385
32. Honda A., Mizumoto K., and Ishihama A. Minimum molecular architectures for transcription and replication of the influenza virus. Proc. Natl. Acad. Sci. USA 99 (2002) 13166-13171
33. Nakagawa Y., Kimura N., Toyoda T., Mizumoto K., Ishihama A., Oda K., and Nakada S. The RNA polymerase PB2 subunit is not required for replication of the influenza virus genome but is involved in capped mRNA synthesis. J. Virol. 69 (1995) 728-733
34. Digard P., Bebrin W.R., Weisshart K., and Coen D.M. The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication. J. Virol. 67 (1993) 398-406
35. Zuccola H.J., Filman D.J., Coen D.M., and Hogle J.M. The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase. Mol. Cell 5 (2000) 267-278
36. Digard P., Williams K.P., Hensley P., Brooks I.S., Dahl C.E., and Coen D.M. Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interface. Proc. Natl. Acad. Sci. USA 92 (1995) 1456-1460
37. Loregian A., Papini E., Satin B., Marsden H.S., Hirst T.R., and Palu G. Intranuclear delivery of an antiviral peptide mediated by the B subunit of Escherichia coli heat-labile enterotoxin. Proc. Natl. Acad. Sci. USA 96 (1999) 5221-5226
38. Pilger B.D., Cui C., and Coen D.M. Identification of a small molecule that inhibits herpes simplex virus DNA polymerase subunit interactions and viral replication. Chem. Biol. 11 (2004) 647-654