Regulation of influenza A virus nucleoprotein oligomerization by phosphorylation

Turrell, L., Hutchinson, E. C. , Vreede, F. T. and Fodor, E. (2015) Regulation of influenza A virus nucleoprotein oligomerization by phosphorylation. Journal of Virology, 89(2), pp. 1452-1455. (doi:10.1128/JVI.02332-14) (PMID:25355893) (PMCID:PMC4300657)

Full text not currently available from Enlighten.


In the influenza virus ribonucleoprotein complex, the oligomerization of the nucleoprotein is mediated by an interaction between the tail-loop of one molecule and the groove of the neighboring molecule. In this study, we show that phosphorylation of a serine residue (S165) within the groove of influenza A virus nucleoprotein inhibits oligomerization and, consequently, ribonucleoprotein activity and viral growth. We propose that nucleoprotein oligomerization in infected cells is regulated by reversible phosphorylation.

Item Type:Articles
Additional Information:This work was supported by Medical Research Council (MRC) grants MR/K000241/1 (to E.F.) and G1100138 (to F.T.V.) and a BBSRC studentship (to L.T.)
Glasgow Author(s) Enlighten ID:Hutchinson, Dr Edward
Authors: Turrell, L., Hutchinson, E. C., Vreede, F. T., and Fodor, E.
College/School:College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:Journal of Virology
Publisher:American Society for Microbiology
ISSN (Online):1098-5514

University Staff: Request a correction | Enlighten Editors: Update this record