tetano
Editor, Senior Moderator
J Virol. 2014 Oct 29. pii: JVI.02332-14. [Epub ahead of print]
Regulation of Influenza A Virus Nucleoprotein Oligomerisation by Phosphorylation.
Turrell L1, Hutchinson EC1, Vreede FT2, Fodor E2.
Author information
Abstract
In the influenza virus ribonucleoprotein complex the oligomerisation of the nucleoprotein is mediated by an interaction between the tail-loop of one molecule and the groove of the neighbouring molecule. In this study we show that phosphorylation of a serine residue (S165) within the groove of influenza A virus nucleoprotein inhibits oligomerisation and, consequently, ribonucleoprotein activity and viral growth. We propose that nucleoprotein oligomerisation in infected cells is regulated by reversible phosphorylation.
Copyright ? 2014, American Society for Microbiology. All Rights Reserved.
PMID:
25355893
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25355893
Regulation of Influenza A Virus Nucleoprotein Oligomerisation by Phosphorylation.
Turrell L1, Hutchinson EC1, Vreede FT2, Fodor E2.
Author information
Abstract
In the influenza virus ribonucleoprotein complex the oligomerisation of the nucleoprotein is mediated by an interaction between the tail-loop of one molecule and the groove of the neighbouring molecule. In this study we show that phosphorylation of a serine residue (S165) within the groove of influenza A virus nucleoprotein inhibits oligomerisation and, consequently, ribonucleoprotein activity and viral growth. We propose that nucleoprotein oligomerisation in infected cells is regulated by reversible phosphorylation.
Copyright ? 2014, American Society for Microbiology. All Rights Reserved.
PMID:
25355893
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25355893