Journal
JOURNAL OF VIROLOGY
Volume 89, Issue 2, Pages 1452-1455Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.02332-14
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Funding
- Medical Research Council (MRC) [MR/K000241/1, G1100138]
- BBSRC
- MRC [MR/K000241/1, G1100138] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [1104336] Funding Source: researchfish
- Medical Research Council [MR/K000241/1, G1100138] Funding Source: researchfish
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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.
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