| Literature DB >> 19007960 |
Benjamin G Hale1, Axel Knebel, Catherine H Botting, Caroline S Galloway, Bernard L Precious, David Jackson, Richard M Elliott, Richard E Randall.
Abstract
Posttranslational modification of viral proteins by cellular enzymes is a feature of many virus replication strategies. Here, we report that during infection the multifunctional human influenza A virus NS1 protein is phosphorylated at threonine-215. Substitution of alanine for threonine at this position reduced early viral propagation, an effect apparently unrelated to NS1 antagonizing host interferon responses or activating phosphoinositide 3-kinase signaling. In vitro, a subset of cellular proline-directed kinases, including cyclin dependent kinases (CDKs) and extracellular signal-regulated kinases (ERKs), potently phosphorylated NS1 protein at threonine-215. Our data suggest that CDK/ERK-mediated phosphorylation of NS1 at threonine-215 is important for efficient virus replication.Entities:
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Year: 2008 PMID： 19007960 DOI： 10.1016/j.virol.2008.10.002
Source DB: PubMed Journal: Virology ISSN： 0042-6822 Impact factor: 3.616