Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6141686 | Virology | 2009 | 6 Pages |
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.
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Authors
Benjamin G. Hale, Axel Knebel, Catherine H. Botting, Caroline S. Galloway, Bernard L. Precious, David Jackson, Richard M. Elliott, Richard E. Randall,