Journal
VIROLOGY
Volume 383, Issue 1, Pages 6-11Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2008.10.002
Keywords
Influenza virus; NS1; Phosphorylation; ERK; CDK
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Funding
- Medical Research Council, UK
- Scottish Funding Council, UK
- The Wellcome Trust
- The University of St. Andrews is a charity registered in Scotland [SC013532]
- Medical Research Council [G0601126] Funding Source: researchfish
- MRC [G0601126] Funding Source: UKRI
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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. (c) 2008 Elsevier Inc. All rights reserved.
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