CDK/ERK-mediated phosphorylation of the human influenza A virus NS1 protein at threonine-215

B. G. Hale, A. Knebel, C. H. Botting, C. S. Galloway, B. L. Precious, David Jackson, R. M. Elliott, R. E. Randall

Research output: Contribution to journalArticlepeer-review

62 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)6-11
Number of pages6
Issue number1
Publication statusPublished - 5 Jan 2009


  • Amino Acid Substitution/genetics Cell Line Cyclin-Dependent Kinases/*metabolism Extracellular Signal-Regulated MAP Kinases/*metabolism Humans Influenza A virus/*physiology Mutagenesis, Site-Directed Phosphorylation Plaque Assay Threonine/metabolism Viral Nonstructural Proteins/*metabolism Virus Replication


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