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

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• 作者：Benjamin G. Hale ; Axel Knebel ; Catherine H. Botting ; Caroline S. Galloway ; Bernard L. Precious ; David Jackson ; Richard M. Elliott ; Richard E. R ; all
• 关键词：Influenza virus ; NS1 ; Phosphorylation ; ERK ; CDK
• 刊名：Virology
• 出版年：2009
• 出版时间：5 January 2009
• 年：2009
• 卷：383
• 期：1
• 页码：6-11
• 全文大小：479 K

文摘

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.