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

Benjamin G. Hale; Axel Knebel; Catherine H. Botting; Caroline S. Galloway; Bernard L. Precious; David Jackson; Richard M. Elliott; Richard E. Randall

doi:10.1016/j.virol.2008.10.002

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

Benjamin G. Hale, Axel Knebel, Catherine H. Botting, Caroline S. Galloway, Bernard L. Precious, David Jackson, Richard M. Elliott, Richard E. Randall^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

67 Citations (Scopus)

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.

Original language	English
Pages (from-to)	6-11
Number of pages	6
Journal	Virology
Volume	383
Issue number	1
DOIs	https://doi.org/10.1016/j.virol.2008.10.002
Publication status	Published - 5 Jan 2009
Externally published	Yes

Keywords

CDK
ERK
Influenza virus
NS1
Phosphorylation

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10.1016/j.virol.2008.10.002

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

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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AU - Hale, Benjamin G.

AU - Knebel, Axel

AU - Botting, Catherine H.

AU - Galloway, Caroline S.

AU - Precious, Bernard L.

AU - Jackson, David

AU - Elliott, Richard M.

AU - Randall, Richard E.

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AB - 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.

KW - CDK

KW - ERK

KW - Influenza virus

KW - NS1

KW - Phosphorylation

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

Abstract

Keywords

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