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Originally published as JGV in Press, 10.1099/vir.0.009050-0 on March 4, 2009 J Gen Virol 90 (2009), 1392-1397; DOI 10.1099/vir.0.009050-0

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Short Communication

Influenza A virus proteins PB1 and NS1 are subject to functionally important phosphorylation by protein kinase C

Shohreh Mahmoudian, Sabrina Auerochs, Monika Gröne and Manfred Marschall

Institute for Clinical and Molecular Virology, University of Erlangen-Nuremberg, Germany

Correspondence
Manfred Marschall
manfred.marschall{at}viro.med.uni-erlangen.de

The virulence of influenza A viruses depends on the activity of the viral RNA polymerase complex and viral regulatory phosphoproteins. We identified that the protein kinase C (PKC) inhibitor Gö6976 had a post-entry anti-influenza viral effect, by using a polymerase activity-based reporter assay. This inhibitory effect was observed for influenza virus-infected cells as well as for cells transiently transfected with constructs for the RNA polymerase complex. Importantly, the in vitro analysis of viral protein phosphorylation identified PKC{alpha} as a kinase phosphorylating PB1 and NS1, but not PB2, PA or NP. Gö6976 was able to block PKC-specific phosphorylation in vitro. Thus, our data suggest that PKC contributes to the phosphorylation of influenza PB1 and NS1 proteins which appears to be functionally relevant for both viral RNA polymerase activity and efficient viral replication.

A supplementary table of primer sequences and a supplementary figure are available with the online version of this paper.






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