Giuseppe
Emeritus
J Gen Virol. 2009 Mar 4. [Epub ahead of print]
The influenza A virus proteins PB1 and NS1 are subject to functionally important phosphorylation by protein kinase C.
Mahmoudian S, Auerochs S, Gr?ne M, Marschall M. - Institute for Clinical and Molecular Virology, University of Erlangen-Nuremberg, Germany.
Virulence of influenza A viruses depends on the activity of the viral RNA polymerase complex and viral regulatory phosphoproteins. We identified a post-entry anti-influenza viral effect of the protein kinase C (PKC) inhibitor G?6976 by using a polymerase-activity based reporter assay.
This inhibitory effect was observed for influenza virus-infected cells as well as cells transiently transfected with constructs for the RNA polymerase complex and nucleo-/nonstructural proteins. Importantly, the in vitro analysis of viral protein phosphorylation identified PKCalpha as a kinase phosphorylating PB1 and NS1, but not PB2, PA and NP.
G?6976 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 functionally relevant for both viral RNA polymerase activity and efficient viral replication.
PMID: 19264651 [PubMed - as supplied by publisher]
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The influenza A virus proteins PB1 and NS1 are subject to functionally important phosphorylation by protein kinase C.
Mahmoudian S, Auerochs S, Gr?ne M, Marschall M. - Institute for Clinical and Molecular Virology, University of Erlangen-Nuremberg, Germany.
Virulence of influenza A viruses depends on the activity of the viral RNA polymerase complex and viral regulatory phosphoproteins. We identified a post-entry anti-influenza viral effect of the protein kinase C (PKC) inhibitor G?6976 by using a polymerase-activity based reporter assay.
This inhibitory effect was observed for influenza virus-infected cells as well as cells transiently transfected with constructs for the RNA polymerase complex and nucleo-/nonstructural proteins. Importantly, the in vitro analysis of viral protein phosphorylation identified PKCalpha as a kinase phosphorylating PB1 and NS1, but not PB2, PA and NP.
G?6976 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 functionally relevant for both viral RNA polymerase activity and efficient viral replication.
PMID: 19264651 [PubMed - as supplied by publisher]
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