Protein kinase C-dependent phosphorylation of Borna disease virus P protein is required for efficient viral spread
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Mutational analysis of the phosphate acceptor sites of the Borna disease virus (BDV) phosphoprotein (P) has suggested a role of phosphorylation for viral spread. However, the studied mutant viruses also had two amino acid exchanges in the X protein, because the reading frames of P and X overlap. To determine the relative contribution of P and X to viral attenuation, we studied a P variant with serine-to-leucine substitutions (PS26L,S28L) in which the wild-type X sequence was conserved. Viral spread of rBDV-PS26L,S28L was impaired in human oligodendroglioma cells and in adult rats. Thus, BDV-P phosphorylation contributes to efficient viral dissemination.
KeywordsRabies Vero Cell Polymerase Activity Viral Life Cycle Human Respiratory Syncytial Virus
This work was supported by the Deutsche Forschungsgemeinschaft. We thank members of the Schwemmle and Gonzalez-Dunia labs for critical reading of the manuscript.
- 19.Prat CM, Schmid S, Farrugia F, Cenac N, Le Masson G, Schwemmle M, Gonzalez-Dunia D (2009) Mutation of the protein kinase C site in borna disease virus phosphoprotein abrogates viral interference with neuronal signaling and restores normal synaptic activity. PLoS Pathog 5(5):e1000425CrossRefPubMedGoogle Scholar