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lüll Protein kinase C-dependent phosphorylation of Borna disease virus P protein is required for efficient viral spread Schmid S; Metz P; Prat CM; Gonzalez-Dunia D; Schwemmle MArch Virol 2010[May]; 155 (5): 789-93Mutational 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 (P(S26L,S28L)) in which the wild-type X sequence was conserved. Viral spread of rBDV-P(S26L,S28L) was impaired in human oligodendroglioma cells and in adult rats. Thus, BDV-P phosphorylation contributes to efficient viral dissemination.|Animals[MESH]|Borna disease virus/*physiology[MESH]|Cells, Cultured[MESH]|Humans[MESH]|Phosphoproteins/*metabolism[MESH]|Phosphorylation[MESH]|Protein Kinase C/chemistry/*physiology[MESH]|Rats[MESH]|Rats, Inbred Lew[MESH]|Viral Structural Proteins/*metabolism[MESH] |