Journal
ARCHIVES OF VIROLOGY
Volume 155, Issue 5, Pages 789-793Publisher
SPRINGER WIEN
DOI: 10.1007/s00705-010-0645-9
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- Deutsche Forschungsgemeinschaft
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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 (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.
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