Protein kinase C-dependent phosphorylation of Borna disease virus P protein is required for efficient viral spread

Arch Virol. 2010 May;155(5):789-93. doi: 10.1007/s00705-010-0645-9. Epub 2010 Mar 24.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Borna disease virus / physiology*
  • Cells, Cultured
  • Humans
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Kinase C / chemistry
  • Protein Kinase C / physiology*
  • Rats
  • Rats, Inbred Lew
  • Viral Structural Proteins / metabolism*


  • P protein, Borna disease virus
  • Phosphoproteins
  • Viral Structural Proteins
  • Protein Kinase C