Archives of Virology

, Volume 155, Issue 5, pp 789–793 | Cite as

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

  • Sonja Schmid
  • Philippe Metz
  • Christine M. A. Prat
  • Daniel Gonzalez-Dunia
  • Martin Schwemmle
Brief Report


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.


Rabies Vero Cell Polymerase Activity Viral Life Cycle Human Respiratory Syncytial Virus 
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This work was supported by the Deutsche Forschungsgemeinschaft. We thank members of the Schwemmle and Gonzalez-Dunia labs for critical reading of the manuscript.


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Copyright information

© Springer-Verlag 2010

Authors and Affiliations

  • Sonja Schmid
    • 1
    • 3
  • Philippe Metz
    • 1
    • 4
  • Christine M. A. Prat
    • 2
  • Daniel Gonzalez-Dunia
    • 2
  • Martin Schwemmle
    • 1
  1. 1.Department of Virology, Institute for Medical Microbiology and HygieneUniversity of FreiburgFreiburgGermany
  2. 2.INSERM U563, Centre de Physiopathologie de Toulouse PurpanUniversité Paul-SabatierToulouseFrance
  3. 3.Department of MicrobiologyMount Sinai School of MedicineNew YorkUSA
  4. 4.Department of Molecular VirologyUniversity of HeidelbergHeidelbergGermany

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