Regulation of the Borna disease virus polymerase complex by the viral nucleoprotein p38 isoform. Brief Report.
Borna disease virus (BDV) polymerase can be reconstituted by co-expression of the viral genes N, P and L. N codes for two proteins, p39 and p38, resulting from alternative translation initiation. Using a viral minireplicon system we observed that unlike p39, p38 was almost completely inactive when expressed with P and L alone. Since BDV polymerase requires a 10-20 fold excess of N protein over P for high activity, we determined whether p38 might serve as buffer that influences the viral N:P ratio. We demonstrate that p38 efficiently rescued BDV polymerase activity in cells expressing unfavorably high amounts of P.
Schneider
U
U
Department of Virology, University of Freiburg, Freiburg, Germany.
Naegele
M
M
Staeheli
P
P
D001891:Borna disease virus / Q000201:enzymology* / Q000502:physiology; D018387:Codon, Initiator; D015967:Gene Expression Regulation, Viral; D005814:Genes, Viral; D009698:Nucleoproteins / Q000235:genetics* / Q000502:physiology*; D014176:Protein Biosynthesis; D020033:Protein Isoforms / Q000235:genetics / Q000502:physiology; D012324:RNA-Dependent RNA Polymerase / Q000235:genetics / Q000378:metabolism*; D012093:Replicon; D017384:Sequence Deletion; D014764:Viral Proteins / Q000235:genetics / Q000502:physiology*; D014779:Virus Replication
D018387:Codon, Initiator; D009698:Nucleoproteins; D020033:Protein Isoforms; D014764:Viral Proteins; D012324:RNA-Dependent RNA Polymerase