Regulation of the Borna disease virus polymerase complex by the viral nucleoprotein p38 isoform

Regulation of the Borna disease virus polymerase complex by the viral nucleoprotein p38 isoform 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Regulation of the Borna disease virus polymerase complex by the viral nucleoprotein p38 isoform

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Publisher
Springer Journals
Copyright
Copyright © 2004 by Springer-Verlag/Wien
Subject
LifeSciences
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-004-0327-6
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Archives of VirologySpringer Journals

Published: Jul 1, 2004

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