Literature DB >> 15221540

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

U Schneider1, M Naegele, P Staeheli.   

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.

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Year:  2004        PMID: 15221540     DOI: 10.1007/s00705-004-0327-6

Source DB:  PubMed          Journal:  Arch Virol        ISSN: 0304-8608            Impact factor:   2.574


  3 in total

1.  Splicing-Dependent Subcellular Targeting of Borna Disease Virus Nucleoprotein Isoforms.

Authors:  Shohei Kojima; Ryo Sato; Mako Yanai; Yumiko Komatsu; Masayuki Horie; Manabu Igarashi; Keizo Tomonaga
Journal:  J Virol       Date:  2019-02-19       Impact factor: 5.103

2.  Adaptation of Borna disease virus to new host species attributed to altered regulation of viral polymerase activity.

Authors:  Andreas Ackermann; Peter Staeheli; Urs Schneider
Journal:  J Virol       Date:  2007-05-23       Impact factor: 5.103

Review 3.  Nucleocytoplasmic shuttling of viral proteins in borna disease virus infection.

Authors:  Tomoyuki Honda; Keizo Tomonaga
Journal:  Viruses       Date:  2013-08-08       Impact factor: 5.048

  3 in total

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