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Short Communication |
1 Abteilung Virologie, Institut für Medizinische Mikrobiologie & Hygiene, Universität Freiburg, D-79104 Freiburg, Germany
2 Robert-Koch-Institut, Nordufer 20, D-13353 Berlin, Germany
Correspondence
Peter Staeheli
staeheli{at}ukl.uni-freiburg.de
Urs Schneider
ursschn{at}ukl.uni-freiburg.de
Borna disease virus polymerase activity is negatively regulated by the viral X protein. Using a virus minireplicon system it was found that all X mutants that no longer interacted with the viral P protein failed to exhibit significant inhibitory activity. The action of X could further be neutralized by expression of a P fragment that contained the X interaction domain but lacked all domains known to mediate interaction with other viral proteins. X thus appears to regulate the activity of the Borna disease virus polymerase by targeting the polymerase cofactor P.
This article has been cited by other articles:
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  M. Poenisch, P. Staeheli, and U. Schneider Viral accessory protein X stimulates the assembly of functional Borna disease virus polymerase complexes J. Gen. Virol., June 1, 2008; 89(6): 1442 - 1445. [Abstract] [Full Text] [PDF]
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 A. Ackermann, P. Staeheli, and U. Schneider Adaptation of Borna Disease Virus to New Host Species Attributed to Altered Regulation of Viral Polymerase Activity J. Virol., August 1, 2007; 81(15): 7933 - 7940. [Abstract] [Full Text] [PDF]
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M. Poenisch, S. Wille, A. Ackermann, P. Staeheli, and U. Schneider The X Protein of Borna Disease Virus Serves Essential Functions in the Viral Multiplication Cycle J. Virol., July 1, 2007; 81(13): 7297 - 7299. [Abstract] [Full Text] [PDF]
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S. Schmid, D. Mayer, U. Schneider, and M. Schwemmle Functional Characterization of the Major and Minor Phosphorylation Sites of the P Protein of Borna Disease Virus J. Virol., June 1, 2007; 81(11): 5497 - 5507. [Abstract] [Full Text] [PDF]
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A. Martin, P. Staeheli, and U. Schneider RNA Polymerase II-Controlled Expression of Antigenomic RNA Enhances the Rescue Efficacies of Two Different Members of the Mononegavirales Independently of the Site of Viral Genome Replication. J. Virol., June 1, 2006; 80(12): 5708 - 5715. [Abstract] [Full Text] [PDF]
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H. Yanai, T. Kobayashi, Y. Hayashi, Y. Watanabe, N. Ohtaki, G. Zhang, J. C. de la Torre, K. Ikuta, and K. Tomonaga A Methionine-Rich Domain Mediates CRM1-Dependent Nuclear Export Activity of Borna Disease Virus Phosphoprotein J. Virol., February 1, 2006; 80(3): 1121 - 1129. [Abstract] [Full Text] [PDF]
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M. Schwardt, D. Mayer, R. Frank, U. Schneider, M. Eickmann, O. Planz, T. Wolff, and M. Schwemmle The negative regulator of Borna disease virus polymerase is a non-structural protein J. Gen. Virol., November 1, 2005; 86(11): 3163 - 3169. [Abstract] [Full Text] [PDF]
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 U. Schneider, K. Blechschmidt, M. Schwemmle, and P. Staeheli Overlap of Interaction Domains Indicates a Central Role of the P Protein in Assembly and Regulation of the Borna Disease Virus Polymerase Complex J. Biol. Chem., December 31, 2004; 279(53): 55290 - 55296. [Abstract] [Full Text] [PDF]
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