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J. Biol. Chem., Vol. 279, Issue 53, 55290-55296, December 31, 2004

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Overlap of Interaction Domains Indicates a Central Role of the P Protein in Assembly and Regulation of the Borna Disease Virus Polymerase Complex^*

Urs Schneider, Kareen Blechschmidt, Martin Schwemmle, and Peter Staeheli

From the Department of Virology, University of Freiburg, D-79104 Freiburg, Germany

The active polymerase complex of Borna disease virus is composed of the viral proteins N, P, and L. The viral X (negative regulatory factor) protein acts as a regulator of polymerase activity. Interactions of P with N and X were previously studied, but interactions with L were poorly defined. Using a mammalian two-hybrid system, we observed that L specifically interacts with P but not with N, X, or itself. Mapping of the L-binding domain in the P molecule revealed that it overlaps with two adjacent domains required for multimerization and interaction with N. Competition experiments showed that the interaction between L and P was inefficient when N was present, indicating that L may preferentially interact with free P in infected cells. Interestingly, a multimerization-defective P mutant maintained the ability to interact with L, N, and X but failed to support reporter gene expression from an artificial Borna disease virus minigenome. Furthermore, dominant negative effects on minigenome activity were only observed when P mutants with an intact multimerization domain were used, suggesting that P multimers, rather than monomers, exhibit biological activity. P mutants lacking functional interaction domains for L or N still formed complexes with these viral proteins when wild-type P was available as a bridging molecule, indicating that P multimers have the potential to act as scaffolds on which the RNA polymerase complex is assembled.

Received for publication, August 4, 2004 , and in revised form, October 6, 2004.

^* This work was supported by Grant SCHN 765/1-3 from the Deutsche Forschungsgemeinschaft. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a grant from the Swiss National Science Foundation. To whom correspondence may be addressed: Dept. of Virology, University of Freiburg, Hermann-Herder-Strasse 11, D-79104 Freiburg, Germany. Tel.: 49-761-203-6622; Fax: 49-761-203-5350; E-mail: urs.schneider{at}uniklinik-freiburg.de. To whom correspondence may be addressed: Dept. of Virology, University of Freiburg, Hermann-Herder-Strasse 11, D-79104 Freiburg, Germany. Tel.: 49-761-203-6579; Fax: 49-761-203-5350; E-mail: peter.staeheli{at}uniklinik-freiburg.de.

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