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Animal: RNA Viruses |
Laboratoire de Génétique des Virus, CNRS, 91198 Gif sur Yvette, France1
Laboratoire des Lyssavirus, Institut Pasteur 25 rue du Dr Roux, 75724 Paris Cedex 15, France2
Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, Connecticut 06030-3305, USA3
Author for correspondence: Danielle Blondel. Fax +33 1 69 82 43 08. e-mail Danielle.Blondel{at}gv.cnrs-gif.fr
The lyssavirus phosphoprotein P is a co-factor of the viral RNA polymerase and plays a central role in virus transcription and replication. It has been shown previously that P interacts with the dynein light chain LC8, which is involved in minus end-directed movement of organelles along microtubules. Co-immunoprecipitation experiments and the two-hybrid system were used to map the LC8-binding site to the sequence 139RSSEDKSTQTTGR151. Site-directed mutagenesis of residues D143 and Q147 to an A residue abolished binding to LC8. The P–LC8 association is not required for virus transcription, since the double mutant was not affected in its transcription ability in a minigenome assay. Based on the crystal structure of LC8 bound to a peptide from neuronal nitric oxide synthase, a model for the complex between the peptide spanning residues 140–150 of P and LC8 is proposed. This model suggests that P binds LC8 in a manner similar to other LC8 cellular partners.
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