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Journal of Virology, November 2000, p. 10212-10216, Vol. 74, No. 21
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Interaction of the Rabies Virus P Protein with the LC8 Dynein Light Chain

Hélène Raux, Anne Flamand, and Danielle Blondel*

Laboratoire de Génétique des Virus, CNRS, 91198 Gif sur Yvette, France

Received 3 April 2000/Accepted 26 July 2000

The rabies virus P protein is involved in viral transcription and replication but its precise function is not clear. We investigated the role of P (CVS strain) by searching for cellular partners by using a two-hybrid screening of a PC12 cDNA library. We isolated a cDNA encoding a 10-kDa dynein light chain (LC8). LC8 is a component of cytoplasmic dynein involved in the minus end-directed movement of organelles along microtubules. We confirmed that this molecule interacts with P by coimmunoprecipitation in infected cells and in cells transfected with a plasmid encoding P protein. LC8 was also detected in virus particles. Series of deletions from the N- and C-terminal ends of P protein were used to map the LC8-binding domain to the central part of P (residues 138 to 172). These results are relevant to speculate that dynein may be involved in the axonal transport of rabies virus along microtubules through neuron cells.

* Corresponding author. Mailing address: Laboratoire de Génétique des Virus, CNRS, 91198 Gif sur Yvette, France. Phone: (33) 1 69 82 38 37. Fax: (33) 1 69 82 43 08. E-mail: Danielle.Blondel{at}gv.cnrs-gif.fr.

Journal of Virology, November 2000, p. 10212-10216, Vol. 74, No. 21
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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