RT Journal Article SR Electronic(1) A1 Poisson, Nicolas A1 Real, Eleonore A1 Gaudin, Yves A1 Vaney, Marie-Christine A1 King, Stephen A1 Jacob, Yves A1 Tordo, Noël A1 Blondel, DanielleYR 2001 T1 Molecular basis for the interaction between rabies virus phosphoprotein P and the dynein light chain LC8: dissociation of dynein-binding properties and transcriptional functionality of P JF Journal of General Virology, VO 82 IS 11 SP 2691 OP 2696 DO https://doi.org/10.1099/0022-1317-82-11-2691 PB Microbiology Society, SN 1465-2099, AB 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., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-82-11-2691