@article{mbs:/content/journal/jgv/10.1099/0022-1317-82-11-2691, author = "Poisson, Nicolas and Real, Eleonore and Gaudin, Yves and Vaney, Marie-Christine and King, Stephen and Jacob, Yves and Tordo, Noël and Blondel, Danielle", title = "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", journal= "Journal of General Virology", year = "2001", volume = "82", number = "11", pages = "2691-2696", doi = "https://doi.org/10.1099/0022-1317-82-11-2691", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-82-11-2691", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "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.", }