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Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor

By Simon Jenni, Louis-Marie Bloyet, Ruben Diaz-Avalos, Bo Liang, Sean P. J. Whelan, Nikolaus Grigorieff, Stephen C. Harrison

Posted 03 Oct 2019
bioRxiv DOI: 10.1101/792960 (published DOI: 10.1016/j.celrep.2019.12.024)

The large (L) proteins of non-segmented, negative-strand RNA viruses are multifunctional enzymes that produce capped, methylated and polyadenylated mRNAs and replicate the viral genome. A phosphoprotein (P), required for efficient RNA-dependent RNA polymerization from the viral ribonucleoprotein (RNP) template, regulates function and conformation of the L protein. We report the structure of vesicular stomatitis virus L in complex with its P cofactor determined by electron cryomicroscopy at 3.0 A resolution, enabling us to visualize bound segments of P. The contacts of three P segments with multiple L domains show how P induces a closed, compact, initiation-competent conformation. Binding of P to L positions its N-terminal domain adjacent to a putative RNA exit channel for efficient encapsidation of newly synthesized genomes with the nucleoprotein and orients its C-terminal domain to interact with the RNP template. The model shows that a conserved tryptophan in the priming loop can support the initiating 5'-nucleotide.

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