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Structure of the vesicular stomatitis virus L protein in complex with Its phosphoprotein cofactor.

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Cell Reports. 2020 Jan 07;30(1):53-60.e5. doi: 10.1016/j.celrep.2019.12.024
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Structure of the vesicular stomatitis virus L protein in complex with Its phosphoprotein cofactor. Grigorieff Lab
Jenni S, Bloyet L, Diaz-Avalos R, Liang B, Whelan SP, Grigorieff N, Harrison SC
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Abstract

The large (L) proteins of non-segmented, negative-strand RNA viruses are multifunctional enzymes that produce capped, methylated, and polyadenylated mRNA and replicate the viral genome. A phosphoprotein (P), required for efficient RNA-dependent RNA polymerization from the viral ribonucleoprotein (RNP) template, regulates the 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 Å 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 an RNP template. The model shows that a conserved tryptophan in the priming loop can support the initiating 5' nucleotide.

PMID: 31914397 [PubMed - indexed for MEDLINE]

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