Structure of vesicular stomatitis virus L-P-N0 complex by cyro-electron microscopy
- 1Department of Molecular Microbiology, Washington University in St. Louis School of Medicine, St Louis, MO 63110, USA.
- 2Centre International de Recherche en Infectiologie, Inserm U1111, CNRS UMR 5308, Université Claude Bernard Lyon 1, Ecole Normale Supérieure de Lyon, Lyon, France.
Abstract
The large protein (L) of nonsegmented, negative-strand RNA viruses, a viral order that includes rabies, Ebola, Nipah, and respiratory syncytial viruses, catalyze RNA-dependent RNA polymerization on nucleocapsid-sheathed RNA templates. L coordinates two distinct processes: messenger RNA (mRNA) transcription and genome replication. During transcription, L catalyzes cotranscriptional mRNA capping, methylation, and polyadenylation. The additional activities are not required during genome replication; instead, RNA synthesis is coupled to encapsidation by soluble nucleoprotein (N0) recruited by the phosphoprotein (P). We determined the structure of a vesicular stomatitis virus polymerase complex comprising L-P and N0. P directly engages the carboxyl-terminal domain of L (L_CTD) to anchor N0 in a continuum of conformations including a more stable configuration with N0 positioned at the RNA-product exit channel, poised for encapsidation. This study reveals a function for L_CTD in encapsidation of nascent RNAs and provides the structure of a polymerase complex required for genomic RNA replication.
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BibTeX
@article{bloyet2026structure,
title = {{Structure of vesicular stomatitis virus L-P-N0 complex by cyro-electron microscopy}},
author = {Louis-Marie Bloyet and Sean P. J. Whelan},
journal = {Science Advances},
year = {2026},
month = oct,
doi = {10.1126/sciadv.aej0664},
url = {https://www.science.org/doi/abs/10.1126/sciadv.aej0664},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Structure of vesicular stomatitis virus L-P-N0 complex by cyro-electron microscopy
AU - Louis-Marie Bloyet
AU - Sean P. J. Whelan
PY - 2026
DA - 2026/10/28
JO - Science Advances
DO - 10.1126/sciadv.aej0664
UR - https://www.science.org/doi/abs/10.1126/sciadv.aej0664
AB - The large protein (L) of nonsegmented, negative-strand RNA viruses, a viral order that includes rabies, Ebola, Nipah, and respiratory syncytial viruses, catalyze RNA-dependent RNA polymerization on nucleocapsid-sheathed RNA templates. L coordinates two distinct processes: messenger RNA (mRNA) transcription and genome replication. During transcription, L catalyzes cotranscriptional mRNA capping, methylation, and polyadenylation. The additional activities are not required during genome replication; instead, RNA synthesis is coupled to encapsidation by soluble nucleoprotein (N0) recruited by the phosphoprotein (P). We determined the structure of a vesicular stomatitis virus polymerase complex comprising L-P and N0. P directly engages the carboxyl-terminal domain of L (L_CTD) to anchor N0 in a continuum of conformations including a more stable configuration with N0 positioned at the RNA-product exit channel, poised for encapsidation. This study reveals a function for L_CTD in encapsidation of nascent RNAs and provides the structure of a polymerase complex required for genomic RNA replication.
SN - 2375-2548
ER -