ArticleProceedings of the National Academy of Sciences of the United States of America2020
Structure of a rabies virus polymerase complex from electron cryo-microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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67 citing papers in PubMed, 102 citations in OpenAlex.
- Dog bite-associated pathogens: advances in pathogenic mechanisms and systemic clinical consequences in humans.One health (Amsterdam, Netherlands) · 2026Review
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- Targeting the RSV and hMPV L Protein: Cryo-EM and Structure-Based Approaches to Antiviral Drug Discovery.Biomolecules · 2026Review
- Small Molecule Inhibition of Mononegavirales RNA Polymerases.Journal of medical virology · 2026Review
- Orchestrated and dynamic nucleotide addition cycle during respiratory syncytial virus early-stage elongation.Nature communications · 2026Article
- Structural insights into measles virus RNA synthesis regulation and pan-paramyxoviral polymerase inhibition by ERDRP-0519.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Assembly of the Linear Viral Nucleocapsid.Microorganisms · 2026Article
- Rabies lyssavirus phosphoprotein possesses RNA duplex-unwinding activities.Molecular therapy. Nucleic acids · 2026Article
- Mumps Virus: Replication, Immune Response, and the Changing Landscape of Vaccine Effectiveness.Pathogens (Basel, Switzerland) · 2026Review
- Structure and function of the RNA polymerase complex of Borna disease virus, a nuclear-replicating non-segmented negative-strand RNA virus.Nucleic acids research · 2026Article
- Putative Novel Viruses in the FamiliesAdvances in virology · 2026Article
- The structure of the mammalian bornavirus polymerase complex.Nature communications · 2025Article
- Cryo-EM structures of Nipah virus polymerase complex reveal highly varied interactions between L and P proteins among paramyxoviruses.Protein & cell · 2025Article
- Article
- Cryo-EM structures of Nipah virus polymerases and high-throughput RdRp assay development enable anti-NiV drug discovery.Nature communications · 2025Article
- Oral dosing of the nucleoside analog obeldesivir is efficacious against RSV infection in African green monkeys.Nature communications · 2025Article
- The Challenge of Lyssavirus Infections in Domestic and Other Animals: A Mix of Virological Confusion, Consternation, Chagrin, and Curiosity.Pathogens (Basel, Switzerland) · 2025Review
- Genomic Characterization and Pathogenicity of a Novel Birnavirus Strain Isolated from Mandarin Fish (Genes · 2025Article
- Functional dissection of the C-terminal domain of rabies virus RNA polymerase L protein.Journal of virology · 2025Article
- Structural insights into the RNA-dependent RNA polymerase complexes from highly pathogenic Marburg and Ebola viruses.Nature communications · 2025Article
7 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Nonsegmented negative-stranded (NNS) RNA viruses, among them the virus that causes rabies (RABV), include many deadly human pathogens. The large polymerase (L) proteins of NNS RNA viruses carry all of the enzymatic functions required for viral messenger RNA (mRNA) transcription and replication: RNA polymerization, mRNA capping, and cap methylation. We describe here a complete structure of RABV L bound with its phosphoprotein cofactor (P), determined by electron cryo-microscopy at 3.3 Å resolution. The complex closely resembles the vesicular stomatitis virus (VSV) L-P, the one other known full-length NNS-RNA L-protein structure, with key local differences (e.g., in L-P interactions). Like the VSV L-P structure, the RABV complex analyzed here represents a preinitiation conformation. Comparison with the likely elongation state, seen in two structures of pneumovirus L-P complexes, suggests differences between priming/initiation and elongation complexes. Analysis of internal cavities within RABV L suggests distinct template and product entry and exit pathways during transcription and replication.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.