ArticleNature communications2024
Structures of the mumps virus polymerase complex via cryo-electron microscopy.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Unreacted RSV Polymerase Structures Expand the Post-Translocation Landscape of the Nucleotide Addition Cycle.Microorganisms · 2026Article
- 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
- 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
- Allosteric pockets in the measles and Nipah virus polymerases: Mechanobiological insights and AI-driven drug discovery opportunities.Mechanobiology in medicine · 2025Article
- Structural insights into the dynamic mechanism of bornavirus polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- 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
- Cryo-EM structures of Nipah virus polymerases and high-throughput RdRp assay development enable anti-NiV drug discovery.Nature communications · 2025Article
- Structure of the measles virus ternary polymerase complex.Nature communications · 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
- Structural basis of Nipah virus RNA synthesis.Nature communications · 2025Article
- Article
- Recent advancements in the diverse roles of polymerase-associated proteins in the replication and pathogenesis of Newcastle disease virus.Veterinary research · 2025Review
- Structural basis of paramyxo- and pneumovirus polymerase inhibition by non-nucleoside small-molecule antivirals.Antimicrobial agents and chemotherapy · 2024Review
- How does the polymerase of non-segmented negative strand RNA viruses commit to transcription or genome replication?Journal of virology · 2024Review
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Authors and funding
8 authors.
Funding
Abstract
The viral polymerase complex, comprising the large protein (L) and phosphoprotein (P), is crucial for both genome replication and transcription in non-segmented negative-strand RNA viruses (nsNSVs), while structures corresponding to these activities remain obscure. Here, we resolved two L-P complex conformations from the mumps virus (MuV), a typical member of nsNSVs, via cryogenic-electron microscopy. One conformation presents all five domains of L forming a continuous RNA tunnel to the methyltransferase domain (MTase), preferably as a transcription state. The other conformation has the appendage averaged out, which is inaccessible to MTase. In both conformations, parallel P tetramers are revealed around MuV L, which, together with structures of other nsNSVs, demonstrates the diverse origins of the L-binding X domain of P. Our study links varying structures of nsNSV polymerase complexes with genome replication and transcription and points to a sliding model for polymerase complexes to advance along the RNA templates.
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