ArticleNature communications2020
Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 50 citations in OpenAlex.
- The La Crosse virus M segment determines virus isolate cell-to-cell spread and virulence.bioRxiv : the preprint server for biology · 2026Article
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- Genetic Adaptation Accompanying the Emergence of Inkoo Virus, the European Orthobunyavirus jamestownense.Annals of the New York Academy of Sciences · 2026Article
- Structures of the Crimean-Congo hemorrhagic fever virus RNA-dependent RNA polymerase.Cell discovery · 2026Article
- Mutation of a conserved lysine in the RdRp fingers domain broadly attenuates orthobunyaviruses.Communications biology · 2026Article
- Structural and functional characterisation of the Crimean-Congo haemorrhagic fever virus RNA dependent RNA polymerase.Nature communications · 2026Article
- Structure of Crimean-Congo haemorrhagic fever virus RNA polymerase.Nature microbiology · 2026Article
- Structural basis for RNA synthesis and inhibition of the orthobunyavirus polymerase.Nature communications · 2026Article
- Orchestrated and dynamic nucleotide addition cycle during respiratory syncytial virus early-stage elongation.Nature communications · 2026Article
- Human liver-derived organoids recapitulate Oropouche virus infection and manifestation, enabling antiviral drug discovery.Cell reports. Medicine · 2026Article
- Targeting the Rift Valley Fever Virus Polymerase: Resistance Mechanisms and Structural Insights.ACS infectious diseases · 2025Article
- Phylogenomics and structural modelling feature accelerated evolution of Oropouche virus: 1955 to 2024.Virologica Sinica · 2025Article
- Structural basis for the activation of plant bunyavirus replication machinery and its dual-targeted inhibition by ribavirin.Nature plants · 2025Article
- Structural characterization of the full-length Hantaan virus polymerase.PLoS pathogens · 2024Article
- Structural snapshots of phenuivirus cap-snatching and transcription.Nucleic acids research · 2024Article
- Structural basis for dimerization of a paramyxovirus polymerase complex.Nature communications · 2024Article
- Structural characterization of the oligomerization of full-length Hantaan virus polymerase into symmetric dimers and hexamers.Nature communications · 2024Article
- NMR side-chain assignments of the Crimean-Congo hemorrhagic fever virus glycoprotein n cytosolic domain.Magnetic resonance (Gottingen, Germany) · 2024Article
- Bunyavirales: Scientific Gaps and Prototype Pathogens for a Large and Diverse Group of Zoonotic Viruses.The Journal of infectious diseases · 2023Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bunyavirales is an order of segmented negative-strand RNA viruses comprising several life-threatening pathogens against which no effective treatment is currently available. Replication and transcription of the RNA genome constitute essential processes performed by the virally encoded multi-domain RNA-dependent RNA polymerase. Here, we describe the complete high-resolution cryo-EM structure of La Crosse virus polymerase. It reveals the presence of key protruding C-terminal domains, notably the cap-binding domain, which undergoes large movements related to its role in transcription initiation, and a zinc-binding domain that displays a fold not previously observed. We capture the polymerase structure at pre-initiation and elongation states, uncovering the coordinated movement of the priming loop, mid-thumb ring linker and lid domain required for the establishment of a ten-base-pair template-product RNA duplex before strand separation into respective exit tunnels. These structural details and the observed dynamics of key functional elements will be instrumental for structure-based development of polymerase inhibitors.
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