ArticleNature microbiology2020
Structure of severe fever with thrombocytopenia syndrome virus L protein elucidates the mechanisms of viral transcription initiation.
Article in Nature microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
43 citing papers in PubMed.
- Evaluation of new adjuvants in enhancing the immune response to a candidate of Severe Fever with Thrombocytopenia Syndrome Virus vaccine.bioRxiv : the preprint server for biology · 2026Article
- Phylogeographic epidemiology of Dabie bandavirus in East Asia: divergent transmission networks and genotype‑linked clinical severity.Infectious diseases of poverty · 2026Article
- Article
- Phylogenetic and biological features of severe fever with thrombocytopenia syndrome virus from multi-species infections in eastern China.Microbiology spectrum · 2026Article
- Structures of the Crimean-Congo hemorrhagic fever virus RNA-dependent RNA polymerase.Cell discovery · 2026Article
- Review
- 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
- Transcriptomic and RNA Modification Landscape of Severe Fever with Thrombocytopenia Syndrome Virus Revealed by Nanopore Direct RNA Sequencing.Microorganisms · 2026Article
- Review
- Targeting the Rift Valley Fever Virus Polymerase: Resistance Mechanisms and Structural Insights.ACS infectious diseases · 2025Article
- Identification of Licoflavone C as a cap-dependent endonuclease inhibitor against severe fever with thrombocytopenia syndrome virus.Acta pharmacologica Sinica · 2025Article
- Structural basis for the activation of plant bunyavirus replication machinery and its dual-targeted inhibition by ribavirin.Nature plants · 2025Article
- Identification of lurasidone as a potent inhibitor of severe fever with thrombocytopenia syndrome virus by targeting the viral nucleoprotein.Frontiers in microbiology · 2025Article
- Structural characterization of the full-length Hantaan virus polymerase.PLoS pathogens · 2024Article
- N6-methyladenosine RNA modification promotes Severe Fever with Thrombocytopenia Syndrome Virus infection.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
Corrections and comments
- Commented on by
- Commented on by
- Erratum issued
Authors and funding
15 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Segmented negative-sense RNA viruses (sNSRVs) encode a single-polypeptide polymerase (L protein) or a heterotrimeric polymerase complex to cannibalize host messenger RNA cap structures serving as primers of transcription, and catalyse RNA synthesis. Here, we report the full-length structure of the severe fever with thrombocytopaenia syndrome virus (SFTSV) L protein, as determined by cryogenic electron microscopy at 3.4 Å, leading to an atomic model harbouring three functional parts (an endonuclease, an RNA-dependent RNA polymerase and a cap-binding domain) and two structural domains (an arm domain with a blocker motif and a carboxy-terminal lariat domain). The SFTSV L protein has a compact architecture in which its cap-binding pocket is surprisingly occupied by an Arg finger of the blocker motif, and the endonuclease active centre faces back towards the cap-binding pocket, suggesting that domain rearrangements are necessary to acquire the pre-initiation state of the active site. Our results provide insight into the complete architecture of sNSRV-encoded L protein and further the understanding of sNSRV transcription initiation.
Indexed as
Identifiers
32341479What OpenQuestion holds
Registered trials
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.