ArticleNature plants2025
Structural basis for the activation of plant bunyavirus replication machinery and its dual-targeted inhibition by ribavirin.
Article in Nature plants, 2025. 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 9 papers.
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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.
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Who cites it
9 citing papers in PubMed.
- Article
- Article
- Structures of the Crimean-Congo hemorrhagic fever virus RNA-dependent RNA polymerase.Cell discovery · 2026Article
- Structural and functional characterisation of the Crimean-Congo haemorrhagic fever virus RNA dependent RNA polymerase.Nature communications · 2026Article
- Contrasting Effects of Tagging Turnip Mosaic Virus Proteins.Pathogens (Basel, Switzerland) · 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
- Host ESCRT machinery orchestrates the assembly of tomato spotted wilt virus ribonucleoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The 6-kilodalton peptide 1 of the familyFrontiers in microbiology · 2025Review
Corrections and comments
- Erratum issued
Authors and funding
11 authors.
Funding
Abstract
Despite the discovery of plant viruses as a new class of pathogens over a century ago, the structure of plant virus replication machinery and antiviral pesticide remains lacking. Here we report five cryogenic electron microscopy structures of a ~330-kDa RNA-dependent RNA polymerase (RdRp) from a devastating plant bunyavirus, tomato spotted wilt orthotospovirus (TSWV), including the apo, viral-RNA-bound, base analogue ribavirin-bound and ribavirin-triphosphate-bound states. They reveal that a flexible loop of RdRp's motif F functions as 'sensor' to perceive viral RNA and further acts as an 'adaptor' to promote the formation of a complete catalytic centre. A ten-base RNA 'hook' structure is sufficient to trigger major conformational changes and activate RdRp. Chemical screening showed that ribavirin is effective against TSWV, and structural data revealed that ribavirin disrupts both hook-binding and catalytic core formation, locking polymerase in its inactive state. This work provides structural insights into the mechanisms of plant bunyavirus RdRp activation and its dual-targeted site inhibition, facilitating the development of pesticides against plant viruses.
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