ArticleNature communications2024
Structural characterization of the oligomerization of full-length Hantaan virus polymerase into symmetric dimers and hexamers.
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 10 papers.
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Who cites it
10 citing papers in PubMed, 7 citations in OpenAlex.
- 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
- 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
- Hantavirus L protein exhibits shutoff activity mediated by its N-terminal endonuclease domain.Scientific reports · 2026Article
- Characterization of minigenome systems for Hantaan and Seoul hantaviruses.Virus research · 2026Article
- The structure of the mammalian bornavirus polymerase complex.Nature communications · 2025Article
- Structural basis for the activation of plant bunyavirus replication machinery and its dual-targeted inhibition by ribavirin.Nature plants · 2025Article
- Structural snapshots of phenuivirus cap-snatching and transcription.Nucleic acids research · 2024Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Hantaan virus is a dangerous human pathogen whose segmented negative-stranded RNA genome is replicated and transcribed by a virally-encoded multi-functional polymerase. Here we describe the complete cryo-electron microscopy structure of Hantaan virus polymerase in several oligomeric forms. Apo polymerase protomers can adopt two drastically different conformations, which assemble into two distinct symmetric homodimers, that can themselves gather to form hexamers. Polymerase dimerization induces the stabilization of most polymerase domains, including the C-terminal domain that contributes the most to dimer's interface, along with a lariat region that participates to the polymerase steadying. Binding to viral RNA induces significant conformational changes resulting in symmetric oligomer disruption and polymerase activation, suggesting the possible involvement of apo multimers as protecting systems that would stabilize the otherwise flexible C-terminal domains. Overall, these results provide insights into the multimerization capability of Hantavirus polymerase and may help to define antiviral compounds to counteract these life-threatening viruses.
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