ArticleEmerging microbes & infections2024
The structure of inactivated mature tick-borne encephalitis virus at 3.0 Å resolution.
Article in Emerging microbes & infections, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Irreversible furin cleavage site exposure renders immature tick-borne flaviviruses fully infectious.Nature communications · 2025Article
- Atomic-resolution structure of a chimeric Powassan tick-borne flavivirus.Science advances · 2025Article
- Live Imaging and Interactome Analysis of Zika and Chikungunya Viral RNAs Via Dual-Action Aptamer Tag.Research square · 2025Article
- MPicker: visualizing and picking membrane proteins for cryo-electron tomography.Nature communications · 2025Article
- Article
- Structural diversity of tick-borne encephalitis virus particles in the inactivated vaccine based on strain Sofjin.Emerging microbes & infections · 2024Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tick-borne encephalitis virus (TBEV) causes a severe disease, tick-borne encephalitis (TBE), that has a substantial epidemiological importance for Northern Eurasia. Between 10,000 and 15,000 TBE cases are registered annually despite the availability of effective formaldehyde-inactivated full-virion vaccines due to insufficient vaccination coverage, as well as sporadic cases of vaccine breakthrough. The development of improved vaccines would benefit from the atomic resolution structure of the antigen. Here we report the refined single-particle cryo-electron microscopy (cryo-EM) structure of the inactivated mature TBEV vaccine strain Sofjin-Chumakov (Far-Eastern subtype) at a resolution of 3.0 Å. The increase of the resolution with respect to the previously published structures of TBEV strains Hypr and Kuutsalo-14 (European subtype) was reached due to improvement of the virus sample quality achieved by the optimized preparation methods. All the surface epitopes of TBEV were structurally conserved in the inactivated virions. ELISA studies with monoclonal antibodies supported the hypothesis of TBEV protein shell cross-linking upon inactivation with formaldehyde.
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Registered trials
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