The structure of inactivated mature tick-borne encephalitis virus at 3.0 Å resolution

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...

Full description

Saved in:
Bibliographic Details
Published in:Emerging microbes & infections 2024-12, Vol.13 (1), p.2313849
Main Authors: Pichkur, Evgeny B, Vorovitch, Mikhail F, Ivanova, Alla L, Protopopova, Elena V, Loktev, Valery B, Osolodkin, Dmitry I, Ishmukhametov, Aydar A, Samygina, Valeriya R
Format: Article
Language:English
Subjects:
Antibodies, Viral
Arachnids
Cryo-electron microscopy
Cryoelectron Microscopy
Encephalitis
Encephalitis Viruses, Tick-Borne
Encephalitis, Tick-Borne
Formaldehyde
Humans
inactivated vaccines
structural virology
tick-borne encephalitis virus
Vaccines
Vaccines, Inactivated
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:2222-1751
2222-1751
DOI:10.1080/22221751.2024.2313849