8QRH
Inactivated tick-borne encephalitis virus (TBEV) vaccine strain Sofjin-Chumakov
Summary for 8QRH
| Entry DOI | 10.2210/pdb8qrh/pdb |
| EMDB information | 18614 |
| Descriptor | Genome polyprotein, Small envelope protein M, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | tbev, flavivirus, virion envelope, viral protein |
| Biological source | Orthoflavivirus encephalitidis (Envelope Protein (E)) More |
| Total number of polymer chains | 6 |
| Total formula weight | 184718.11 |
| Authors | Moiseenko, A.V.,Zhang, Y.,Vorovitch, M.,Ivanova, A.,Liu, Z.,Osolodkin, D.I.,Egorov, A.,Ishmukhametov, A.,Sokolova, O.S. (deposition date: 2023-10-07, release date: 2024-06-05, Last modification date: 2024-11-06) |
| Primary citation | Pichkur, E.B.,Vorovitch, M.F.,Ivanova, A.L.,Protopopova, E.V.,Loktev, V.B.,Osolodkin, D.I.,Ishmukhametov, A.A.,Samygina, V.R. The structure of inactivated mature tick-borne encephalitis virus at 3.0 angstrom resolution. Emerg Microbes Infect, 13:2313849-2313849, 2024 Cited by PubMed 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. PubMed: 38465849DOI: 10.1080/22221751.2024.2313849 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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