9SWK
Immature TBEV envelope spike with interaction partners underneath - SPA
Summary for 9SWK
| Entry DOI | 10.2210/pdb9swk/pdb |
| EMDB information | 55311 |
| Descriptor | Envelope protein E, Protein prM, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | tick borne encephalitis virus, envelope, flavivirus, spike, virus, asymmetric, immature particle, spa |
| Biological source | Tick-borne encephalitis virus More |
| Total number of polymer chains | 9 |
| Total formula weight | 376991.04 |
| Authors | Fuzik, T.,Plevka, P.,Smerdova, L.,Nepovimova, L. (deposition date: 2025-10-07, release date: 2026-05-20, Last modification date: 2026-07-29) |
| Primary citation | Fuzik, T.,Anastasina, M.,Pajtinka, P.,Domanska, A.,Pulkkinen, L.I.A.,Smerdova, L.,Nepovimova, L.,Formanova-Pokorna, P.,Strakova, P.,Novacek, J.,Ruzek, D.,Vacha, R.,Butcher, S.J.,Plevka, P. Structures of asymmetric particles of tick-borne encephalitis virus provide insight into flavivirus assembly and maturation. Sci Adv, 12:eaee4765-eaee4765, 2026 Cited by PubMed Abstract: Flaviviruses are globally distributed human pathogens. However, the mechanisms underlying flavivirus assembly and maturation remain poorly understood. Here, we show that many particles of tick-borne encephalitis virus (TBEV) are asymmetric and lack subsets of surface heterodimers. Immature particles of TBEV contain incomplete spikes, providing evidence that their coats assemble directly from heterodimers of premembrane (prM) and envelope (E) proteins. Exposure of TBEV particles to acidic pH in the Golgi complex promotes maturation. The spikes and herringbone regions in TBEV maturation intermediates are oriented randomly rather than conforming to a common icosahedral symmetry. Consequently, the mature herringbone lattice forms around a randomly oriented nucleation center, expanding by addition of membrane-envelope heterodimers as the spikes disassemble and prMs are cleaved. The observed incompleteness of the protein coats explains, as an alternative to particle breathing, how flaviviruses can be neutralized by antibodies that bind to regions of E proteins normally inaccessible in the spiky or herringbone structures. PubMed: 42397903DOI: 10.1126/sciadv.aee4765 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.57 Å) |
Structure validation
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