8PPQ

Tick-borne encephalitis virus Kuutsalo-14 prM3E3 trimer

8PPQ の概要

• エントリーDOI: 10.2210/pdb8ppq/pdb
• EMDBエントリー: 17808
• 分子名称: Envelope protein E, Protein prM, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: complex, spike, fusion protein, glycosylation, transmembrane protein, maturation, virus, trimer, hexamer, dimer
• 由来する生物種: Tick-borne encephalitis virus; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 215568.44

構造登録者

Anastasina, M.,Domanska, A.,Pulkkinen, L.I.A.,Butcher, S.J. (登録日: 2023-07-07, 公開日: 2024-06-12, 最終更新日: 2024-10-23)

主引用文献

Anastasina, M.,Fuzik, T.,Domanska, A.,Pulkkinen, L.I.A.,Smerdova, L.,Formanova, P.P.,Strakova, P.,Novacek, J.,Ruzek, D.,Plevka, P.,Butcher, S.J.
The structure of immature tick-borne encephalitis virus supports the collapse model of flavivirus maturation.
Sci Adv, 10:eadl1888-eadl1888, 2024

PubMed Abstract: We present structures of three immature tick-borne encephalitis virus (TBEV) isolates. Our atomic models of the major viral components, the E and prM proteins, indicate that the pr domains of prM have a critical role in holding the heterohexameric prM3E3 spikes in a metastable conformation. Destabilization of the prM furin-sensitive loop at acidic pH facilitates its processing. The prM topology and domain assignment in TBEV is similar to the mosquito-borne Binjari virus, but is in contrast to other immature flavivirus models. These results support that prM cleavage, the collapse of E protein ectodomains onto the virion surface, the large movement of the membrane domains of both E and M, and the release of the pr fragment from the particle render the virus mature and infectious. Our work favors the collapse model of flavivirus maturation warranting further studies of immature flaviviruses to determine the sequence of events and mechanistic details driving flavivirus maturation.

PubMed: 38959313
DOI: 10.1126/sciadv.adl1888

実験手法

ELECTRON MICROSCOPY (3.9 Å)