8OLE

Cryo-EM reconstruction of VP4 assembly from SA11 Rotavirus Non-Tripsinized Triple Layered Particle

これはPDB形式変換不可エントリーです。

8OLE の概要

• エントリーDOI: 10.2210/pdb8ole/pdb
• EMDBエントリー: 16956
• 分子名称: Outer capsid protein VP4 (1 entity in total)
• 機能のキーワード: rotavirus, dsrna virus, virus
• 由来する生物種: Rotavirus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 260249.67

構造登録者

Asensio-Cob, D.,Perez-Mata, C.,Gomez-Blanco, J.,Vargas, J.,Rodriguez, J.M.,Luque, D. (登録日: 2023-03-30, 公開日: 2024-09-25, 最終更新日: 2025-10-08)

主引用文献

Asensio-Cob, D.,Mata, C.P.,Gomez-Blanco, J.,Vargas, J.,Rodriguez, J.M.,Luque, D.
Structural determinants of rotavirus proteolytic activation.
Plos Pathog., 21:e1013063-e1013063, 2025

PubMed Abstract: The infectivity of rotavirus (RV), the leading cause of childhood diarrhea, hinges on the activation of viral particles through the proteolysis of the spike protein by trypsin-like proteases in the host intestinal lumen. In order to determine the structural basis of trypsin activation, we have used cryogenic electron microscopy (cryo-EM) and advanced image processing methods to compare uncleaved and cleaved RV particles. We find that the conformation of the non-proteolyzed spike is constrained by the position of loops that surround its structure, linking the lectin domains of the spike head to its body. The proteolysis of these loops removes this structural constraint, thereby enabling the spike to undergo the necessary conformational changes required for cell membrane penetration. Thus, these loops function as regulatory elements to ensure that the spike protein is activated precisely when and where it is needed to facilitate a successful infection.

PubMed: 40794814
DOI: 10.1371/journal.ppat.1013063

実験手法

ELECTRON MICROSCOPY (4.4 Å)