8AAY

Nudaurelia capensis omega virus maturation intermediate captured at pH5.6 (insect cell expressed VLPs): small class from symmetry expansion

8AAY の概要

• エントリーDOI: 10.2210/pdb8aay/pdb
• EMDBエントリー: 15307
• 分子名称: p70 (1 entity in total)
• 機能のキーワード: icosahedral virus, auto-catalytic cleavage, virus maturation, virus-like particle, virus like particle
• 由来する生物種: Nudaurelia capensis omega virus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 279567.81

構造登録者

Castells-Graells, R.,Hesketh, E.L.,Johnson, J.E.,Ranson, N.A.,Lawson, D.M.,Lomonossoff, G.P. (登録日: 2022-07-04, 公開日: 2022-12-28, 最終更新日: 2026-03-18)

主引用文献

Castells-Graells, R.,Hesketh, E.L.,Matsui, T.,Johnson, J.E.,Ranson, N.A.,Lawson, D.M.,Lomonossoff, G.P.
Unraveling the maturation pathway of a eukaryotic virus through cryo-EM.
Proc.Natl.Acad.Sci.USA, 123:e2420493123-e2420493123, 2026

PubMed Abstract: Virus maturation is a fundamental biological process involving large-scale structural reorganizations that drive functional activation and lead to infectivity. Understanding the steps from the initial procapsid assembly to mature virions is essential, both for comprehending viral life cycles and for developing antiviral therapies. However, capturing these steps has been challenging due to the transient and elusive nature of intermediate states. The nonenveloped, T = 4, ssRNA-containing, omega virus (NωV) is a highly accessible model system that exemplifies the maturation process of a eukaryotic virus. During maturation, the particle shrinks in outer diameter from 482 Å (pH 7.6) to 428 Å (pH 5.0). It is possible to mimic the maturation process in vitro by lowering the pH of a population of procapsids produced in heterologous systems. Indeed, by controlling the pH in vitro, it is possible to produce homogenous populations of intermediate NωV virus-like particles (VLPs) that occur too fleetingly to be observed in vivo. Here, we report structural models, based on cryoelectron microscopy (cryo-EM), of five intermediates in the NωV maturation process. The structures of the intermediate particles reveal unique, quaternary position-dependent trajectories and refolding of subunit N and C-terminal regions, including the formation of the autocatalytic cleavage site at N570. The detailed structures reported here, coupled with previously determined structures of the procapsids and mature particles, allow the maturation pathway to be described in detail for a eukaryotic virus.

PubMed: 41739563
DOI: 10.1073/pnas.2420493123

実験手法

ELECTRON MICROSCOPY (3.39 Å)