9FYA

Structure of the Sabia Virus spike complex in a closed conformation

9FYA の概要

• エントリーDOI: 10.2210/pdb9fya/pdb
• EMDBエントリー: 50862
• 分子名称: Glycoprotein G2, Glycoprotein G1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: class-i spike complex, viral protein
• 由来する生物種: Sabia virus; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 169451.94

構造登録者

Diskin, R.,Cohen-Dvashi, H. (登録日: 2024-07-03, 公開日: 2025-06-11, 最終更新日: 2025-09-17)

主引用文献

Cohen-Dvashi, H.,Katz, M.,Diskin, R.
Metal-induced conformational changes in the Sabia virus spike complex.
Nat Microbiol, 10:2221-2230, 2025

PubMed Abstract: Haemorrhagic fever viruses from the Arenaviridae are a source of concern owing to their potential to cause lethal outbreaks and the lack of effective therapeutics. While structures of spike proteins from 'Old World' arenaviruses are available, the differences and similarities to 'New World' arenaviruses, such as the Sabiá virus, remain unclear owing to the lack of New World spike structures. Here we present the structure of the isolated spike complex from the Sabiá virus, which mediates viral attachment and entry to the host cells, using single-particle cryo-electron microscopy. We find two distinct conformational states of the spike, representing its native closed state at 2.6 Å resolution and an open state at 2.9 Å resolution that it assumes during cell entry. In addition, we show that the opening of the spike and subsequent cell entry are dependent on acidic pH and an unidentified metal ion. Our study suggests potential differences in the cell entry mechanisms of clade B arenaviruses compared with others in the Arenaviridae family.

PubMed: 40751015
DOI: 10.1038/s41564-025-02075-8

実験手法

ELECTRON MICROSCOPY (2.64 Å)