5VU2

Electron cryo-microscopy of "immature" Chikungunya VLP

5VU2 の概要

• エントリーDOI: 10.2210/pdb5vu2/pdb
• EMDBエントリー: 8734
• 分子名称: E1 envelope glycoprotein, E3 envelope glycoprotein, capsid protein, ... (5 entities in total)
• 機能のキーワード: chikungunya, virus, immature, virus like particle
• 由来する生物種: Chikungunya virus strain Senegal 37997 (CHIKV); 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 911444.03

構造登録者

Rossmann, M.G.,Yap, M.L. (登録日: 2017-05-18, 公開日: 2017-12-06, 最終更新日: 2024-10-16)

主引用文献

Yap, M.L.,Klose, T.,Urakami, A.,Hasan, S.S.,Akahata, W.,Rossmann, M.G.
Structural studies of Chikungunya virus maturation.
Proc. Natl. Acad. Sci. U.S.A., 114:13703-13707, 2017

PubMed Abstract: Cleavage of the alphavirus precursor glycoprotein p62 into the E2 and E3 glycoproteins before assembly with the nucleocapsid is the key to producing fusion-competent mature spikes on alphaviruses. Here we present a cryo-EM, 6.8-Å resolution structure of an "immature" Chikungunya virus in which the cleavage site has been mutated to inhibit proteolysis. The spikes in the immature virus have a larger radius and are less compact than in the mature virus. Furthermore, domains B on the E2 glycoproteins have less freedom of movement in the immature virus, keeping the fusion loops protected under domain B. In addition, the nucleocapsid of the immature virus is more compact than in the mature virus, protecting a conserved ribosome-binding site in the capsid protein from exposure. These differences suggest that the posttranslational processing of the spikes and nucleocapsid is necessary to produce infectious virus.

PubMed: 29203665
DOI: 10.1073/pnas.1713166114

実験手法

ELECTRON MICROSCOPY (6.8 Å)