3J2W

Electron cryo-microscopy of Chikungunya virus

3J2W の概要

• エントリーDOI: 10.2210/pdb3j2w/pdb
• 関連するPDBエントリー: 3J2X 3J2Y 3J2Z 3J30 4GQ8
• EMDBエントリー: 5577
• 分子名称: Glycoprotein E1, Glycoprotein E2, Capsid protein, ... (6 entities in total)
• 機能のキーワード: e1-e2 glycoprotein, nucleocapsid protein, transmembrane helix, virus
• 由来する生物種: Chikungunya virus (CHIKV); 詳細
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 441693.44

構造登録者

Sun, S.,Xiang, Y.,Rossmann, M.G. (登録日: 2013-01-28, 公開日: 2013-04-24, 最終更新日: 2024-11-06)

主引用文献

Sun, S.,Xiang, Y.,Akahata, W.,Holdaway, H.,Pal, P.,Zhang, X.,Diamond, M.S.,Nabel, G.J.,Rossmann, M.G.
Structural analyses at pseudo atomic resolution of Chikungunya virus and antibodies show mechanisms of neutralization.
Elife, 2:e00435-e00435, 2013

PubMed Abstract: A 5.3 Å resolution, cryo-electron microscopy (cryoEM) map of Chikungunya virus-like particles (VLPs) has been interpreted using the previously published crystal structure of the Chikungunya E1-E2 glycoprotein heterodimer. The heterodimer structure was divided into domains to obtain a good fit to the cryoEM density. Differences in the T = 4 quasi-equivalent heterodimer components show their adaptation to different environments. The spikes on the icosahedral 3-fold axes and those in general positions are significantly different, possibly representing different phases during initial generation of fusogenic E1 trimers. CryoEM maps of neutralizing Fab fragments complexed with VLPs have been interpreted using the crystal structures of the Fab fragments and the VLP structure. Based on these analyses the CHK-152 antibody was shown to stabilize the viral surface, hindering the exposure of the fusion-loop, likely neutralizing infection by blocking fusion. The CHK-9, m10 and m242 antibodies surround the receptor-attachment site, probably inhibiting infection by blocking cell attachment. DOI:http://dx.doi.org/10.7554/eLife.00435.001.

PubMed: 23577234
DOI: 10.7554/eLife.00435

実験手法

ELECTRON MICROSCOPY (5 Å)