3J2Z

Electron Cryo-microscopy of Chikungunya VLP in complex with neutralizing antibody Fab m10

3J2Z の概要

• エントリーDOI: 10.2210/pdb3j2z/pdb
• 関連するPDBエントリー: 3J2W 3J2X 3J2Y 3J30
• EMDBエントリー: 5579
• 分子名称: m10 light chain, m10 heavy chain (2 entities in total)
• 機能のキーワード: alpha virus, chikungunya vlp, neutralizing antibody m10, immune system
• 由来する生物種: Mus musculus (mouse); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 186980.27

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: 2024-11-27)

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 (16.9 Å)