4UOK

Electron Cryo-microscopy of Venezuelan Equine Encephalitis Virus TC-83 in complex with neutralizing antibody Fab 3B4C-4

4UOK の概要

• エントリーDOI: 10.2210/pdb4uok/pdb
• 関連するPDBエントリー: 4UOM
• EMDBエントリー: 2655
• 分子名称: FAB FRAGMENT HEAVY CHAIN, FAB FRAGMENT LIGHT CHAIN (2 entities in total)
• 機能のキーワード: immune system, viral protein, alphavirus, venezuelan, antibody neutralization, fab
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47057.10

構造登録者

Porta, J.,Jose, J.,Roehrig, J.T.,Blair, C.D.,Kuhn, R.J.,Rossmann, M.G. (登録日: 2014-06-04, 公開日: 2014-09-17, 最終更新日: 2019-05-29)

主引用文献

Porta, J.,Jose, J.,Roehrig, J.T.,Blair, C.D.,Kuhn, R.J.,Rossmann, M.G.
Locking and blocking the viral landscape of an alphavirus with neutralizing antibodies.
J.Virol., 88:9616-9623, 2014

PubMed Abstract: Alphaviruses are serious, sometimes lethal human pathogens that belong to the family Togaviridae. The structures of human Venezuelan equine encephalitis virus (VEEV), an alphavirus, in complex with two strongly neutralizing antibody Fab fragments (F5 and 3B4C-4) have been determined using a combination of cryo-electron microscopy and homology modeling. We characterize these monoclonal antibody Fab fragments, which are known to abrogate VEEV infectivity by binding to the E2 (envelope) surface glycoprotein. Both of these antibody Fab fragments cross-link the surface E2 glycoproteins and therefore probably inhibit infectivity by blocking the conformational changes that are required for making the virus fusogenic. The F5 Fab fragment cross-links E2 proteins within one trimeric spike, whereas the 3B4C-4 Fab fragment cross-links E2 proteins from neighboring spikes. Furthermore, F5 probably blocks the receptor-binding site, whereas 3B4C-4 sterically hinders the exposure of the fusion loop at the end of the E2 B-domain.

PubMed: 24920796
DOI: 10.1128/JVI.01286-14

実験手法

ELECTRON MICROSCOPY (18 Å)