5W3E

CryoEM structure of rhinovirus B14 in complex with C5 Fab (33 degrees Celsius, molar ratio 1:3, full particle)

5W3E の概要

• エントリーDOI: 10.2210/pdb5w3e/pdb
• EMDBエントリー: 8754 8761 8762 8763
• 分子名称: C5 antibody variable heavy domain, C5 antibody variable light domain, viral protein 1, ... (7 entities in total)
• 機能のキーワード: virus, antibody, virus-immune system complex, virus/immune system
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 117369.02

構造登録者

Liu, Y.,Dong, Y.,Rossmann, M.G. (登録日: 2017-06-07, 公開日: 2017-07-12, 最終更新日: 2024-10-16)

主引用文献

Dong, Y.,Liu, Y.,Jiang, W.,Smith, T.J.,Xu, Z.,Rossmann, M.G.
Antibody-induced uncoating of human rhinovirus B14.
Proc. Natl. Acad. Sci. U.S.A., 114:8017-8022, 2017

PubMed Abstract: Rhinoviruses (RVs) are the major causes of common colds in humans. They have a nonenveloped, icosahedral capsid surrounding a positive-strand RNA genome. Here we report that the antigen-binding (Fab) fragment of a neutralizing antibody (C5) can trigger genome release from RV-B14 to form emptied particles and neutralize virus infection. Using cryo-electron microscopy, structures of the C5 Fab in complex with the full and emptied particles have been determined at 2.3 Å and 3.0 Å resolution, respectively. Each of the 60 Fab molecules binds primarily to a region on viral protein 3 (VP3). Binding of the C5 Fabs to RV-B14 results in significant conformational changes around holes in the capsid through which the viral RNA might exit. These results are so far the highest resolution view of an antibody-virus complex and elucidate a mechanism whereby antibodies neutralize RVs and related viruses by inducing virus uncoating.

PubMed: 28696310
DOI: 10.1073/pnas.1707369114

実験手法

ELECTRON MICROSCOPY (2.53 Å)