5XS7

Structure of Coxsackievirus A6 (CVA6) virus A-particle in complex with the neutralizing antibody fragment 1D5

5XS7 の概要

• エントリーDOI: 10.2210/pdb5xs7/pdb
• EMDBエントリー: 6757
• 分子名称: Light chain of Fab 1D5, Heavy chain of Fab 1D5, Genome polyprotein, ... (5 entities in total)
• 機能のキーワード: coxsackievirus a6, immune-complex, icosahedral, virus
• 由来する生物種: Mus musculus; 詳細
• 細胞内の位置: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Virion : A0A0K2BNC7 A0A0K2BNC7 A0A0K2BNC7
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 112975.76

構造登録者

Zheng, Q.B.,He, M.Z.,Xu, L.F.,Yu, H.,Li, S.W.,Cheng, T. (登録日: 2017-06-12, 公開日: 2017-09-27, 最終更新日: 2024-10-30)

主引用文献

Xu, L.,Zheng, Q.,Li, S.,He, M.,Wu, Y.,Li, Y.,Zhu, R.,Yu, H.,Hong, Q.,Jiang, J.,Li, Z.,Li, S.,Zhao, H.,Yang, L.,Hou, W.,Wang, W.,Ye, X.,Zhang, J.,Baker, T.S.,Cheng, T.,Zhou, Z.H.,Yan, X.,Xia, N.
Atomic structures of Coxsackievirus A6 and its complex with a neutralizing antibody
Nat Commun, 8:505-505, 2017

PubMed Abstract: Coxsackievirus A6 (CVA6) has recently emerged as a major cause of hand, foot and mouth disease in children worldwide but no vaccine is available against CVA6 infections. Here, we demonstrate the isolation of two forms of stable CVA6 particles-procapsid and A-particle-with excellent biochemical stability and natural antigenicity to serve as vaccine candidates. Despite the presence (in A-particle) or absence (in procapsid) of capsid-RNA interactions, the two CVA6 particles have essentially identical atomic capsid structures resembling the uncoating intermediates of other enteroviruses. Our near-atomic resolution structure of CVA6 A-particle complexed with a neutralizing antibody maps an immune-dominant neutralizing epitope to the surface loops of VP1. The structure-guided cell-based inhibition studies further demonstrate that these loops could serve as excellent targets for designing anti-CVA6 vaccines.Coxsackievirus A6 (CVA6) causes hand, foot and mouth disease in children. Here the authors present the CVA6 procapsid and A-particle cryo-EM structures and identify an immune-dominant neutralizing epitope, which can be exploited for vaccine development.

PubMed: 28894095
DOI: 10.1038/s41467-017-00477-9

実験手法

ELECTRON MICROSCOPY (3.8 Å)