4RQP

Crystal structure of the natually occurring empty particle of a clinical C4 strain EV71

4RQP の概要

• エントリーDOI: 10.2210/pdb4rqp/pdb
• 関連するPDBエントリー: 4n43 4n53 4RR3 4RS5
• 分子名称: Capsid protein VP1, Capsid protein VP3, Capsid protein VP0 (3 entities in total)
• 機能のキーワード: beta barrel, icosahedral virus, natually occurring empty particle with unknown function, replicate in host cell cytoplasm, virus
• 由来する生物種: Enterovirus A71; 詳細
• 細胞内の位置: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : F6KTB0 F6KTB0 F6KTB0
• タンパク質・核酸の鎖数: 15
• 化学式量合計: 471745.70

構造登録者

Chen, R.,Lyu, K. (登録日: 2014-11-04, 公開日: 2014-12-17, 最終更新日: 2024-02-28)

主引用文献

Lyu, K.,Wang, G.C.,He, Y.L.,Han, J.F.,Ye, Q.,Qin, C.F.,Chen, R.
Crystal structures of enterovirus 71 (EV71) recombinant virus particles provide insights into vaccine design.
J.Biol.Chem., 290:3198-3208, 2015

PubMed Abstract: Hand-foot-and-mouth disease (HFMD) remains a major health concern in the Asia-Pacific regions, and its major causative agents include human enterovirus 71 (EV71) and coxsackievirus A16. A desirable vaccine against HFMD would be multivalent and able to elicit protective responses against multiple HFMD causative agents. Previously, we have demonstrated that a thermostable recombinant EV71 vaccine candidate can be produced by the insertion of a foreign peptide into the BC loop of VP1 without affecting viral replication. Here we present crystal structures of two different naturally occurring empty particles, one from a clinical C4 strain EV71 and the other from its recombinant virus containing an insertion in the VP1 BC loop. Crystal structure analysis demonstrated that the inserted foreign peptide is well exposed on the particle surface without significant structural changes in the capsid. Importantly, such insertions do not seem to affect the virus uncoating process as illustrated by the conformational similarity between an uncoating intermediate of another recombinant virus and that of EV71. Especially, at least 18 residues from the N terminus of VP1 are transiently externalized. Altogether, our study provides insights into vaccine development against HFMD.

PubMed: 25492868
DOI: 10.1074/jbc.M114.624536

実験手法

X-RAY DIFFRACTION (3.151 Å)