7QB5

Coxsackievirus A24v (CVA24v) in complex with a dimeric C2-C9-linked sialic acid inhibitor

これはPDB形式変換不可エントリーです。

7QB5 の概要

• エントリーDOI: 10.2210/pdb7qb5/pdb
• 分子名称: Capsid protein VP1, Capsid protein VP2, Capsid protein VP3, ... (9 entities in total)
• 機能のキーワード: coxsackievirus a24v, cva24v, sialic acid based inhibitor, virus
• 由来する生物種: Coxsackievirus A24; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 98882.14

構造登録者

Zocher, G.,Stehle, T. (登録日: 2021-11-18, 公開日: 2022-05-18, 最終更新日: 2024-01-31)

主引用文献

Johansson, E.,Caraballo, R.,Zocher, G.,Mistry, N.,Arnberg, N.,Stehle, T.,Elofsson, M.
Exploring divalent conjugates of 5- N -acetyl-neuraminic acid as inhibitors of coxsackievirus A24 variant (CVA24v) transduction.
Rsc Adv, 12:2319-2331, 2022

PubMed Abstract: Coxsackievirus A24 variant (CVA24v) is responsible for several outbreaks and two pandemics of the highly contagious eye infection acute hemorrhagic conjunctivitis (AHC). Currently, neither prevention (vaccines) nor treatments (antivirals) are available for combating this disease. CVA24v attaches to cells by binding Neu5Ac-containing glycans on the surface of cells which facilitates entry. Previously, we have demonstrated that pentavalent Neu5Ac conjugates attenuate CVA24v infection of human corneal epithelial (HCE) cells. In this study, we report on the structure-based design of three classes of divalent Neu5Ac conjugates, with varying spacer lengths, and their effect on CVA24v transduction in HCE cells. In relative terms, the most efficient class of divalent Neu5Ac conjugates are more efficient than the pentavalent Neu5Ac conjugates previously reported.

PubMed: 35425270
DOI: 10.1039/d1ra08968d

実験手法

X-RAY DIFFRACTION (1.728 Å)