5BNO

Crystal structure of human enterovirus D68 in complex with 6'SLN

5BNO の概要

• エントリーDOI: 10.2210/pdb5bno/pdb
• 関連するPDBエントリー: 5BNN 5BNP
• 関連するBIRD辞書のPRD_ID: PRD_900046
• 分子名称: Capsid protein VP1, Capsid protein VP2, Capsid protein VP3, ... (6 entities in total)
• 機能のキーワード: enterovirus, capsid, beta jelly roll, virus, receptor
• 由来する生物種: Enterovirus D68; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 95704.95

構造登録者

Liu, Y.,Sheng, J.,Meng, G.,Xiao, C.,Rossmann, M.G. (登録日: 2015-05-26, 公開日: 2015-11-18, 最終更新日: 2023-09-27)

主引用文献

Liu, Y.,Sheng, J.,Baggen, J.,Meng, G.,Xiao, C.,Thibaut, H.J.,van Kuppeveld, F.J.,Rossmann, M.G.
Sialic acid-dependent cell entry of human enterovirus D68.
Nat Commun, 6:8865-8865, 2015

PubMed Abstract: Human enterovirus D68 (EV-D68) is a causative agent of childhood respiratory diseases and has now emerged as a global public health threat. Nevertheless, knowledge of the tissue tropism and pathogenesis of EV-D68 has been hindered by a lack of studies on the receptor-mediated EV-D68 entry into host cells. Here we demonstrate that cell surface sialic acid is essential for EV-D68 to bind to and infect susceptible cells. Crystal structures of EV-D68 in complex with sialylated glycan receptor analogues show that they bind into the 'canyon' on the virus surface. The sialic acid receptor induces a cascade of conformational changes in the virus to eject a fatty-acid-like molecule that regulates the stability of the virus. Thus, virus binding to a sialic acid receptor and to immunoglobulin-like receptors used by most other enteroviruses share a conserved mechanism for priming viral uncoating and facilitating cell entry.

PubMed: 26563423
DOI: 10.1038/ncomms9865

実験手法

X-RAY DIFFRACTION (2.15 Å)