7W73

Cryo-EM map of PEDV S protein with one protomer in the D0-up conformation while the other two in the D0-down conformation

7W73 の概要

• エントリーDOI: 10.2210/pdb7w73/pdb
• EMDBエントリー: 32338
• 分子名称: Spike glycoprotein, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: pedv, spike, glycoprotein, viral protein
• 由来する生物種: Porcine epidemic diarrhea virus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 496543.99

構造登録者

Hsu, S.T.D.,Draczkowski, P.,Wang, Y.S. (登録日: 2021-12-03, 公開日: 2022-08-03, 最終更新日: 2022-12-21)

主引用文献

Huang, C.Y.,Draczkowski, P.,Wang, Y.S.,Chang, C.Y.,Chien, Y.C.,Cheng, Y.H.,Wu, Y.M.,Wang, C.H.,Chang, Y.C.,Chang, Y.C.,Yang, T.J.,Tsai, Y.X.,Khoo, K.H.,Chang, H.W.,Hsu, S.D.
In situ structure and dynamics of an alphacoronavirus spike protein by cryo-ET and cryo-EM.
Nat Commun, 13:4877-4877, 2022

PubMed Abstract: Porcine epidemic diarrhea (PED) is a highly contagious swine disease caused by porcine epidemic diarrhea virus (PEDV). PED causes enteric disorders with an exceptionally high fatality in neonates, bringing substantial economic losses in the pork industry. The trimeric spike (S) glycoprotein of PEDV is responsible for virus-host recognition, membrane fusion, and is the main target for vaccine development and antigenic analysis. The atomic structures of the recombinant PEDV S proteins of two different strains have been reported, but they reveal distinct N-terminal domain 0 (D0) architectures that may correspond to different functional states. The existence of the D0 is a unique feature of alphacoronavirus. Here we combined cryo-electron tomography (cryo-ET) and cryo-electron microscopy (cryo-EM) to demonstrate in situ the asynchronous S protein D0 motions on intact viral particles of a highly virulent PEDV Pintung 52 strain. We further determined the cryo-EM structure of the recombinant S protein derived from a porcine cell line, which revealed additional domain motions likely associated with receptor binding. By integrating mass spectrometry and cryo-EM, we delineated the complex compositions and spatial distribution of the PEDV S protein N-glycans, and demonstrated the functional role of a key N-glycan in modulating the D0 conformation.

PubMed: 35986008
DOI: 10.1038/s41467-022-32588-3

実験手法

ELECTRON MICROSCOPY (6.4 Å)