https://scholars.lib.ntu.edu.tw/handle/123456789/633480
標題: | In situ structure and dynamics of an alphacoronavirus spike protein by cryo-ET and cryo-EM | 作者: | Huang, Cheng Yu Draczkowski, Piotr Wang, Yong Sheng Chang, Chia Yu Chien, Yu Chun Cheng, Yun Han Wu, Yi Min Wang, Chun Hsiung Chang, Yuan Chih YEN-CHEN CHANG Yang, Tzu Jing Tsai, Yu Xi Khoo, Kay Hooi HUI-WEN CHANG Hsu, Shang Te Danny |
公開日期: | 1-十二月-2022 | 卷: | 13 | 期: | 1 | 來源出版物: | Nature Communications | 摘要: | 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. |
URI: | https://www.scopus.com/record/display.uri?eid=2-s2.0-85136503747&origin=resultslist&sort=plf-f https://scholars.lib.ntu.edu.tw/handle/123456789/633480 |
ISSN: | 2041-1723 | DOI: | 10.1038/s41467-022-32588-3 |
顯示於: | 分子暨比較病理生物學研究所 |
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