| Literature DB >> 33420048 |
Xiyong Song1,2,3, Yuejun Shi1,4, Wei Ding5, Tongxin Niu6, Limeng Sun1,4, Yubei Tan1,4, Yong Chen2,3, Jiale Shi1,4, Qiqi Xiong1,4, Xiaojun Huang6, Shaobo Xiao1,4, Yanping Zhu2, Chongyun Cheng2, Zhen F Fu1,4,7, Zhi-Jie Liu8,9, Guiqing Peng10,11.
Abstract
Coronaviruses spike (S) glycoproteins mediate viral entry into host cells by binding to host receptors. However, how the S1 subunit undergoes conformational changes for receptor recognition has not been elucidated in Alphacoronavirus. Here, we report the cryo-EM structures of the HCoV-229E S trimer in prefusion state with two conformations. The activated conformation may pose the potential exposure of the S1-RBDs by decreasing of the interaction area between the S1-RBDs and the surrounding S1-NTDs and S1-RBDs compared to the closed conformation. Furthermore, structural comparison of our structures with the previously reported HCoV-229E S structure showed that the S trimers trended to open the S2 subunit from the closed conformation to open conformation, which could promote the transition from pre- to postfusion. Our results provide insights into the mechanisms involved in S glycoprotein-mediated Alphacoronavirus entry and have implications for vaccine and therapeutic antibody design.Entities:
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Year: 2021 PMID： 33420048 PMCID： PMC7794242 DOI： 10.1038/s41467-020-20401-y
Source DB: PubMed Journal: Nat Commun ISSN： 2041-1723 Impact factor: 14.919