Cryo-EM analysis of the HCoV-229E spike glycoprotein reveals dynamic prefusion conformational changes

doi:10.1038/s41467-020-20401-y

	Cryo-EM analysis of the HCoV-229E spike glycoprotein reveals dynamic prefusion conformational changes
	Song, Xiyong 1,2,3; Shi, Yuejun 1,4; Ding, Wei 5; Niu, Tongxin 6; Sun, Limeng 1,4; Tan, Yubei 1,4; Chen, Yong 2,3; Shi, Jiale 1,4; Xiong, Qiqi 1,4; Huang, Xiaojun 6; Xiao, Shaobo 1,4; Zhu, Yanping 2; Cheng, Chongyun 2; Fu, Zhen F.1,4,7; Liu, Zhi-Jie8,9 ; Peng, Guiqing 1,4
	2021-01-08
发表期刊	NATURE COMMUNICATIONS (IF:14.7[JCR-2023],16.1[5-Year])
ISSN	2041-1723
卷号	12 期号:1
DOI	10.1038/s41467-020-20401-y
摘要	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. The spike protein of coronaviruses (S-protein) is an envelope-anchored trimeric type I transmembrane glycoprotein that mediates receptor binding and the fusion of the viral and host cell membranes. Here the authors report the conformational states of HCoV-229E S trimer and observe the conformational changes in S1 subunit from closed state to activated state for receptor binding.
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收录类别	SCIE
语种	英语
WOS研究方向	Science & Technology - Other Topics
WOS类目	Multidisciplinary Sciences
WOS记录号	WOS:000626604800010
出版者	NATURE RESEARCH
原始文献类型	Article
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/126185
专题	iHuman研究所_PI研究组_刘志杰组 iHuman研究所
通讯作者	Liu, Zhi-Jie; Peng, Guiqing
作者单位	1.Huazhong Agr Univ, Coll Vet Med, State Key Lab Agr Microbiol, Wuhan, Peoples R China; 2.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing, Peoples R China; 3.Univ Chinese Acad Sci, Beijing, Peoples R China; 4.Huazhong Agr Univ, Cooperat Innovat Ctr Sustainable Pig Prod, Key Lab Prevent Vet Med Hubei Prov, Wuhan, Peoples R China; 5.Chinese Acad Sci, Inst Phys, CAS Key Lab Soft Matter Phys, POB 603, Beijing, Peoples R China; 6.Chinese Acad Sci, Ctr Biol Imaging, Inst Biophys, Beijing, Peoples R China; 7.Univ Georgia, Dept Pathol, Coll Vet Med, Athens, GA USA; 8.Kunming Med Univ, Inst Mol & Clin Med, Kunming, Yunnan, Peoples R China; 9.ShanghaiTech Univ, iHuman Inst, Shanghai, Peoples R China
通讯作者单位	iHuman研究所
推荐引用方式 GB/T 7714	Song, Xiyong,Shi, Yuejun,Ding, Wei,et al. Cryo-EM analysis of the HCoV-229E spike glycoprotein reveals dynamic prefusion conformational changes[J]. NATURE COMMUNICATIONS,2021,12(1).
APA	Song, Xiyong.,Shi, Yuejun.,Ding, Wei.,Niu, Tongxin.,Sun, Limeng.,...&Peng, Guiqing.(2021).Cryo-EM analysis of the HCoV-229E spike glycoprotein reveals dynamic prefusion conformational changes.NATURE COMMUNICATIONS,12(1).
MLA	Song, Xiyong,et al."Cryo-EM analysis of the HCoV-229E spike glycoprotein reveals dynamic prefusion conformational changes".NATURE COMMUNICATIONS 12.1(2021).