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Characterization of the SARS-CoV-2 Spike in an Early Prefusion Conformation

By Tingting Li, Qingbing Zheng, Hai Yu, Dinghui Wu, Wenhui Xue, Yuyun Zhang, Xiaofen Huang, Lizhi Zhou, Zhigang Zhang, Zhenghui Zha, Tingting Chen, Zhiping Wang, Jie Chen, Hui Sun, Tingting Deng, Yingbin Wang, Yixin Chen, Qinjian Zhao, Jun Zhang, Ying Gu, Shaowei Li, Ningshao Xia

Posted 17 Mar 2020
bioRxiv DOI: 10.1101/2020.03.16.994152

Pandemic coronavirus disease 2019 (COVID-19) is caused by the emerging severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), for which there are no efficacious vaccines or therapeutics that are urgently needed. We expressed three versions of spike (S) proteins—receptor binding domain (RBD), S1 subunit and S ectodomain—in insect cells. RBD appears monomer in solutions, whereas S1 and S associate into homotrimer with substantial glycosylation. The three proteins confer excellent antigenicity with six convalescent COVID-19 patient sera. Cryo-electron microscopy (cryo-EM) analyses indicate that the SARS-CoV-2 S trimer dominate in a unique conformation distinguished from the classic prefusion conformation of coronaviruses by the upper S1 region at lower position ~15 Å proximal to viral membrane. Such conformation is proposed as an early prefusion state for the SARS-CoV-2 spike that may broaden the knowledge of coronavirus and facilitate vaccine development.

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