Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein

Xiaoyi Fan, Duanfang Cao (), Lingfei Kong and Xinzheng Zhang ()
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Xiaoyi Fan: Chinese Academy of Sciences
Duanfang Cao: Chinese Academy of Sciences
Lingfei Kong: Chinese Academy of Sciences
Xinzheng Zhang: Chinese Academy of Sciences

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract Global emergencies caused by the severe acute respiratory syndrome coronavirus (SARS-CoV), Middle-East respiratory syndrome coronavirus (MERS-CoV) and SARS-CoV-2 significantly endanger human health. The spike (S) glycoprotein is the key antigen and its conserved S2 subunit contributes to viral entry by mediating host-viral membrane fusion. However, structural information of the post-fusion S2 from these highly pathogenic human-infecting coronaviruses is still lacking. We used single-particle cryo-electron microscopy to show that the post-fusion SARS-CoV S2 forms a further rotated HR1-HR2 six-helix bundle and a tightly bound linker region upstream of the HR2 motif. The structures of pre- and post-fusion SARS-CoV S glycoprotein dramatically differ, resembling that of the Mouse hepatitis virus (MHV) and other class I viral fusion proteins. This structure suggests potential targets for the development of vaccines and therapies against a wide range of SARS-like coronaviruses.

Date: 2020
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DOI: 10.1038/s41467-020-17371-6

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