TY - JOUR
T1 - Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein
AU - Tai, Linhua
AU - Zhu, Guoliang
AU - Yang, Minnan
AU - Cao, Lei
AU - Xing, Xiaorui
AU - Yin, Guoliang
AU - Chan, Chun
AU - Qin, Chengfeng
AU - Rao, Zihe
AU - Wang, Xiangxi
AU - Sun, Fei
AU - Zhu, Yun
N1 - Publisher Copyright:
© 2021 National Academy of Sciences. All rights reserved.
PY - 2021/11/30
Y1 - 2021/11/30
N2 - The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates membrane fusion to allow entry of the viral genome into host cells. To understand its detailed entry mechanism and develop a specific entry inhibitor, in situ structural information on the SARS-CoV-2 spike protein in different states is urgent. Here, by using cryo-electron tomography, we observed both prefusion and postfusion spikes in β-propiolactone-inactivated SARS-CoV-2 virions and solved the in situ structure of the postfusion spike at nanometer resolution. Compared to previous reports, the six-helix bundle fusion core, the glycosylation sites, and the location of the transmembrane domain were clearly resolved. We observed oligomerization patterns of the spikes on the viral membrane, likely suggesting a mechanism of fusion pore formation.
AB - The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates membrane fusion to allow entry of the viral genome into host cells. To understand its detailed entry mechanism and develop a specific entry inhibitor, in situ structural information on the SARS-CoV-2 spike protein in different states is urgent. Here, by using cryo-electron tomography, we observed both prefusion and postfusion spikes in β-propiolactone-inactivated SARS-CoV-2 virions and solved the in situ structure of the postfusion spike at nanometer resolution. Compared to previous reports, the six-helix bundle fusion core, the glycosylation sites, and the location of the transmembrane domain were clearly resolved. We observed oligomerization patterns of the spikes on the viral membrane, likely suggesting a mechanism of fusion pore formation.
KW - Cryo-electron tomography
KW - Postfusion state
KW - SARS-CoV-2
KW - Spike protein
KW - Subtomogram analysis
UR - http://www.scopus.com/inward/record.url?scp=85120346447&partnerID=8YFLogxK
U2 - 10.1073/pnas.2112703118
DO - 10.1073/pnas.2112703118
M3 - Article
C2 - 34782481
AN - SCOPUS:85120346447
SN - 0027-8424
VL - 118
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 48
M1 - e2112703118
ER -