Open AccessNanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein
Author(s) -
Linhua Tai,
Guoliang Zhu,
Mu Yang,
Lei Cao,
Xing Xin,
Guoliang Yin,
Chun Chan,
ChengFeng Qin,
Zihe Rao,
Xiangxi Wang,
Fei Sun,
Yun Zhu
Publication year - 2021
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2112703118
Subject(s) - biophysics , lipid bilayer fusion , biology , coronavirus , transmembrane domain , microbiology and biotechnology , transmembrane protein , protein structure , virology , covid-19 , membrane , virus , biochemistry , receptor , medicine , disease , pathology , infectious disease (medical specialty)
Significance Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a severe threat to public health and the global economy. Its spike protein is responsible for the membrane fusion and is thus a major target for vaccine and drug development. Our study presents the in situ structure of the spike protein in the postfusion state with higher resolution, giving further insights into the design of a viral entry inhibitor. Our observation of the oligomerization states of spikes on the viral membrane implies a possible mechanism of membrane fusion for viral infection.