FRETing over SARS-CoV-2: Conformational Dynamics of the Spike Glycoprotein

Vitor Hugo B Serrão; Jeffrey E Lee

doi:10.1016/j.chom.2020.11.008

FRETing over SARS-CoV-2: Conformational Dynamics of the Spike Glycoprotein

Cell Host Microbe. 2020 Dec 9;28(6):778-779. doi: 10.1016/j.chom.2020.11.008.

Authors

Vitor Hugo B Serrão¹, Jeffrey E Lee²

Affiliations

¹ Department of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, 1 King's College Circle, Toronto, ON M5S 1A8, Canada.
² Department of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, 1 King's College Circle, Toronto, ON M5S 1A8, Canada. Electronic address: jeff.lee@utoronto.ca.

Abstract

In this issue of Cell Host & Microbe, Lu et al. utilize single-molecule FRET to reveal the conformation dynamics of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein, showing transitions from a closed ground state to the open receptor-accessible conformation via an on-path intermediate. These insights into spike conformations will facilitate rational immunogen design.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

COVID-19 / genetics
COVID-19 / immunology*
COVID-19 / virology
Fluorescence Resonance Energy Transfer
Humans
Pandemics*
Protein Conformation
SARS-CoV-2 / immunology*
SARS-CoV-2 / pathogenicity
Spike Glycoprotein, Coronavirus / chemistry
Spike Glycoprotein, Coronavirus / immunology
Spike Glycoprotein, Coronavirus / ultrastructure*
Vaccines, Synthetic / chemistry
Vaccines, Synthetic / immunology
Vaccines, Synthetic / ultrastructure

Substances

Spike Glycoprotein, Coronavirus
Vaccines, Synthetic
spike protein, SARS-CoV-2