Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation

• Published in: Nature structural & molecular biology Vol. 27; no. 10; pp. 942 - 949
• Main Authors: McCallum, Matthew, Walls, Alexandra C., Bowen, John E., Corti, Davide, Veesler, David
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.10.2020; Nature Publishing Group
• Subjects: 101/28; 631/326/596/4130; 631/535/1258/1259; Antibodies, Monoclonal - metabolism; Antibodies, Neutralizing - metabolism; Betacoronavirus - chemistry; Betacoronavirus - genetics; Betacoronavirus - immunology; Betacoronavirus - metabolism; Biochemistry; Biological Microscopy; Biomedical and Life Sciences; Causes of; Conformation; Coronaviruses; Cryoelectron Microscopy; Disulfides - chemistry; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Epidemics; Genetic aspects; Glycoproteins; Health aspects; Humans; Life Sciences; Membrane Biology; Models, Molecular; Mutation; Properties; Protein Conformation; Protein Domains; Protein Engineering; Protein Multimerization; Protein Stability; Protein Structure; Proteins; SARS-CoV-2; Spike Glycoprotein, Coronavirus - chemistry; Spike Glycoprotein, Coronavirus - genetics; Spike Glycoprotein, Coronavirus - immunology; Spike Glycoprotein, Coronavirus - metabolism; United States; Virulence (Microbiology); United States

SARS-CoV-2 is the causative agent of the COVID-19 pandemic, with 10 million infections and more than 500,000 fatalities by June 2020. To initiate infection, the SARS-CoV-2 spike (S) glycoprotein promotes attachment to the host cell surface and fusion of the viral and host membranes. Prefusion SARS-C...