SARS-CoV-2 D614G spike mutation increases entry efficiency with enhanced ACE2-binding affinity

• Published in: Nature communications Vol. 12; no. 1; pp. 848 - 9
• Main Authors: Ozono, Seiya, Zhang, Yanzhao, Ode, Hirotaka, Sano, Kaori, Tan, Toong Seng, Imai, Kazuo, Miyoshi, Kazuyasu, Kishigami, Satoshi, Ueno, Takamasa, Iwatani, Yasumasa, Suzuki, Tadaki, Tokunaga, Kenzo
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 08.02.2021; Nature Publishing Group; Nature Portfolio
• Subjects: 101/1; 119/118; 13/106; 13/109; 13/44; 42/70; 631/326/596/2557; 631/326/596/4130; 82/103; 82/29; 82/80; ACE2; Affinity; Angiotensin-converting enzyme 2; Angiotensin-Converting Enzyme 2 - metabolism; Antisera; Binding; Binding, Competitive; COVID-19; COVID-19 - epidemiology; COVID-19 - prevention & control; COVID-19 - virology; Humanities and Social Sciences; Humans; Models, Molecular; multidisciplinary; Mutants; Mutation; Neutralization; Pandemics; Protein Binding; Protein Domains; Proteins; Receptors, Virus - metabolism; SARS-CoV-2 - genetics; SARS-CoV-2 - physiology; Science; Science (multidisciplinary); Serine Endopeptidases - metabolism; Severe acute respiratory syndrome coronavirus 2; Spike Glycoprotein, Coronavirus - chemistry; Spike Glycoprotein, Coronavirus - genetics; Spike Glycoprotein, Coronavirus - metabolism; Spike protein; Viral diseases; Virus Internalization

The causative agent of the COVID-19 pandemic, SARS-CoV-2, is steadily mutating during continuous transmission among humans. Such mutations can occur in the spike (S) protein that binds to the ACE2 receptor and is cleaved by TMPRSS2. However, whether S mutations affect SARS-CoV-2 cell entry remains u...