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

Ozono, Seiya; Zhang, Yanzhao; Ode, Hirotaka; Sano, Kaori; Seng Tan, Toong; Imai, Kazuo; Miyoshi, Kazuyasu; Kishigami, Satoshi; Ueno, Takamasa; Iwatani, Yasumasa; Suzuki, Tadaki; Tokunaga, Kenzo

doi:10.1038/s41467-021-21118-2

Public

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

Published in Nature Communications • Feb 8, 2021

Authors:

Seiya Ozono

Yanzhao Zhang

Hirotaka Ode

Abstract

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...

Subject

Neutralization

Mutation

Viral entry

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