イマイ　カズオ   IMAI Kazuo   今井　一男    所属   埼玉医科大学  医学部 臨床検査医学（中央検査部）    職種   専任講師
論文種別	学術雑誌(原著)
言語種別	英語
査読の有無	査読なし
表題	SARS-CoV-2 D614G spike mutation increases entry efficiency with enhanced ACE2-binding affinity.
掲載誌名	正式名：Nature communications
巻・号・頁	12(1),848-848頁
著者・共著者	Seiya Ozono,Yanzhao Zhang,Hirotaka Ode,Kaori Sano,Toong Seng Tan,Kazuo Imai,Kazuyasu Miyoshi,Satoshi Kishigami,Takamasa Ueno,Yasumasa Iwatani,Tadaki Suzuki,Kenzo Tokunaga
発行年月	2021/02
概要	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 unknown. Here, we show that naturally occurring S mutations can reduce or enhance cell entry via ACE2 and TMPRSS2. A SARS-CoV-2 S-pseudotyped lentivirus exhibits substantially lower entry than that of SARS-CoV S. Among S variants, the D614G mutant shows the highest cell entry, as supported by structural and binding analyses. Nevertheless, the D614G mutation does not affect neutralization by antisera against prototypic viruses. Taken together, we conclude that the D614G mutation increases cell entry by acquiring higher affinity to ACE2 while maintaining neutralization susceptibility. Based on these findings, further worldwide surveillance is required to understand SARS-CoV-2 transmissibility among humans.
DOI	10.1038/s41467-021-21118-2
PMID	33558493