ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV

被引：22
|
作者：
Acharya, Atanu [1 ]
Lynch, Diane L. [1 ]
Pavlova, Anna [1 ]
Pang, Yui Tik [1 ]
Gumbart, James C. [1 ]
机构：
[1] Georgia Inst Technol, Sch Phys, Atlanta, GA 30332 USA
来源：
CHEMICAL COMMUNICATIONS | 2021年 / 57卷 / 48期
基金：
美国国家科学基金会;
关键词：
RECEPTOR-BINDING; SPIKE;
D O I：
10.1039/d1cc02305e
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
We report a distinct difference in the interactions of the glycans of the host-cell receptor, ACE2, with SARS-CoV-2 and SARS-CoV S-protein receptor-binding domains (RBDs). Our analysis demonstrates that the ACE2 glycan at N322 enhances interactions with the SARS-CoV-2 RBD while the ACE2 glycan at N90 may offer protection against infections of both coronaviruses depending on its composition. The interactions of the ACE2 glycan at N322 with SARS-CoV RBD are blocked by the presence of the RBD glycan at N357 of the SARS-CoV RBD. The absence of this glycosylation site on SARS-CoV-2 RBD may enhance its binding with ACE2.
引用
收藏
页码：5949 / 5952
页数：4
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