ACE2 N-glycosylation modulates interactions with SARS-CoV-2 spike protein in a site-specific manner

• DOI: 10.1038/s42003-022-04170-6
• Publication Date: 2022-11-05T11:03:00Z
• Authors: Ayana Isobe; Yasuha Arai; Daisuke Kuroda; Nobuaki Okumura; Takao Ono; Shota Ushiba; Shin-ichi Nakakita; Tomo Daidoji; Yasuo Suzuki; Takaaki Nakaya; Kazuhiko Matsumoto; Yohei Watanabe
• Keywords: spike protein; 2019-20 coronavirus outbreak

Abstract SARS-CoV-2 has evolved continuously and accumulated spike mutations with each variant having a different binding for the cellular ACE2 receptor. It is not known whether interactions between such mutated spikes glycans are conserved among lineages. Here, we focused on three glycosylation sites (53, 90 322) that geometrically close to investigated effect of their pattern affinity. These deletions caused distinct site-specific changes in acted cooperatively. Of note, particular interaction profiles were parental virus variants concern (VOCs) Delta Omicron. Our study provides insights better understanding importance ACE2/SARS-CoV-2 guidance further optimization soluble therapeutic use.