RRC ID 73032
著者 Isobe A, Arai Y, Kuroda D, Okumura N, Ono T, Ushiba S, Nakakita SI, Daidoji T, Suzuki Y, Nakaya T, Matsumoto K, Watanabe Y.
タイトル ACE2 N-glycosylation modulates interactions with SARS-CoV-2 spike protein in a site-specific manner.
ジャーナル Commun Biol
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 the interactions between such mutated spikes and ACE2 glycans are conserved among different variant lineages. Here, we focused on three ACE2 glycosylation sites (53, 90 and 322) that are geometrically close to spike binding sites and investigated the effect of their glycosylation pattern on spike affinity. These glycosylation deletions caused distinct site-specific changes in interactions with the spike and acted cooperatively. Of note, the particular interaction profiles were conserved between the SARS-CoV-2 parental virus and the variants of concern (VOCs) Delta and Omicron. Our study provides insights for a better understanding of the importance of ACE2 glycosylation on ACE2/SARS-CoV-2 spike interaction and guidance for further optimization of soluble ACE2 for therapeutic use.
巻・号 5(1)
ページ 1188
公開日 2022-11-5
DOI 10.1038/s42003-022-04170-6
PII 10.1038/s42003-022-04170-6
PMID 36335195
PMC PMC9637154
MeSH Angiotensin-Converting Enzyme 2 / genetics COVID-19* Glycosylation Humans Peptidyl-Dipeptidase A Protein Binding SARS-CoV-2 / genetics Spike Glycoprotein, Coronavirus* / chemistry
IF 4.165
オルトメトリクス指標
オルトメトリクス指標項目
最多言及媒体 X(Twitter)
各媒体での言及数の合計 10
過去6か月間でのオルトメトリクス指標の変動値 3.5
リソース情報
ヒト・動物細胞 293(RCB1637) Vero(RCB0001)