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ACE2 N-glycosylation modulates interactions with SARS-CoV-2 spike protein in a site-specific manner
Communications Biology ( IF 5.2 ) Pub Date : 2022-11-05 , DOI: 10.1038/s42003-022-04170-6
Ayana Isobe 1 , Yasuha Arai 1 , Daisuke Kuroda 2 , Nobuaki Okumura 3 , Takao Ono 4 , Shota Ushiba 5 , Shin-Ichi Nakakita 6 , Tomo Daidoji 1 , Yasuo Suzuki 7 , Takaaki Nakaya 1 , Kazuhiko Matsumoto 4 , Yohei Watanabe 1
Affiliation  

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.



中文翻译:

ACE2 N-糖基化以位点特异性方式调节与 SARS-CoV-2 刺突蛋白的相互作用

SARS-CoV-2 不断进化并积累了尖峰突变,每种变体与细胞 ACE2 受体的结合不同。目前尚不清楚这种突变尖峰与 ACE2 聚糖之间的相互作用在不同的变体谱系中是否保守。在这里,我们专注于在几何上接近尖峰结合位点的三个 ACE2 糖基化位点(53、90 和 322),并研究了它们的糖基化模式对尖峰亲和力的影响。这些糖基化缺失导致与尖峰相互作用的明显位点特异性变化并协同作用。值得注意的是,在 SARS-CoV-2 亲本病毒与关注的变体 (VOC) Delta 和 Omicron 之间,特定的相互作用谱是保守的。

更新日期:2022-11-05
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