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ACE2 N-glycosylation modulates interactions with SARS-CoV-2 spike protein in a site-specific manner.
Isobe, Ayana; Arai, Yasuha; Kuroda, Daisuke; Okumura, Nobuaki; Ono, Takao; Ushiba, Shota; Nakakita, Shin-Ichi; Daidoji, Tomo; Suzuki, Yasuo; Nakaya, Takaaki; Matsumoto, Kazuhiko; Watanabe, Yohei.
  • Isobe A; Department of Infectious Diseases, Kyoto Prefectural University of Medicine, Kyoto, 602-8566, Japan.
  • Arai Y; Department of Infectious Diseases, Kyoto Prefectural University of Medicine, Kyoto, 602-8566, Japan.
  • Kuroda D; Research Center for Drug and Vaccine Development, National Institute of Infectious Diseases, Tokyo, 162-8640, Japan.
  • Okumura N; Institute for Protein Research, Osaka University, Osaka, 565-0871, Japan.
  • Ono T; SANKEN, Osaka University, Osaka, 567-0047, Japan.
  • Ushiba S; Murata Manufacturing Co., Ltd., Kyoto, 617-8555, Japan.
  • Nakakita SI; Division of Functional Glycomics, Kagawa University, Kagawa, 761-0793, Japan.
  • Daidoji T; Department of Infectious Diseases, Kyoto Prefectural University of Medicine, Kyoto, 602-8566, Japan.
  • Suzuki Y; Department of Medical Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, 422-8526, Japan.
  • Nakaya T; Department of Infectious Diseases, Kyoto Prefectural University of Medicine, Kyoto, 602-8566, Japan.
  • Matsumoto K; SANKEN, Osaka University, Osaka, 567-0047, Japan.
  • Watanabe Y; Department of Infectious Diseases, Kyoto Prefectural University of Medicine, Kyoto, 602-8566, Japan. nabe@koto.kpu-m.ac.jp.
Commun Biol ; 5(1): 1188, 2022 Nov 05.
Article in English | MEDLINE | ID: covidwho-2106511
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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / COVID-19 Topics: Variants Limits: Humans Language: English Journal: Commun Biol Year: 2022 Document Type: Article Affiliation country: S42003-022-04170-6

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / COVID-19 Topics: Variants Limits: Humans Language: English Journal: Commun Biol Year: 2022 Document Type: Article Affiliation country: S42003-022-04170-6