Evidence map›Paper›PMID 36335195›Full record

ArticleCommunications biology2022

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

Ayana Isobe, Yasuha Arai, Daisuke Kuroda, Nobuaki Okumura, Takao Ono, Shota Ushiba, Shin-Ichi Nakakita, Tomo Daidoji, Yasuo Suzuki, Takaaki Nakaya and 2 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.6field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 38 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 7 institutions in 1 country.

Ayana Isobe *Department of Infectious Diseases, Kyoto Prefectural University of Medicine, Kyoto, 602-8566, Japan.
Yasuha Arai *Department of Infectious Diseases, Kyoto Prefectural University of Medicine, Kyoto, 602-8566, Japan.
Daisuke Kuroda *Research Center for Drug and Vaccine Development, National Institute of Infectious Diseases, Tokyo, 162-8640, Japan.ORCID 0000-0003-2390-4785
Nobuaki OkumuraInstitute for Protein Research, Osaka University, Osaka, 565-0871, Japan.
Takao OnoSANKEN, Osaka University, Osaka, 567-0047, Japan.
Shota UshibaMurata Manufacturing Co., Ltd., Kyoto, 617-8555, Japan.ORCID 0000-0001-7652-081X
Shin-Ichi NakakitaDivision of Functional Glycomics, Kagawa University, Kagawa, 761-0793, Japan.ORCID 0000-0001-6669-8657
Tomo DaidojiDepartment of Infectious Diseases, Kyoto Prefectural University of Medicine, Kyoto, 602-8566, Japan.
Yasuo SuzukiDepartment of Medical Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, 422-8526, Japan.
Takaaki NakayaDepartment of Infectious Diseases, Kyoto Prefectural University of Medicine, Kyoto, 602-8566, Japan.ORCID 0000-0002-7513-6186
Kazuhiko MatsumotoSANKEN, Osaka University, Osaka, 567-0047, Japan.
Yohei WatanabeDepartment of Infectious Diseases, Kyoto Prefectural University of Medicine, Kyoto, 602-8566, Japan. nabe@koto.kpu-m.ac.jp.ORCID 0000-0002-8305-6952
Kyoto Prefectural University of Medicine · JPThe University of Osaka · JPKagawa University · JPMurata (Japan) · JPNational Institute of Infectious Diseases · JPProtein Research Foundation · JPUniversity of Shizuoka · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

COVID-19Spike Glycoprotein, CoronavirusAngiotensin-Converting Enzyme 2GlycosylationHumansPeptidyl-Dipeptidase AProtein BindingSARS-CoV-2Angiotensin-Converting Enzyme 2Peptidyl-Dipeptidase ASpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID36335195
PMCPMC9637154
OpenAlexW4308260688

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.