Evidence map›Paper›PMID 36968546›Full record

ArticleACS central science2023

O-Linked Sialoglycans Modulate the Proteolysis of SARS-CoV-2 Spike and Likely Contribute to the Mutational Trajectory in Variants of Concern.

Edgar Gonzalez-Rodriguez, Mia Zol-Hanlon, Ganka Bineva-Todd, Andrea Marchesi, Mark Skehel, Keira E Mahoney, Chloë Roustan, Annabel Borg, Lucia Di Vagno, Svend Kjær and 12 more

Open access · diamondFull text read
In one paragraph

Article in ACS central science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

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  10. A Bioorthogonal Precision Tool for HumanJournal of the American Chemical Society · 2024
    Article
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  16. Variations inBiomolecules · 2023
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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

22 authors at 6 institutions in 5 countries.

Edgar Gonzalez-RodriguezChemical Glycobiology Laboratory, The Francis Crick Institute, NW1 1AT London, United Kingdom.ORCID https://orcid.org/0000-0003-3458-1942
Mia Zol-HanlonChemical Glycobiology Laboratory, The Francis Crick Institute, NW1 1AT London, United Kingdom.
Ganka Bineva-ToddChemical Glycobiology Laboratory, The Francis Crick Institute, NW1 1AT London, United Kingdom.
Andrea MarchesiChemical Glycobiology Laboratory, The Francis Crick Institute, NW1 1AT London, United Kingdom.
Mark SkehelProteomics Science Technology Platform, The Francis Crick Institute, NW1 1AT London, United Kingdom.
Keira E MahoneyDepartment of Chemistry, Yale University, 275 Prospect Street, 06511 New Haven, Connecticut, United States.ORCID https://orcid.org/0000-0003-4561-9838
Chloë RoustanStructural Biology Science Technology Platform, The Francis Crick Institute, NW1 1AT London, United Kingdom.
Annabel BorgStructural Biology Science Technology Platform, The Francis Crick Institute, NW1 1AT London, United Kingdom.
Lucia Di VagnoChemical Glycobiology Laboratory, The Francis Crick Institute, NW1 1AT London, United Kingdom.
Svend KjærStructural Biology Science Technology Platform, The Francis Crick Institute, NW1 1AT London, United Kingdom.
Antoni G WrobelStructural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT London, United Kingdom.
Donald J BentonStructural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT London, United Kingdom.
Philipp NawrathStructural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT London, United Kingdom.ORCID https://orcid.org/0000-0001-9222-2046
Sabine L FlitschManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, M1 7DN Manchester, United Kingdom.ORCID https://orcid.org/0000-0003-3974-646X
Dhira JoshiChemical Biology Science Technology Platform, The Francis Crick Institute, NW1 1AT London, United Kingdom.
Andrés Manuel González-RamírezInstitute of Biocomputation and Physics of Complex Systems, University of Zaragoza, 50018 Zaragoza, Spain.
Katalin A WilkinsonTuberculosis Laboratory, The Francis Crick Institute, NW1 1AT London, United Kingdom.
Robert J WilkinsonTuberculosis Laboratory, The Francis Crick Institute, NW1 1AT London, United Kingdom.
Emma C WallThe Francis Crick Institute, NW1 1AT London, United Kingdom.
Ramón Hurtado-GuerreroInstitute of Biocomputation and Physics of Complex Systems, University of Zaragoza, 50018 Zaragoza, Spain.ORCID https://orcid.org/0000-0002-3122-9401
Stacy A MalakerDepartment of Chemistry, Yale University, 275 Prospect Street, 06511 New Haven, Connecticut, United States.ORCID https://orcid.org/0000-0003-2382-5067
Benjamin SchumannChemical Glycobiology Laboratory, The Francis Crick Institute, NW1 1AT London, United Kingdom.ORCID https://orcid.org/0000-0001-5504-0147
The Francis Crick Institute · GBUniversity of Cape Town · ZAYale University · USUniversidad de Zaragoza · ESUniversity of Copenhagen · DKUniversity of Manchester · GB

Funding

Toward understanding the role of altered glycosylation in cancerR35GM147039 · NIGMS · YALE UNIVERSITY · PI Stacy Alyse Malaker · 2022 to 2026
$2.0M
NIGMS NIH HHS R35 GM147039Wellcome Trust CC1283Wellcome Trust CC2112Wellcome Trust CC2127
6 · The paper itself

Abstract

The emergence of a polybasic cleavage motif for the protease furin in SARS-CoV-2 spike has been established as a major factor for human viral transmission. The region N-terminal to that motif is extensively mutated in variants of concern (VOCs). Besides furin, spikes from these variants appear to rely on other proteases for maturation, including TMPRSS2. Glycans near the cleavage site have raised questions about proteolytic processing and the consequences of variant-borne mutations. Here, we identify that sialic acid-containing O-linked glycans on Thr678 of SARS-CoV-2 spike influence furin and TMPRSS2 cleavage and posit O-linked glycosylation as a likely driving force for the emergence of VOC mutations. We provide direct evidence that the glycosyltransferase GalNAc-T1 primes glycosylation at Thr678 in the living cell, an event that is suppressed by mutations in the VOCs Alpha, Delta, and Omicron. We found that the sole incorporation of

Identifiers

PMID36968546
PMCPMC10037455
OpenAlexW4321076815

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read27
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.