Evidence map›Paper›PMID 34590826›Full record

ArticleACS chemical biology2021

Impacting Bacterial Sialidase Activity by Incorporating Bioorthogonal Chemical Reporters onto Mammalian Cell-Surface Sialosides.

Zoeisha S Chinoy, Emilie Montembault, Kelley W Moremen, Anne Royou, Frédéric Friscourt

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

5 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Review
  3. Journal of advanced veterinary and animal research · 2023
    Article
  4. Article
  5. Article
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

5 authors at 2 institutions in 2 countries.

Zoeisha S ChinoyInstitut Européen de Chimie et Biologie, Université de Bordeaux, 2 rue Robert Escarpit, 33607 Pessac, France.
Emilie MontembaultInstitut Européen de Chimie et Biologie, Université de Bordeaux, 2 rue Robert Escarpit, 33607 Pessac, France.
Kelley W MoremenDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, United States.
Anne RoyouInstitut Européen de Chimie et Biologie, Université de Bordeaux, 2 rue Robert Escarpit, 33607 Pessac, France.
Frédéric FriscourtInstitut Européen de Chimie et Biologie, Université de Bordeaux, 2 rue Robert Escarpit, 33607 Pessac, France.ORCID 0000-0002-0749-0861
Centre National de la Recherche Scientifique · FRUniversity of Georgia · US

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
Recombinant Production of Glycosylation Enzymes for Biochem/Structural StudiesP01GM107012 · NIGMS · UNIVERSITY OF GEORGIA · PI PRESTEGARD, JAMES H. · 2013 to 2017
$7.5M
Origin of N-Glycan Site-Specific HeterogeneityR01GM130915 · NIGMS · UNIVERSITY OF GEORGIA · PI KANNAN, NATARAJAN, MOREMEN, KELLEY W. · 2019 to 2022
$3.4M
NIGMS NIH HHS P01 GM107012NIGMS NIH HHS P41 GM103390NIGMS NIH HHS R01 GM130915
6 · The paper itself

Abstract

Bioorthogonal chemical reporters, in synergy with click chemistry, have emerged as a key technology for tagging complex glycans in living cells. This strategy relies on the fact that bioorthogonal chemical reporters are highly reactive species while being biologically noninvasive. Here, we report that chemical reporters and especially sydnones may have, on the contrary, enormous impact on biomolecule processing enzymes. More specifically, we show that editing cell-surface sialic acid-containing glycans (sialosides) with bioorthogonal chemical reporters can significantly affect the activity of bacterial sialidases, enzymes expressed by bacteria during pathogenesis for cleaving sialic acid sugars from mammalian cell-surface glycans. Upon screening various chemical reporters, as well as their position on the sialic acid residue, we identified that pathogenic bacterial sialidases were unable to cleave sialosides displaying a sydnone at the 5-position of sialic acids

Indexed as

Antigens, CDBacteriabeta-D-Galactoside alpha 2-6-Sialyltransferasebeta-Galactoside alpha-2,3-SialyltransferaseBiomarkersCell Line, TumorCell MembraneGene Expression RegulationHumansNeuraminidaseSialic AcidsSialyltransferasesSubstrate SpecificityAntigens, CDbeta-D-Galactoside alpha 2-6-Sialyltransferasebeta-Galactoside alpha-2,3-SialyltransferaseBiomarkersNeuraminidaseSialic AcidsSialyltransferasesST3GAL4 protein, humanST6GAL1 protein, human

Identifiers

PMID34590826
PMCPMC8604778
OpenAlexW3204840683

What OpenQuestion holds

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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.