Evidence map›Paper›PMID 41524730›Full record

ArticleGlycobiology2026

Efficient mucin O-glycan degradation by specific mucin degrading intestinal bacteria: towards understanding enzyme-glycan interactions.

Carol de Ram, Maryse D Berkhout, Marta Kozioł, Laura Blasco Matias, Cynthia Klostermann, Carolina O Pandeirada, Sjef Boeren, Athanasia Ioannou, Jean-Paul Vincken, Clara Belzer and 1 more

Abstract read
In one paragraph

Article in Glycobiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

11 authors.

Carol de RamLaboratory of Food Chemistry, Wageningen University & Research, Bornse Weilanden 9, 6708 WG Wageningen, the Netherlands.
Maryse D BerkhoutLaboratory of Microbiology, Wageningen University & Research, Stippeneng 4, 6708 WE Wageningen, the Netherlands.ORCID 0000-0003-3765-8853
Marta KoziołLaboratory of Food Chemistry, Wageningen University & Research, Bornse Weilanden 9, 6708 WG Wageningen, the Netherlands.
Laura Blasco MatiasLaboratory of Food Chemistry, Wageningen University & Research, Bornse Weilanden 9, 6708 WG Wageningen, the Netherlands.
Cynthia KlostermannLaboratory of Food Chemistry, Wageningen University & Research, Bornse Weilanden 9, 6708 WG Wageningen, the Netherlands.
Carolina O PandeiradaLaboratory of Food Chemistry, Wageningen University & Research, Bornse Weilanden 9, 6708 WG Wageningen, the Netherlands.
Sjef BoerenLaboratory of Biochemistry, Wageningen University & Research, Stippeneng 4, 6708 WE Wageningen, the Netherlands.ORCID 0000-0002-0847-8821
Athanasia IoannouLaboratory of Microbiology, Wageningen University & Research, Stippeneng 4, 6708 WE Wageningen, the Netherlands.
Jean-Paul VinckenLaboratory of Food Chemistry, Wageningen University & Research, Bornse Weilanden 9, 6708 WG Wageningen, the Netherlands.
Clara BelzerLaboratory of Microbiology, Wageningen University & Research, Stippeneng 4, 6708 WE Wageningen, the Netherlands.
Henk ScholsLaboratory of Food Chemistry, Wageningen University & Research, Bornse Weilanden 9, 6708 WG Wageningen, the Netherlands.ORCID 0000-0002-5712-1554

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intestinal mucin glycan-degrading bacteria are important for mucus turnover, stimulating mucus production, and producing beneficial metabolites. The mucin-degrading bacteria require various enzymes to break down mucin O-glycans. In this study, mucin glycan-degrading bacteria Akkermansia muciniphila, Ruminococcus torques, and Bacteroides thetaiotaomicron, were grown on porcine gastric mucin in monocultures, co-cultures, and a synthetic bacterial community. Enzyme extracts from these cultures were incubated with a selection of glycans, varying in sugar and linkage composition, to investigate enzyme specificities. Proteomics identified β-galactosidases, α-N-acetylgalactosaminidases, β-N-acetylglucosaminidases, α-fucosidases, α-sialidases, sulphatases, carbohydrate esterases, and polysaccharide lyases involved in O-glycan degradation. Enzymes produced by A. muciniphila and R. torques efficiently cleaved β-linked galactose and N-acetylgalactosamine. B. thetaiotaomicron enzymes minimally cleaved mucin glycans although multiple β-galactosidases and β-N-acetylglucosaminidases were produced. A. muciniphila favoured removal of fucose linked to non-terminal sugars whereas R. torques and B. thetaiotaomicron favoured removal of fucose linked to terminal sugars. A. muciniphila enzymes favoured cleavage of fucose α1-2 linked over α1-3 linked and cleavage of N-acetylglucosamine β1-3 linked over β1-4 linked. Both A. muciniphila and B. thetaiotaomicron favoured cleavage of galactose β1-4 linked over β1-3 linked and sialic acid α2-3 linked over α2-6 linked. Removal of sulphate from mucin structures was only observed by B. thetaiotaomicron. Bacterial co-cultures and the synthetic community produced all enzymes identified in the monocultures resulting in efficient mucin O-glycan degradation. Combining proteomics and glycan linkage cleavage by bacterial enzymes, showed differences in glycan degradation by the bacteria. This highlighted the importance of intestinal bacterial composition in mucin glycan degradation.

Indexed as

IntestinesMucinsPolysaccharidesAkkermansiaAnimalsBacteroides thetaiotaomicronSwineMucinsPolysaccharidesA. muciniphilaB. thetaiotaomicronenzymatic cleavageglycan degradationR. torques

Identifiers

PMID41524730
PMCPMC12834350

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.