Evidence map›Paper›PMID 42509267›Full record

ArticleNature microbiology2026

Unique adaptations in sulfatases underpin colonic mucin degradation by Akkermansia muciniphila.

Debajit Dey, Naba D Salman, Charles W E Tomlinson, Chunsheng Jin, Grete Raba, Sadie R Schaus, Marcus Nilsson, Zak McIver, Reyme Herman, Adam Simpkin and 14 more

Erratum issuedAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

24 authors.

Debajit Dey *Department of Biology, University of York, York, UK.
Naba D Salman *Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology, University of Gothenburg, Gothenburg, Sweden.
Charles W E TomlinsonDepartment of Biology, University of York, York, UK.ORCID http://orcid.org/0000-0002-1845-6028
Chunsheng JinInstitute of Biomedicine, Department of Medical Biochemistry and Cell Biology, University of Gothenburg, Gothenburg, Sweden.ORCID http://orcid.org/0000-0002-0229-102X
Grete RabaInstitute of Biomedicine, Department of Medical Biochemistry and Cell Biology, University of Gothenburg, Gothenburg, Sweden.ORCID http://orcid.org/0000-0002-7764-3878
Sadie R SchausDepartment of Microbiology and Immunology, University of Michigan, Ann Arbor, MI, USA.
Marcus NilssonInstitute of Biomedicine, Department of Medical Biochemistry and Cell Biology, University of Gothenburg, Gothenburg, Sweden.
Zak McIverDepartment of Biology, University of York, York, UK.
Reyme HermanDepartment of Biology, University of York, York, UK.ORCID http://orcid.org/0000-0002-6620-3981
Adam SimpkinDepartment of Biochemistry, Cell and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.
Matthew DavyYork Structural Biology Laboratory (YSBL), Department of Chemistry, University of York, York, UK.
Daniel J RigdenDepartment of Biochemistry, Cell and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.
Mirjam CzjzekIntegrative Biology of Marine Models, UMR 8227, Station Biologique de Roscoff, CNRS, Sorbonne Université, Univ Paris 06, Roscoff, France.ORCID http://orcid.org/0000-0002-7483-2841
Dominic P ByrneDepartment of Biochemistry, Cell and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.
Mihai OlteanDepartment of Transplantation Surgery, Institute for Clinical Sciences, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Alexander CaseDepartment of Biology, University of York, York, UK.ORCID http://orcid.org/0009-0009-7708-4234
Christoph G BaumannDepartment of Biology, University of York, York, UK.ORCID http://orcid.org/0000-0002-8818-972X
Gareth S A WrightSchool of Life Sciences, University of Essex, Colchester, UK.ORCID http://orcid.org/0000-0002-3756-9634
Sjoerd van der PostInstitute of Biomedicine, Department of Medical Biochemistry and Cell Biology, University of Gothenburg, Gothenburg, Sweden.ORCID http://orcid.org/0000-0002-7965-5311
Edwin A YatesDepartment of Biochemistry, Cell and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.
Eric C MartensDepartment of Microbiology and Immunology, University of Michigan, Ann Arbor, MI, USA.ORCID http://orcid.org/0000-0001-6681-2990
Lauren DaveyDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada.ORCID http://orcid.org/0000-0002-9541-485X
Ana S LuisInstitute of Biomedicine, Department of Medical Biochemistry and Cell Biology, University of Gothenburg, Gothenburg, Sweden. ana.luis@medkem.gu.se.ORCID http://orcid.org/0000-0002-5086-7353
Alan CartmellDepartment of Biology, University of York, York, UK. alan.cartmell@york.ac.uk.ORCID http://orcid.org/0000-0002-5512-249X

Funding

Unraveling the enzymatic pathway of gut bacterial mucus degradation to treat inflammationR01DK125445 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KOROPATKIN, NICOLE M, MARTENS, ERIC C · 2020 to 2023
$2.2M
NIDDK NIH HHS R01 DK125445Wellcome TrustWellcome Trust (Wellcome) 225897/Z/22/Z
6 · The paper itself

Abstract

Excessive foraging of colonic mucin glycans by gut bacteria is associated with diseases such as inflammatory bowel disease. Although Akkermansia muciniphila is an important mucin degrader, the role of carbohydrate sulfatases that facilitate digestion of these heavily sulfated glycans remains unclear. Combining in vitro digestion assays, proteomics and structural biology, we show that A. muciniphila sulfatases, such as Amuc1755 and Amuc0953, have rare adaptations targeted towards known sulfated mucin structures. They show larger degrees of modularity, including a previously unknown mucin-binding domain. When grown on colonic mucin substrates, glycoproteins of reduced size were important for the growth of A. muciniphila. Further mutational analysis and localization studies revealed that desulfation of N-acetyl-D-glucosamine was periplasmic, while desulfation of D-galactose occurred extracellularly and in the periplasm. These data improve our understanding of contexts for the positive health correlations of A. muciniphila while metabolizing colonic mucin as its sole carbon source.

Indexed as

ColonMucinsSulfatasesAcetylglucosamineAkkermansiaGalactosePeriplasmAcetylglucosamineGalactoseMucinsSulfatases

Identifiers

PMID42509267
PMCPMC13524802

What OpenQuestion holds

Textmetadata
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.