Evidence map›Paper›PMID 30349080›Full record

ArticleNature microbiology2018

A surface endogalactanase in Bacteroides thetaiotaomicron confers keystone status for arabinogalactan degradation.

Alan Cartmell, Jose Muñoz-Muñoz, Jonathon A Briggs, Didier A Ndeh, Elisabeth C Lowe, Arnaud Baslé, Nicolas Terrapon, Katherine Stott, Tiaan Heunis, Joe Gray and 9 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Nature microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
19.3field-weighted citation impact, top 1% 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

59 citing papers in PubMed, 163 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Degradation of mucinbioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
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  11. β-galactanase: an effective tool for the degradation of plant β-ᴅ-galactan.World journal of microbiology & biotechnology · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

19 authors at 5 institutions in 4 countries.

Alan CartmellInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
Jose Muñoz-MuñozInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
Jonathon A BriggsInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.ORCID http://orcid.org/0000-0003-4181-2809
Didier A NdehInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
Elisabeth C LoweInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
Arnaud BasléInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
Nicolas TerraponArchitecture et Fonction des Macromolécules Biologiques, Centre National de la Recherche Scientifique (CNRS), Aix-Marseille University, Marseille, France.ORCID http://orcid.org/0000-0002-3693-6017
Katherine StottDepartment of Biochemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-4014-1188
Tiaan HeunisInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
Joe GrayInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
Li YuDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Paul DupreeDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Pearl Z FernandesSchool of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Sayali ShahSchool of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Spencer J WilliamsSchool of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.
Aurore LabourelInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
Matthias TrostInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.ORCID http://orcid.org/0000-0002-5732-700X
Bernard HenrissatArchitecture et Fonction des Macromolécules Biologiques, Centre National de la Recherche Scientifique (CNRS), Aix-Marseille University, Marseille, France.
Harry J GilbertInstitute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK. harry.gilbert@ncl.ac.uk.ORCID http://orcid.org/0000-0003-3597-2347
Newcastle University · GBThe University of Melbourne · AUUniversity of Cambridge · GBCentre National de la Recherche Scientifique · FRNorthumbria University · GB

Funding

European Research Council 322820Wellcome Trust
6 · The paper itself

Abstract

Glycans are major nutrients for the human gut microbiota (HGM). Arabinogalactan proteins (AGPs) comprise a heterogenous group of plant glycans in which a β1,3-galactan backbone and β1,6-galactan side chains are conserved. Diversity is provided by the variable nature of the sugars that decorate the galactans. The mechanisms by which nutritionally relevant AGPs are degraded in the HGM are poorly understood. Here we explore how the HGM organism Bacteroides thetaiotaomicron metabolizes AGPs. We propose a sequential degradative model in which exo-acting glycoside hydrolase (GH) family 43 β1,3-galactanases release the side chains. These oligosaccharide side chains are depolymerized by the synergistic action of exo-acting enzymes in which catalytic interactions are dependent on whether degradation is initiated by a lyase or GH. We identified two GHs that establish two previously undiscovered GH families. The crystal structures of the exo-β1,3-galactanases identified a key specificity determinant and departure from the canonical catalytic apparatus of GH43 enzymes. Growth studies of Bacteroidetes spp. on complex AGP revealed 3 keystone organisms that facilitated utilization of the glycan by 17 recipient bacteria, which included B. thetaiotaomicron. A surface endo-β1,3-galactanase, when engineered into B. thetaiotaomicron, enabled the bacterium to utilize complex AGPs and act as a keystone organism.

Indexed as

Bacterial ProteinsBacteroides thetaiotaomicronCrystallography, X-RayGastrointestinal MicrobiomeGlycoside HydrolasesHumansMucoproteinsOligosaccharidesPlant ProteinsSubstrate Specificityarabinogalactan proteinsBacterial Proteinsexo-beta-(1--3)-D-galactanaseGlycoside HydrolasesMucoproteinsOligosaccharidesPlant Proteins

Identifiers

PMID30349080
PMCPMC6217937
OpenAlexW2897925715

What OpenQuestion holds

Textmetadata
LicenceTDM
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.