Evidence map›Paper›PMID 32973204›Full record

ArticleNature communications2020

Structural basis of mammalian mucin processing by the human gut O-glycopeptidase OgpA from Akkermansia muciniphila.

Beatriz Trastoy, Andreas Naegeli, Itxaso Anso, Jonathan Sjögren, Marcelo E Guerin

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed, 2 pooled it
5.3field-weighted citation impact, top 3% 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

61 citing papers in PubMed, 2 syntheses or guidelines pooled it, 104 citations in OpenAlex.

  1. The role ofFrontiers in medicine · 2025
    Pooled it
  2. Pooled it
  3. Discovery of a secretedGut microbes · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Mucinase fromFrontiers in microbiology · 2026
    Article
  8. Review
  9. The Biology ofAnnual review of microbiology · 2025
    Review
  10. Review
  11. Article
  12. Analysis Strategy for Identifying theMolecules (Basel, Switzerland) · 2025
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. The role ofFrontiers in immunology · 2025
    Review

1 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Beatriz Trastoy *Structural Biology Unit, Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801A, 48160, Derio, Spain.ORCID http://orcid.org/0000-0002-2178-732X
Andreas Naegeli *Genovis AB, Box 790, 22007, Lund, Sweden.
Itxaso Anso *Structural Biology Unit, Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801A, 48160, Derio, Spain.ORCID http://orcid.org/0000-0002-4106-8031
Jonathan SjögrenGenovis AB, Box 790, 22007, Lund, Sweden. jonathan.sjogren@genovis.com.ORCID http://orcid.org/0000-0003-1371-9623
Marcelo E GuerinStructural Biology Unit, Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801A, 48160, Derio, Spain. mrcguerin@gmail.com.ORCID http://orcid.org/0000-0001-9524-3184
CIC bioGUNE · ESGenovis (Sweden) · SEIkerbasque · ES

Funding

Rationalizing glycoengineering strategies for immunotherapeutic antibodiesR01AI149297 · NIAID · EMORY UNIVERSITY · PI JEFFREY Victor RAVETCH, ERIC JOHN SUNDBERG · 2020 to 2026
$3.7M
NIAID NIH HHS R01 AI149297
6 · The paper itself

Abstract

Akkermansia muciniphila is a mucin-degrading bacterium commonly found in the human gut that promotes a beneficial effect on health, likely based on the regulation of mucus thickness and gut barrier integrity, but also on the modulation of the immune system. In this work, we focus in OgpA from A. muciniphila, an O-glycopeptidase that exclusively hydrolyzes the peptide bond N-terminal to serine or threonine residues substituted with an O-glycan. We determine the high-resolution X-ray crystal structures of the unliganded form of OgpA, the complex with the glycodrosocin O-glycopeptide substrate and its product, providing a comprehensive set of snapshots of the enzyme along the catalytic cycle. In combination with O-glycopeptide chemistry, enzyme kinetics, and computational methods we unveil the molecular mechanism of O-glycan recognition and specificity for OgpA. The data also contribute to understanding how A. muciniphila processes mucins in the gut, as well as analysis of post-translational O-glycosylation events in proteins.

Indexed as

AkkermansiaAnimalsBinding SitesCrystallography, X-RayGastrointestinal MicrobiomeGlycopeptidesHumansMammalsMolecular Docking SimulationMucin-1MucinsPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidasePolysaccharidesProtein ConformationSequence AlignmentVerrucomicrobiaGlycopeptidesMucin-1MucinsPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidasePolysaccharides

Identifiers

PMID32973204
PMCPMC7518263
OpenAlexW3088398787

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.