Evidence map›Paper›PMID 40000644›Full record

ArticleNature communications2025

Dual functional POGases from bacteria encompassing broader O-glycanase and adhesin activities.

Linjiao Zhou, Uriel Ortega-Rodriguez, Matthew J Flores, Yasuyuki Matsumoto, John Q Bettinger, Wells W Wu, Yaqin Zhang, Su-Ryun Kim, Thomas G Biel, Jordan D Pritts and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Discovery of a secretedGut microbes · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
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  7. 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

13 authors.

Linjiao ZhouOffice of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.
Uriel Ortega-RodriguezOffice of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.ORCID http://orcid.org/0000-0002-1700-357X
Matthew J FloresOffice of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.
Yasuyuki MatsumotoOffice of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.ORCID http://orcid.org/0000-0003-2606-2616
John Q BettingerOffice of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.
Wells W WuFacility for Biotechnology Resources, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.
Yaqin ZhangOffice of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.
Su-Ryun KimOffice of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.
Thomas G BielOffice of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.
Jordan D PrittsOffice of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.
Rong-Fong ShenFacility for Biotechnology Resources, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.
V Ashutosh RaoOffice of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA.ORCID http://orcid.org/0000-0001-6817-8049
Tongzhong JuOffice of Pharmaceutical Quality, Center for Drug Evaluation and Research, Food and Drug Administration, Silver Spring, MD, USA. Tongzhong.ju@fda.hhs.gov.ORCID http://orcid.org/0000-0002-4429-1976

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mucin-type O-glycans on glycoproteins are pivotal for biology and impact the quality of biotherapeutics. Furthermore, glycans on host cells serve as ligands for lectins/adhesins on bacteria for bacterium-host interactions in the colonization or attachment/invasion of bacteria. Defining the structure-function relationship of O-glycans is hindered by a lack of enzyme(s) to release sialylated O-glycans from glycoproteins. Here we show identification of endo-α-N-acetylgalactosaminidases (O-glycanases, GH101) with broad substrate specificities, termed Peptide:O-Glycosidase (POGase). In 5 POGase orthologs identified, we characterize one that releases sialylated O-glycans from glycopeptides, glycoproteins and biotherapeutics. Three peptide motifs differentiate the POGase existing in phylum Actinomycetota from known O-glycanases in other bacteria. While the GH101 domain classifies POGases, other domains confer the efficient enzyme activity and binding to major glycans decorating epithelial cells. The dual functional POGases encompassing broader O-glycanase and adhesin activities will facilitate the study of O-glycomics, quality assessment of biotherapeutics, and development of microbiology and medicine.

Indexed as

Adhesins, BacterialBacteriaBacterial ProteinsGlycoside HydrolasesGlycoproteinsHumansPolysaccharidesSubstrate SpecificityAdhesins, BacterialBacterial ProteinsGlycoproteinsGlycoside HydrolasesPolysaccharides

Identifiers

PMID40000644
PMCPMC11861894

What Socratic 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 Socratic graph.