ArticleNature communications2022
Structural and mechanistic insights into the cleavage of clustered O-glycan patches-containing glycoproteins by mucinases of the human gut.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 46 citations in OpenAlex.
- Discovery of a secretedGut microbes · 2026Article
- The protease code of the bacterial gut microbiota: ecological regulation, barrier disruption, and rewiring host defense and signaling.Gut microbes · 2026Review
- Determination of Gene-Level Fitness Contributions Across the Mucin-Utilization Network of Bacteroides thetaiotaomicron.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Functional conservation of divergent peptidase_M60 O-glycopeptidases in enterococcus.Glycobiology · 2026Article
- Enhanced microbiota-derived mucinases in colorectal cancer patients revealed by gut metagenome probing coupled with functional validation.Applied and environmental microbiology · 2026Article
- Mucin Type Drives Composition and Mucin Glycan Degradation of an In Vitro Synthetic Microbial Community.Environmental microbiology · 2026Article
- Glycerol monolaurate attenuates necrotic enteritis in broilers by improving gut-liver health and remodeling the gut microbiota.Journal of animal science and biotechnology · 2026Article
- Synthesis of Polyhydroxylated Pyrrolidinyl Analogs of Sugar Nucleotides. Experimental and Computational Studies on Their Interactions With GalNAC-T's.Chembiochem : a European journal of chemical biology · 2026Article
- Mucinase fromFrontiers in microbiology · 2026Article
- Probiotic Engraftment of Akkermansia muciniphila in an In Vitro Synthetic Microbial Community.Microbial ecology · 2025Article
- GlycoFASP: A Universal Method to Prepare Complex Mixtures for O-Glycoproteomic Analysis.Analytical chemistry · 2025Article
- Microbial binding module employs sophisticated clustered saccharide patches to selectively adhere to mucins.Nature communications · 2025Article
- The Biology ofAnnual review of microbiology · 2025Review
- Breaking down barriers: is intestinal mucus degradation byInfection and immunity · 2025Review
- Review
- The Role of Whey in Functional Microorganism Growth and Metabolite Generation: A Biotechnological Perspective.Foods (Basel, Switzerland) · 2025Review
- A Bacteroides thetaiotaomicron genetic locus encodes activities consistent with mucin O-glycoprotein processing and N-acetylgalactosamine metabolism.Nature communications · 2025Article
- Unravelling the Glycan Code: Molecular Dynamics and Quantum Chemistry Reveal How O-Glycan Functional Groups Govern OgpA Selectivity in Mucin Degradation by Akkermansia muciniphila.Microbial biotechnology · 2025Article
- Glycan-mediated adhesion mechanisms in antibiotic-resistant bacteria.BBA advances · 2025Article
- Mucin-driven ecological interactions in an in vitro synthetic community of human gut microbes.Glycobiology · 2024Article
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mucinases of human gut bacteria cleave peptide bonds in mucins strictly depending on the presence of neighboring O-glycans. The Akkermansia muciniphila AM0627 mucinase cleaves specifically in between contiguous (bis) O-glycans of defined truncated structures, suggesting that this enzyme may recognize clustered O-glycan patches. Here, we report the structure and molecular mechanism of AM0627 in complex with a glycopeptide containing a bis-T (Galβ1-3GalNAcα1-O-Ser/Thr) O-glycan, revealing that AM0627 recognizes both the sugar moieties and the peptide sequence. AM0627 exhibits preference for bis-T over bis-Tn (GalNAcα1-O-Ser/Thr) O-glycopeptide substrates, with the first GalNAc residue being essential for cleavage. AM0627 follows a mechanism relying on a nucleophilic water molecule and a catalytic base Glu residue. Structural comparison among mucinases identifies a conserved Tyr engaged in sugar-π interactions in both AM0627 and the Bacteroides thetaiotaomicron BT4244 mucinase as responsible for the common activity of these two mucinases with bis-T/Tn substrates. Our work illustrates how mucinases through tremendous flexibility adapt to the diversity in distribution and patterns of O-glycans on mucins.
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