ArticleNature communications2025
Microbial binding module employs sophisticated clustered saccharide patches to selectively adhere to mucins.
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 9 papers.
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Who cites it
9 citing papers in PubMed.
- Discovery of a secretedGut microbes · 2026Article
- Age-related remodeling of the intestinal mucus barrier in pigs: implications for post-weaning diarrhea.Veterinary and animal science · 2026Article
- MUC17 and the intestinal glycocalyx: structure, regulation, and barrier function in health and disease.Bioscience reports · 2026Review
- From Glycocode to Precision Oncology: Therapeutic Strategies Targeting Aberrant O-GalNAc Glycosylation in Cancer.Chemical reviews · 2026Review
- Distinct O-Linked Glycosylation Systems in Signaling and Immune Regulation.International journal of molecular sciences · 2026Review
- Outcome associations of CSF total tau in suspected non-Alzheimer pathophysiology.Journal of neurology · 2026Article
- Glycoengineering strategies for constructing defined Mucin O-glycans.Frontiers in molecular biosciences · 2026Review
- Article
- Spatial N-glycan rearrangement on αNature communications · 2025Article
Corrections and comments
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Authors and funding
23 authors.
Funding
Abstract
The mucus lining wet body surfaces forms the interphase and barrier for the microbiota and resident microbiomes. Large mucin proteins densely decorated with O-glycans make up the mucus lining to entrap, feed and shape the microbiota, and repress biofilm formation and virulence. How mucins exert these effects is poorly understood and critical is how the microbiota recognize, sense, and break down mucins. Here, we provide structural molecular evidence that a small mucin-binding module designated X409 recognizes clustered saccharide patches comprised of rows of inner monosaccharides in adjacent O-glycans. These patches are unique to mucins and binding to these provides an elegant mechanism to retain adherence to mucins despite trimming of O-glycans during microbial scavenging of monosaccharides from mucins. Realization of clustered saccharide patch-binding motifs provides a hitherto overlooked scenario of contextual glycan epitopes and impetus for discovery of new classes of glycan-binding proteins.
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Registered trials
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