ArticleNature chemical biology2023
Mechanism of high-mannose N-glycan breakdown and metabolism by Bifidobacterium longum.
Article in Nature chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Comparative Insights into Digestion and Gut Microbiota Modulation of Polysaccharides from Ginseng, Ganoderma lucidum, and Dendrobium officinale.Foods (Basel, Switzerland) · 2026Article
- The colostrum chronicles: identifying porcine milk oligosaccharides in colostrum and investigating their role in litter performance.Journal of animal science · 2026Article
- Revisiting nitrogen assimilation strategies in the mammalian gut: lessons from Enterobacteriaceae as pathobiont models and a challenge to the limitation paradigm.Archives of microbiology · 2025Review
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- Article
- Cross-feeding of bifidobacteria promotes intestinal homeostasis: a lifelong perspective on the host health.NPJ biofilms and microbiomes · 2024Review
- Genomic factors shape carbon and nitrogen metabolic niche breadth across Saccharomycotina yeasts.Science (New York, N.Y.) · 2024Article
- Genomic and ecological factors shaping specialism and generalism across an entire subphylum.bioRxiv : the preprint server for biology · 2023Article
- Effect ofFoods (Basel, Switzerland) · 2023Article
- Milk glycan metabolism by intestinal bifidobacteria: insights from comparative genomics.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
21 authors at 6 institutions in 3 countries.
Funding
Abstract
Bifidobacteria are early colonizers of the human gut and play central roles in human health and metabolism. To thrive in this competitive niche, these bacteria evolved the capacity to use complex carbohydrates, including mammalian N-glycans. Herein, we elucidated pivotal biochemical steps involved in high-mannose N-glycan utilization by Bifidobacterium longum. After N-glycan release by an endo-β-N-acetylglucosaminidase, the mannosyl arms are trimmed by the cooperative action of three functionally distinct glycoside hydrolase 38 (GH38) α-mannosidases and a specific GH125 α-1,6-mannosidase. High-resolution cryo-electron microscopy structures revealed that bifidobacterial GH38 α-mannosidases form homotetramers, with the N-terminal jelly roll domain contributing to substrate selectivity. Additionally, an α-glucosidase enables the processing of monoglucosylated N-glycans. Notably, the main degradation product, mannose, is isomerized into fructose before phosphorylation, an unconventional metabolic route connecting it to the bifid shunt pathway. These findings shed light on key molecular mechanisms used by bifidobacteria to use high-mannose N-glycans, a perennial carbon and energy source in the intestinal lumen.
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Registered trials
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