ArticleNature communications2024
Human gut microbes express functionally distinct endoglycosidases to metabolize the same N-glycan substrate.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- The functional and catalytic landscape of urease reveals a conserved target againstGut microbes · 2026Article
- Plant-Derived Foods and Medicines as Modulators of the Gut Microbiome: Molecular Interactions and Implications for Disease and Therapy.Molecules (Basel, Switzerland) · 2026Review
- Phytoplankton dynamics shape bacterioplankton community structure and metabolism during the austral summer-autumn transition in the Western Antarctic Peninsula.FEMS microbiology ecology · 2026Article
- Sequence-Based and Functional Analysis for the Discovery of N-Glycan Degrading Glycosidases From the Microbial Metagenome of the Infant Gut.MicrobiologyOpen · 2026Article
- Crystal structure of endo-β-N-acetylglucosaminidase HSα.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Herbal polysaccharides-a rising star in engineering multifunctional biomaterials for tissue repair and regeneration.Regenerative biomaterials · 2026Review
- Exploring the Activity of a NovelInternational journal of molecular sciences · 2025Article
- Understanding microbiota-driven oncogenesis: The role of metabolites in tumorigenesis.iScience · 2025Review
- Modeling glycans with AlphaFold 3: capabilities, caveats, and limitations.Glycobiology · 2025Article
- 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
- The mechanistic basis for interprotomer deglycosylation of antibodies by corynebacterial IgG-specific endoglycosidases.Nature communications · 2025Article
- Selective utilization of medicinal polysaccharides by human gut Bacteroides and Parabacteroides species.Nature communications · 2025Article
- Combined Inhibition of Thrombosis byInternational journal of general medicine · 2025Article
- Identification of serum N-glycans signatures in three major gastrointestinal cancers by high-throughput N-glycome profiling.Clinical proteomics · 2024Article
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Authors and funding
12 authors.
Funding
Abstract
Bacteroidales (syn. Bacteroidetes) are prominent members of the human gastrointestinal ecosystem mainly due to their efficient glycan-degrading machinery, organized into gene clusters known as polysaccharide utilization loci (PULs). A single PUL was reported for catabolism of high-mannose (HM) N-glycan glyco-polypeptides in the gut symbiont Bacteroides thetaiotaomicron, encoding a surface endo-β-N-acetylglucosaminidase (ENGase), BT3987. Here, we discover an ENGase from the GH18 family in B. thetaiotaomicron, BT1285, encoded in a distinct PUL with its own repertoire of proteins for catabolism of the same HM N-glycan substrate as that of BT3987. We employ X-ray crystallography, electron microscopy, mass spectrometry-based activity measurements, alanine scanning mutagenesis and a broad range of biophysical methods to comprehensively define the molecular mechanism by which BT1285 recognizes and hydrolyzes HM N-glycans, revealing that the stabilities and activities of BT1285 and BT3987 were optimal in markedly different conditions. BT1285 exhibits significantly higher affinity and faster hydrolysis of poorly accessible HM N-glycans than does BT3987. We also find that two HM-processing endoglycosidases from the human gut-resident Alistipes finegoldii display condition-specific functional properties. Altogether, our data suggest that human gut microbes employ evolutionary strategies to express distinct ENGases in order to optimally metabolize the same N-glycan substrate in the gastroinstestinal tract.
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