ArticleApplied and environmental microbiology2012
Lactobacillus casei ferments the N-Acetylglucosamine moiety of fucosyl-α-1,3-N-acetylglucosamine and excretes L-fucose.
Article in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 49 citations in OpenAlex.
- Trial
- Chb and nag genes drive N,N'-diacetylchitobiose metabolism in probiotic Lacticaseibacillus paracasei.Applied microbiology and biotechnology · 2026Article
- FUT2-mediated intestinal fucosylation: a master regulator of host-microbiota symbiosis in health and disease.Frontiers in microbiology · 2026Review
- Prebiotic potential of exopolysaccharide-derived oligosaccharides prepared using sandwich-integration bioprocess of acidolysis-electrodialysis and microbial fermentation.Food chemistry: X · 2025Article
- The Impact of Human Milk Oligosaccharides on Antibiotic-Induced Microbial Dysbiosis and Gut Inflammation in Mice.Antibiotics (Basel, Switzerland) · 2025Article
- Human Milk Oligosaccharides: Decoding Their Structural Variability, Health Benefits, and the Evolution of Infant Nutrition.Nutrients · 2024Review
- Molecular strategies for the utilisation of human milk oligosaccharides by infant gut-associated bacteria.FEMS microbiology reviews · 2023Review
- L-Fucose is involved in human-gut microbiome interactions.Applied microbiology and biotechnology · 2023Review
- Necrotizing Enterocolitis: The Role of Hypoxia, Gut Microbiome, and Microbial Metabolites.International journal of molecular sciences · 2023Review
- Characterization and stabilization of the α-L-fucosidase set from Lacticaseibacillus rhamnosus INIA P603.Applied microbiology and biotechnology · 2022Article
- Infant-gut associated Bifidobacterium dentium strains utilize the galactose moiety and release lacto-N-triose from the human milk oligosaccharides lacto-N-tetraose and lacto-N-neotetraose.Scientific reports · 2021Article
- Acceptive Immunity: The Role of Fucosylated Glycans in Human Host-Microbiome Interactions.International journal of molecular sciences · 2021Review
- Human milk and mucosa-associated disaccharides impact on cultured infant fecal microbiota.Scientific reports · 2020Article
- Evaluating the Impact of Four Major Nutrients on Gut Microbial Metabolism by a Targeted Metabolomics Approach.Journal of proteome research · 2020Article
- Article
- The lactose operon from Lactobacillus casei is involved in the transport and metabolism of the human milk oligosaccharide core-2 N-acetyllactosamine.Scientific reports · 2018Article
- Utilization of Host-Derived Glycans by IntestinalFrontiers in microbiology · 2018Review
- Systematic genetic dissection of PTS in Vibrio cholerae uncovers a novel glucose transporter and a limited role for PTS during infection of a mammalian host.Molecular microbiology · 2017Article
- The Extracellular Wall-Bound β-N-Acetylglucosaminidase from Lactobacillus casei Is Involved in the Metabolism of the Human Milk Oligosaccharide Lacto-N-Triose.Applied and environmental microbiology · 2016Article
- Enteric Pathogens Exploit the Microbiota-generated Nutritional Environment of the Gut.Microbiology spectrum · 2015Article
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have previously characterized from Lactobacillus casei BL23 three α-L-fucosidases, AlfA, AlfB, and AlfC, which hydrolyze in vitro natural fucosyl-oligosaccharides. In this work, we have shown that L. casei is able to grow in the presence of fucosyl-α-1,3-N-acetylglucosamine (Fuc-α-1,3-GlcNAc) as a carbon source. Interestingly, L. casei excretes the L-fucose moiety during growth on Fuc-α-1,3-GlcNAc, indicating that only the N-acetylglucosamine moiety is being metabolized. Analysis of the genomic sequence of L. casei BL23 shows that downstream from alfB, which encodes the α-L-fucosidase AlfB, a gene, alfR, that encodes a transcriptional regulator is present. Divergently from alfB, three genes, alfEFG, that encode proteins with homology to the enzyme IIAB (EIIAB), EIIC, and EIID components of a mannose-class phosphoenolpyruvate:sugar phosphotransferase system (PTS) are present. Inactivation of either alfB or alfF abolishes the growth of L. casei on Fuc-α-1,3-GlcNAc. This proves that AlfB is involved in Fuc-α-1,3-GlcNAc metabolism and that the transporter encoded by alfEFG participates in the uptake of this disaccharide. A mutation in the PTS general component enzyme I does not eliminate the utilization of Fuc-α-1,3-GlcNAc, suggesting that the transport via the PTS encoded by alfEFG is not coupled to phosphorylation of the disaccharide. Transcriptional analysis with alfR and ccpA mutants shows that the two gene clusters alfBR and alfEFG are regulated by substrate-specific induction mediated by the inactivation of the transcriptional repressor AlfR and by carbon catabolite repression mediated by the catabolite control protein A (CcpA). This work reports for the first time the characterization of the physiological role of an α-L-fucosidase in lactic acid bacteria and the utilization of Fuc-α-1,3-GlcNAc as a carbon source for bacteria.
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