Reference - Detail
| RRC ID | 21444 |
|---|---|
| Author | Garrido D, Nwosu C, Ruiz-Moyano S, Aldredge D, German JB, Lebrilla CB, Mills DA. |
| Title | Endo-β-N-acetylglucosaminidases from infant gut-associated bifidobacteria release complex N-glycans from human milk glycoproteins. |
| Journal | Mol Cell Proteomics |
| Abstract |
Breastfeeding is one of the main factors guiding the composition of the infant gut microbiota in the first months of life. This process is shaped in part by the high amounts of human milk oligosaccharides that serve as a carbon source for saccharolytic bacteria such as Bifidobacterium species. Infant-borne bifidobacteria have developed various molecular strategies for utilizing these oligosaccharides as a carbon source. We hypothesized that these species also interact with N-glycans found in host glycoproteins that are structurally similar to free oligosaccharides in human milk. Endo-β-N-acetylglucosaminidases were identified in certain isolates of Bifidobacterium longum subsp. longum, B. longum subsp. infantis, and Bifidobacterium breve, and their presence correlated with the ability of these strains to deglycosylate glycoproteins. An endoglycosidase from B. infantis ATCC 15697, EndoBI-1, was active toward all major types of N-linked glycans found in glycosylated proteins. Its activity was not affected by core fucosylation or extensive fucosylation, antenna number, or sialylation, releasing several N-glycans from human lactoferrin and immunoglobulins A and G. Extensive N-deglycosylation of whole breast milk was also observed after coincubation with this enzyme. Mutation of the active site of EndoBI-1 did not abolish binding to N-glycosylated proteins, and this mutant specifically recognized Man(3)GlcNAc(2)(α1-6Fuc), the core structure of human N-glycans. EndoBI-1 is constitutively expressed in B. infantis, and incubation of the bacterium with human or bovine lactoferrin led to the induction of genes associated to import and consumption of human milk oligosaccharides, suggesting linked regulatory mechanisms among these glycans. This work reveals an unprecedented interaction of bifidobacteria with host N-glycans and describes a novel endoglycosidase with broad specificity on diverse N-glycan types, potentially a useful tool for glycoproteomics studies. |
| Volume | 11(9) |
| Pages | 775-85 |
| Published | 2012-9-1 |
| DOI | 10.1074/mcp.M112.018119 |
| PII | S1535-9476(20)32587-1 |
| PMID | 22745059 |
| PMC | PMC3434770 |
| MeSH | Bifidobacterium / enzymology* Bifidobacterium / isolation & purification Bifidobacterium / metabolism Gastrointestinal Tract / microbiology* Glycoproteins / chemistry Glycoproteins / metabolism* Humans Infant Infant, Newborn Lactoferrin / metabolism Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / metabolism* Metagenome Milk, Human / chemistry Milk, Human / metabolism* Polysaccharides / metabolism* |
| IF | 4.87 |
| Times Cited | 78 |
| WOS Category | BIOCHEMICAL RESEARCH METHODS |
| Altmetric score |
オルトメトリクス指標項目
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| The most frequently cited source | Patent(IFI CLAIMS) |
| Total number of mentions | 18 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| General Microbes | JCM 1254 JCM 7002 JCM 7003 JCM 7004 JCM 7007 JCM 7009 JCM 7011 JCM 7017 JCM 7019 JCM 7020 JCM 11346 |