Proteomics

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The Human Gut Firmicute Roseburia intestinalis is a Primary Degrader of Dietary β-Mannans


ABSTRACT: β-Mannans are plant cell wall polysaccharides that are commonly found in human diets. However, a mechanistic understanding into the key populations that degrade this glycan is absent, especially for the dominant Firmicutes phylum. Here, we show that the prominent butyrate-producing Firmicute Roseburia intestinalis expresses two loci conferring metabolism of β-mannans. We combine multi-“omic” analyses and detailed biochemical studies to comprehensively characterize loci-encoded proteins that are involved in β-mannan capturing, importation, de-branching and degradation into monosaccharides. In mixed cultures, R. intestinalis shares the available β-mannan with Bacteroides ovatus, demonstrating that the apparatus allows coexistence in a competitive environment. In murine experiments, β-mannan selectively promotes beneficial gut bacteria, exemplified by increased R. intestinalis, and reduction of mucus-degraders. Our findings highlight that R. intestinalis is a primary degrader of this dietary fiber and that this metabolic capacity could be exploited to selectively promote key members of the healthy microbiota using β-mannan-based therapeutic interventions.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Roseburia Intestinalis L1-82

SUBMITTER: Magnus Arntzen  

LAB HEAD: Bjørge Westereng

PROVIDER: PXD012448 | Pride | 2019-02-21

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
CWA_Glc_1_1.raw Raw
CWA_Glc_1_2.raw Raw
CWA_Glc_1_3.raw Raw
CWA_Glc_2_1.raw Raw
CWA_Glc_2_2.raw Raw
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β-Mannans are plant cell wall polysaccharides that are commonly found in human diets. However, a mechanistic understanding into the key populations that degrade this glycan is absent, especially for the dominant Firmicutes phylum. Here, we show that the prominent butyrate-producing Firmicute Roseburia intestinalis expresses two loci conferring metabolism of β-mannans. We combine multi-"omic" analyses and detailed biochemical studies to comprehensively characterize loci-encoded proteins that are  ...[more]

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