Journal
NATURE
Volume 544, Issue 7648, Pages 65-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature21725
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Funding
- European Research Council [322820]
- Agence Nationale de la Recherche [ANR 12-BIME-0006-01]
- Biotechnology and Biological Research Council [BB/K020358/1, BB/K001949/1]
- Wellcome Trust [WT097907MA]
- European Union Seventh Framework Programme under the WallTraC project [263916]
- Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the US Department of Energy [DE-FG02-12ER16324]
- Marie Sklodowska-Curie Fellowship [707922]
- Beef and Cattle Research Council [FDE.15.13]
- BBSRC [BBS/E/J/000C0618, BBS/E/J/000PR9790] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BBS/E/J/000C0618, BBS/E/J/000PR9790] Funding Source: researchfish
- Marie Curie Actions (MSCA) [707922] Funding Source: Marie Curie Actions (MSCA)
- Agence Nationale de la Recherche (ANR) [ANR-12-BIME-0006] Funding Source: Agence Nationale de la Recherche (ANR)
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The metabolism of carbohydrate polymers drives microbial diversity in the human gut microbiota. It is unclear, however, whether bacterial consortia or single organisms are required to depolymerize highly complex glycans. Here we show that the gut bacterium Bacteroides thetaiotaomicron uses the most structurally complex glycan known: the plant pectic polysaccharide rhamnogalacturonan-II, cleaving all but 1 of its 21 distinct glycosidic linkages. The deconstruction of rhamnogalacturonan-II side chains and backbone are coordinated to overcome steric constraints, and the degradation involves previously undiscovered enzyme families and catalytic activities. The degradation system informs revision of the current structural model of rhamnogalacturonan-II and highlights how individual gut bacteria orchestrate manifold enzymes to metabolize the most challenging glycan in the human diet.
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