Complex pectin metabolism by gut bacteria reveals novel catalytic functions

Didier Ndeh, Artur Rogowski, Alan Cartmell, Ana S. Luis, Arnaud Baslé, Joseph Gray, Immacolata Venditto, Jonathon Briggs, Xiaoyang Zhang, Aurore Labourel, Nicolas Terrapon, Fanny Buffetto, Sergey Nepogodiev, Yao Xiao, Robert A. Field, Yanping Zhu, Malcolm A. O'Neill, Breeanna R. Urbanowicz, William S. York, Gideon J. DaviesD. Wade Abbott, Marie Christine Ralet, Eric C. Martens, Bernard Henrissat, Harry J. Gilbert

Research output: Contribution to journalArticlepeer-review

195 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)65-70
Number of pages6
JournalNature
Volume544
Issue number7648
Early online date22 Mar 2017
DOIs
Publication statusPublished - 6 Apr 2017

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