Complex pectin metabolism by gut bacteria reveals novel catalytic functions

DOI: 10.1038/nature21725

Authors: Didier Ndeh (Newcastle University) , Artur Rogowski (Newcastle University) , Alan Cartmell (Newcastle University) , Ana S. Luis (Newcastle University) , Arnaud Basle (Newcastle University) , Joseph Gray (Newcastle University) , Immacolata Venditto (CIISA, Faculdade de Medicina Veterinaria, Universidade de Lisboa) , Jonathon Briggs (Newcastle University) , Xiaoyang Zhang (Newcastle University) , Aurore Labourel (Newcastle University) , Nicolas Terrapon (Aix-Marseille University) , Fanny Buffetto (INRA) , Sergey Nepogodiev (John Innes Centre Norwich Research Park) , Yao Xiao (University of Michigan Medical School) , Robert A. Field (John Innes Centre Norwich Research Park) , Yanping Zhu (The University of Georgia) , Malcolm A. O’neill (The University of Georgia) , Breeanna R. Urbanowicz (The University of Georgia) , William S. York (The University of Georgia) , Gideon J. Davies (University of York) , D. Wade Abbott (Lethbridge Research Centre) , Marie-christine Ralet (INRA) , Eric C. Martens (University of Michigan Medical School) , Bernard Henrissat (INRA; King Abdulaziz University) , Harry J. Gilbert (Newcastle University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature , VOL 411

State: Published (Approved)
Published: March 2017
Diamond Proposal Number(s): 1960 , 7854 , 9948

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.

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I24-Microfocus Macromolecular Crystallography