Complex N-glycan breakdown by gut Bacteroides involves an extensive enzymatic apparatus encoded by multiple co-regulated genetic loci

Justina Briliūtė, Paulina A. Urbanowicz, Ana S. Luis, Arnaud Baslé, Neil Paterson, Osmond Rebello, Jenifer Hendel, Didier A. Ndeh, Elisabeth C. Lowe, Eric C. Martens, Daniel I. R. Spencer, David N. Bolam (Lead / Corresponding author), Lucy I. Crouch (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)

Abstract

Glycans are the major carbon sources available to the human colonic microbiota. Numerous N-glycosylated proteins are found in the human gut, from both dietary and host sources, including immunoglobulins such as IgA that are secreted into the intestine at high levels. Here, we show that many mutualistic gut Bacteroides spp. have the capacity to utilize complex N-glycans (CNGs) as nutrients, including those from immunoglobulins. Detailed mechanistic studies using transcriptomic, biochemical, structural and genetic techniques reveal the pathway employed by Bacteroides thetaiotaomicron (Bt) for CNG degradation. The breakdown process involves an extensive enzymatic apparatus encoded by multiple non-adjacent loci and comprises 19 different carbohydrate-active enzymes from different families, including a CNG-specific endo-glycosidase activity. Furthermore, CNG degradation involves the activity of carbohydrate-active enzymes that have previously been implicated in the degradation of other classes of glycan. This complex and diverse apparatus provides Bt with the capacity to access the myriad different structural variants of CNGs likely to be found in the intestinal niche.

Original languageEnglish
Pages (from-to)1571-1581
Number of pages11
JournalNature Microbiology
Volume4
Issue number9
Early online date3 Jun 2019
DOIs
Publication statusPublished - Sep 2019

Keywords

  • Bacterial genetics
  • Biochemistry
  • Microbiome
  • Structural biology

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