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

Lookup NU author(s): Justina Briliūtė, Dr Elisabeth Lowe, Dr David Bolam, Dr Lucy Crouch



This is the authors' accepted manuscript of an article that has been published in its final definitive form by Springer Nature, 2019.

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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 which are secreted into the intestine at high levels. Here we show that many mutualistic gut Bacteroides spp. have the capacity to utilise 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 B.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 (CAZymes) from different families, including a CNG specific endo-glycosidase activity. Furthermore, CNG degradation involves the activity of CAZymes 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.

Publication metadata

Author(s): Briliute J, Urbanowicz PA, Luis AS, Baslé A, Paterson N, Rebello O, Hendel J, Ndeh DA, Lowe EC, Martens EC, Spencer DIR, Bolam DN, Crouch LI

Publication type: Article

Publication status: Published

Journal: Nature Microbiology

Year: 2019

Volume: 4

Pages: 1571-1581

Print publication date: 01/09/2019

Online publication date: 03/06/2019

Acceptance date: 24/04/2019

Date deposited: 20/06/2019

ISSN (electronic): 2058-5276

Publisher: Springer Nature


DOI: 10.1038/s41564-019-0466-x


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Funder referenceFunder name
BBSRC/Innovate UK IB catalyst award