Functions and specificity of bacterial carbohydrate sulfatases targeting host glycans

Luis, Ana S, Yates, Edwin A ORCID: 0000-0001-9365-5433 and Cartmell, Alan ORCID: 0000-0002-5512-249X (2023) Functions and specificity of bacterial carbohydrate sulfatases targeting host glycans. ESSAYS IN BIOCHEMISTRY, 67 (3). pp. 429-442.

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Official URL: http://dx.doi.org/10.1042/ebc20220120

Abstract

Sulfated host glycans (mucin O-glycans and glycosaminoglycans [GAGs]) are critical nutrient sources and colonisation factors for Bacteroidetes of the human gut microbiota (HGM); a complex ecosystem comprising essential microorganisms that coevolved with humans to serve important roles in pathogen protection, immune signalling, and host nutrition. Carbohydrate sulfatases are essential enzymes to access sulfated host glycans and are capable of exquisite regio- and stereo-selective substrate recognition. In these enzymes, the common recognition features of each subfamily are correlated with their genomic and environmental context. The exo-acting carbohydrate sulfatases are attractive drug targets amenable to small-molecule screening and subsequent engineering, and their high specificity will help elucidate the role of glycan sulfation in health and disease. Inhibition of carbohydrate sulfatases provides potential routes to control Bacteroidetes growth and to explore the influence of host glycan metabolism by Bacteroidetes on the HGM ecosystem. The roles of carbohydrate sulfatases from the HGM organism Bacteroides thetaiotaomicron and the soil isolated Pedobacter heparinus (P. heparinus) in sulfated host glycan metabolism are examined and contrasted, and the structural features underpinning glycan recognition and specificity explored.

Item Type:	Article
Uncontrolled Keywords:	Humans, Bacteria, Sulfatases, Carbohydrates, Polysaccharides, Glycosaminoglycans, Ecosystem
Divisions:	Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology
Depositing User:	Symplectic Admin
Date Deposited:	07 Feb 2023 11:18
Last Modified:	31 May 2023 12:15
DOI:	10.1042/EBC20220120
Open Access URL:	https://doi.org/10.1042/EBC20220120
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3168245