Work

Bioinformatics-Facilitated Identification of Novel Bacterial Sulfoglycosidases That Hydrolyze 6-Sulfo-N-acetylglucosamine

Year: 2024

Type: article

Abstract: High Resolution Image Download MS PowerPoint Slide Glycan sulfation is a widespread postglycosylation modification crucial for modulating biological functions including cellular adhesion, signaling, and bacterial colonization. 6-Sulfo-β-GlcNAcases are a class of enzyme that alters sulfation patterns. Such changes in sulfation patterns are linked to diseases such as bowel inflammation, colitis, and cancer. Despite their significance, 6-sulfo-β-GlcNAcases, which cleave β-linked 6-sulfo- N -acetylglucosamine (6S-GlcNAc), have been but rarely identified. This scarcity results mainly from the short, diverse, and distinctive sulfate-binding motifs required for recognition of the 6-sulfate group in 6S-GlcNAc in addition to the conserved GH20 family features. In this study, we discovered 6-sulfo-β-GlcNAcases and assigned two novel sulfate-binding motifs by the use of comparative genomics, structural predictions, and activity-based screening. Our findings expand the known microbiota capable of degrading sulfated glycans and add significant enzymes to the tool kit for analysis and synthesis of sulfated oligosaccharides.

Source: ACS Bio & Med Chem Au

DOI: 10.1021/acsbiomedchemau.4c00088

Authors: Mochen Dong, Zhuoyun Chen, Yuan He, Rémi Zallot, Yi Jin

Institutions: Cardiff University, University of Manchester, Northwest University, Manchester Metropolitan University

Language: English

Topic: Glycosylation and Glycoproteins Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $3,500