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primary topic: A comparative study of the substrate preference of the sialidases, CpNanI, HpNanH, and BbSia2 towards 2-Aminobenzamide-labeled 3'-Sialyllactose, 6'-Sialyllactose, and Sialyllacto-N-tetraose-b

A comparative study of the substrate preference of the sialidases, CpNanI, HpNanH, and BbSia2 towards 2-Aminobenzamide-labeled 3'-Sialyllactose, 6'-Sialyllactose, and Sialyllacto-N-tetraose-b
type: AcademicArticle
type: Article
abstract: Sialidases catalyze the removal of terminal sialic acids from sialylated biomolecules, and their substrate preference is frequently indicated in terms of the glycosidic linkages cleaved (α2-3, α2-6, and α2-8) without mention of the remaining sub-terminal reducing-end saccharide moieties. Many human gut commensal and pathogenic bacteria secrete sialidases to forage for sialic acids, which are then utilized as an energy source or assimilated into membrane/capsular structural components. Infant gut commensals similarly utilize sialylated human milk oligosaccharides containing different glycosidic linkages. Here, we have studied the preference of the bacterial sialidases, BbSia2 from Bifidobacterium bifidum, CpNanI from Clostridium perfringens, and HpNanH from Glaesserella parasuis, for the glycosidic linkages, Siaα2-3Gal, Siaα2-6Gal, and Siaα2-6GlcNAc, by employing 2-Aminobenzamide-labeled human milk oligosaccharides, 3'-Sialyllactose (3'-SL), 6'-Sialyllactose (6'-SL), and Sialyllacto-N-tetraose-b (LSTb), respectively, as proxies for these glycosidic linkages. BbSia2, CpNanI, and HpNanH hydrolyzed these three oligosaccharides with the glycosidic linkage preferences, 3'-SL (Siaα2-3Gal) \geq LSTb (Siaα2-6GlcNAc) \geq 6'-SL (Siaα2-6Gal), 3'-SL (Siaα2-3Gal) \geq 6'-SL (Siaα2-6Gal) > LSTb (Siaα2-6GlcNAc), and 3'-SL (Siaα2-3Gal) \geq 6'-SL (Siaα2-6Gal) > LSTb (Siaα2-6GlcNAc), respectively. Our finding suggests that sub-terminal reducing-end saccharide moieties can profoundly influence the substrate preference of sialidases, and advocates for the characterization and indication of the substrate preference of sialidases in terms of both the glycosidic linkage and the sub-terminal reducing-end saccharide moiety.
date: 2024-09
volume: 39
issue: 101791
author list: authors
type: EPrint
type: ArticleEPrint
is part of: repository

Elsevier BV
type: Organization

Biochem. Biophys. Rep.
type: Collection

Madhu Lata
type: Person
given name: Madhu
family name: Lata

T N C Ramya
type: Person
given name: T N C
family name: Ramya

http://crdd.osdd.net/open/3325/
title: HTML Summary of #3325 A comparative study of the substrate preference of the sialidases, CpNanI, HpNanH, and BbSia2 towards 2-Aminobenzamide-labeled 3'-Sialyllactose, 6'-Sialyllactose, and Sialyllacto-N-tetraose-b
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primary topic: A comparative study of the substrate preference of the sialidases, CpNanI, HpNanH, and BbSia2 towards 2-Aminobenzamide-labeled 3'-Sialyllactose, 6'-Sialyllactose, and Sialyllacto-N-tetraose-b