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

IF 2.3 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Madhu Lata , T.N.C. Ramya
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引用次数: 0

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) ≥ LSTb (Siaα2-6GlcNAc) ≥ 6-SL (Siaα2-6Gal), 3-SL (Siaα2-3Gal) ≥ 6-SL (Siaα2-6Gal) > LSTb (Siaα2-6GlcNAc), and 3′-SL (Siaα2-3Gal) ≥ 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.

硅烷基糖酶、CpNanI、HpNanH 和 BbSia2 对 2-氨基苯甲酰胺标记的 3′-Sialyllactose、6′-Sialyllactose 和 Sialyllacto-N-tetraose-b 底物偏好的比较研究
硅烷基化酶催化硅烷基化生物大分子中末端硅酸的去除,它们对底物的偏好通常以裂解的糖苷键(α2-3、α2-6 和 α2-8)来表示,而不提及剩余的亚端还原糖分子。许多人体肠道共生菌和致病菌都会分泌硅烷酸酶来觅食硅烷酸,然后将其用作能量来源或同化为膜/囊结构成分。婴儿肠道共生菌也同样利用含有不同糖苷键的硅烷基化人乳寡糖。在这里,我们研究了双歧杆菌的 BbSia2、产气荚膜梭状芽孢杆菌的 CpNanI 和寄生褐藻的 HpNanH 等细菌ialid 酶对糖苷键 Siaα2-3Gal、Siaα2-6Gal 和 Siaα2-6Gal 的偏好、通过使用 2-氨基苯甲酰胺标记的母乳寡糖、3′-Sialyllactose(3′-SL)、6′-Sialyllactose(6′-SL)和 Sialyllacto-N-tetraose-b (LSTb)分别作为这些糖苷键的替代物,对 Siaα2-3Gal、Siaα2-6Gal 和 Siaα2-6GlcNAc 进行了分析。BbSia2、CpNanI 和 HpNanH 以糖苷键优先水解这三种寡糖、3′-SL (Siaα2-3Gal) ≥ LSTb (Siaα2-6GlcNAc) ≥ 6′-SL (Siaα2-6Gal), 3′-SL (Siaα2-3Gal) ≥ 6′-SL (Siaα2-6Gal) >;LSTb(Siaα2-6GlcNAc),以及 3′-SL(Siaα2-3Gal)≥ 6′-SL(Siaα2-6Gal)> LSTb(Siaα2-6GlcNAc)。我们的研究结果表明,亚端还原端糖分子会深刻影响硅烷基糖苷酶的底物偏好,因此主张从糖苷键和亚端还原端糖分子两个方面来表征和指示硅烷基糖苷酶的底物偏好。
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来源期刊
Biochemistry and Biophysics Reports
Biochemistry and Biophysics Reports Biochemistry, Genetics and Molecular Biology-Biophysics
CiteScore
4.60
自引率
0.00%
发文量
191
审稿时长
59 days
期刊介绍: Open access, online only, peer-reviewed international journal in the Life Sciences, established in 2014 Biochemistry and Biophysics Reports (BB Reports) publishes original research in all aspects of Biochemistry, Biophysics and related areas like Molecular and Cell Biology. BB Reports welcomes solid though more preliminary, descriptive and small scale results if they have the potential to stimulate and/or contribute to future research, leading to new insights or hypothesis. Primary criteria for acceptance is that the work is original, scientifically and technically sound and provides valuable knowledge to life sciences research. We strongly believe all results deserve to be published and documented for the advancement of science. BB Reports specifically appreciates receiving reports on: Negative results, Replication studies, Reanalysis of previous datasets.
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