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An enzymatic strategy to asymmetrically branched N-glycans.

ABSTRACT: An enzymatic strategy was developed to generate asymmetrically branched N-glycans from natural sources by using a panel of glycosidases and glycosyltransferases. Briefly, LacZ ?-galactosidase was employed to selectively trim symmetrically branched N-glycans isolated from bovine fetuin. The yielding structures were then converted to asymmetrically branched core structures by robust glycosyltransferase for further extension.

SUBMITTER: Calderon AD

PROVIDER: S-EPMC5603075 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature

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An enzymatic strategy to asymmetrically branched N-glycans.

Calderon Angie D AD Zhou Jun J Guan Wanyi W Wu Zhigang Z Guo Yuxi Y Bai Jing J Li Qing Q Wang Peng George PG Fang Junqiang J Li Lei L

Organic & biomolecular chemistry 20170901 35

An enzymatic strategy was developed to generate asymmetrically branched N-glycans from natural sources by using a panel of glycosidases and glycosyltransferases. Briefly, LacZ β-galactosidase was employed to selectively trim symmetrically branched N-glycans isolated from bovine fetuin. The yielding structures were then converted to asymmetrically branched core structures by robust glycosyltransferase for further extension. ...[more]

PMID: 28832049

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Project description:Patients with IgA nephropathy (IgAN) have elevated circulating levels of IgA1 with some O-glycans consisting of galactose (Gal)-deficient N-acetylgalactosamine (GalNAc) with or without N-acetylneuraminic acid (NeuAc). We have analyzed O-glycosylation heterogeneity of naturally asialo-IgA1 (Ale) myeloma protein that mimics Gal-deficient IgA1 (Gd-IgA1) of patients with IgAN, except that IgA1 O-glycans of IgAN patients are frequently sialylated. Specifically, serum IgA1 of healthy controls has more ?2,3-sialylated O-glycans (NeuAc attached to Gal) than ?2,6-sialylated O-glycans (NeuAc attached to GalNAc). As IgA1-producing cells from IgAN patients have an increased activity of ?2,6-sialyltransferase (ST6GalNAc), we hypothesize that such activity may promote premature sialylation of GalNAc and, thus, production of Gd-IgA1, as sialylation of GalNAc prevents subsequent Gal attachment. Distribution of NeuAc in IgA1 O-glycans may play an important role in the pathogenesis of IgAN. To better understand biological functions of NeuAc in IgA1, we established protocols for enzymatic sialylation leading to ?2,3- or ?2,6-sialylation of IgA1 O-glycans. Sialylation of Gal-deficient asialo-IgA1 (Ale) myeloma protein by an ST6GalNAc enzyme generated sialylated IgA1 that mimics the Gal-deficient IgA1 glycoforms in patients with IgAN, characterized by ?2,6-sialylated Gal-deficient GalNAc. In contrast, sialylation of the same myeloma protein by an ?2,3-sialyltransferase yielded IgA1 typical for healthy controls, characterized by ?2,3-sialylated Gal. The GalNAc-specific lectin from Helix aspersa (HAA) is used to measure levels of Gd-IgA1. We assessed HAA binding to IgA1 sialylated at Gal or GalNAc. As expected, ?2,6-sialylation of IgA1 markedly decreased reactivity with HAA. Notably, ?2,3-sialylation also decreased reactivity with HAA. Neuraminidase treatment recovered the original HAA reactivity in both instances. These results suggest that binding of a GalNAc-specific lectin is modulated by sialylation of GalNAc as well as Gal in the clustered IgA1 O-glycans. Thus, enzymatic sialylation offers a useful model to test the role of NeuAc in reactivities of the clustered O-glycans with lectins.

Dataset Information

An enzymatic strategy to asymmetrically branched N-glycans.

Publications

An enzymatic strategy to asymmetrically branched N-glycans.

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