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Glycoproteomic studies of IgE from a novel hyper IgE syndrome linked to PGM3 mutation.

Abstract：

:Glycans serve as important regulators of antibody activities and half-lives. IgE is the most heavily glycosylated antibody, but in comparison to other antibodies little is known about its glycan structure function relationships. We therefore describe the site specific IgE glycosylation from a patient with a novel hyper IgE syndrome linked to mutations in PGM3, which is an enzyme involved in synthesizing UDP-GlcNAc, a sugar donor widely required for glycosylation. A two-step method was developed to prepare two IgE samples from less than 1 mL of serum collected from a patient with PGM3 mutation and a patient with atopic dermatitis as a control subject. Then, a glycoproteomic strategy was used to study the site-specific glycosylation. No glycosylation was found at Asn264, whilst high mannose glycans were only detected at Asn275, tri-antennary glycans were exclusively observed at Asn99 and Asn252, and non-fucosylated complex glycans were detected at Asn99. The results showed similar glycosylation profiles between the two IgE samples. These observations, together with previous knowledge of IgE glycosylation, imply that IgE glycosylation is similarly regulated among healthy control, allergy and PGM3 related hyper IgE syndrome.

journal_name

Glycoconj J

journal_title

Glycoconjugate journal

authors

Wu G,Hitchen PG,Panico M,North SJ,Barbouche MR,Binet D,Morris HR,Dell A,Haslam SM

doi

10.1007/s10719-015-9638-y

subject

Has Abstract

pub_date

2016-06-01 00:00:00

pages

447-56

issue

3

eissn

0282-0080

issn

1573-4986

pii

10.1007/s10719-015-9638-y

journal_volume

33

pub_type

杂志文章

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