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Review
. 2019:423:77-93.
doi: 10.1007/82_2019_151.

IgE Glycosylation in Health and Disease

Kai-Ting Shade  1 , Michelle E Conroy  1 , Robert M Anthony  2
Affiliations
Review

IgE Glycosylation in Health and Disease

Kai-Ting Shade et al. Curr Top Microbiol Immunol. 2019.

Abstract

IgE are absolutely required for initiation of allergy reactions, which affect over 20% of the world's population. IgE are the least prevalent immunoglobulins in circulation with 12-h and 2-day half-lives in mouse and human serum, respectively, but an extended tissue half-life of 3-weeks bound to the surface of mast cells by the high affinity IgE receptor, FcεRI (Gould and Sutton 2008). Although the importance of glycosylation to IgG biology is well established, less is known regarding the contribution of IgE glycosylation to allergic inflammation. IgE has seven and nine N-linked glycosylation sites distributed across human and murine constant chains, respectively. Here we discuss studies that have analyzed IgE glycosylation and its function, and how IgE glycosylation contributions to health and disease.

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Figures

Fig. 1
Fig. 1. Human IgE and its glycans.
a Schematics of IgE structure and glycosylation. Predicted N-glycosylation sites in each constant domain (Cε) are represented by closed and open circles for complex and oligomannose glycans, respectively. b Complex glycans are composed of fucose (red), GlcNAc (blue), mannose (green), galactose (yellow circles), and sialic acid (pink). Core complex structure is shown in dotted box. Oligomannose glycans are composed of GlcNAc and between 5 and 9 mannoses
See this image and copyright information in PMC

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