Person: Shade, Kai-Ting
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Shade
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Kai-Ting
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Shade, Kai-Ting
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Publication Sialylation of Immunoglobulin E Is a Determinant of Allergic Pathogenicity(Springer Science and Business Media LLC, 2020-05-20) Shade, Kai-Ting; Conroy, Michelle; Washburn, Nathaniel; Kitaoka, Maya; Huynh, Daniel; Laprise, Emma; Patil, Sarita U.; Shreffler, Wayne; Anthony, Robert M.; Anthony, RApproximately one-third of the world’s population suffers from allergies1. Allergen exposure crosslinks mast cell- and basophil-bound immunoglobulin E (IgE), triggering the release of inflammatory mediators, including histamine2. Although IgE is absolutely required for allergies, it is not understood why total and allergen-specific IgE concentrations do not reproducibly correlate with allergic disease3-5. It is well-established that glycosylation of IgG dictates its effector function and has disease-specific patterns. However, whether IgE glycans differ in disease states or impact biological activity is completely unknown6. We therefore unbiasedly examined glycosylation patterns of total IgE from peanut-allergic and non-atopic individuals. This revealed an increase in sialic acid content on total IgE from peanut-allergic individuals compared to non-atopic subjects. Sialic acid removal from IgE attenuated effector cell degranulation and anaphylaxis in multiple functional models of allergic disease. Therapeutic interventions, including sialic acid removal from cell-bound IgE with a FcεRI targeted-neuraminidase, or administration of asialylated IgE, markedly reduced anaphylaxis. Together, these results establish IgE glycosylation, and specifically sialylation, as an important regulator of allergic disease.