Sialylation of immunoglobulin E is a determinant of allergic pathogenicity.

ABSTRACT: Approximately one-third of the world's population suffers from allergies¹. Exposure to allergens crosslinks immunoglobulin E (IgE) antibodies that are bound to mast cells and basophils, 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 disease^3-5. 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 affect biological activity is completely unknown⁶. Here we perform an unbiased examination of glycosylation patterns of total IgE from individuals

SUBMITTER: Shade KC 

PROVIDER: S-EPMC7386252 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature