Instead, analysis of (C) anti-TNP IgE mAbs in blood serum 6 h after injection by TNP-reactive ELISA (n = 3 for all groups) or (D) (anti-TNP) IgE loading on blood basophils 6 h after injection by flow cytometry (n = 2-5 for all groups). Sialylation of IgE reduces Fc RI interaction and mast cell and basophil activation in vitro and increases IgE half-life in vivo De-sialylated anti-TNP IgE mAbs showed a stronger interaction with human and murine Fc RI than originally sialylated and additionally sialylated IgE mAbs, whereas the latter two sialylated IgE glycoforms showed a comparable low or no interaction with Fc RI in these assays, respectively (Figure 1F). Immunoglobulin E (IgE) plays a crucial role in allergic reactions, including systemic anaphylaxis, by binding to the high-affinity IgE receptor Fc RI (Fc RI + Fc RI + Fc RI ) on mast cells and basophils and, upon allergen-mediated aggregation, inducing the release of inflammatory mediators.[[1], [3]] The allergic potential of IgE antibodies (Abs) is further affected by IgE glycosylation-dependent interactions with membrane-bound and soluble carbohydrate-binding proteins (e.g., galectins, siglecs, and C-type lectin receptors) as well as different structural features (E1-4).[[1], [3]] Many healthy individuals harbor allergen-specific IgE Abs in the absence of an allergic disease (E5, E6), suggesting qualitative differences in IgE-triggered responses. [Extracted from the article]