Antigen properties shape organization of FcεRI aggregates to tune mast cell signaling.

ABSTRACT: Fc receptors containing immunoreceptor tyrosine-based activation motifs (ITAMs) are critical components of the innate immune system that bridge adaptive antibody recognition to cellular effector responses. In allergic responses, the high-affinity IgE receptor, FcεRI, is activated when multivalent antigens crosslink receptor-bound IgE, yet the molecular mechanisms linking antigen structure to signaling output remain incompletely understood. Here, we compare two antigens presenting identical IgE-binding haptens but differing in geometry: the high-valency, heterogeneous DNP-BSA and the defined trivalent antigen DF3. We find that these ligands elicit distinct patterns of degranulation and FcεRI γ-chain phosphorylation, correlating with differences in the recruitment of the inhibitory lipid pho

SUBMITTER: Rinaldi DA 

PROVIDER: S-EPMC10441289 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature