A native IgE in complex with profilin provides insights into allergen recognition and cross-reactivity.

ABSTRACT: Allergies have become a rising health problem, where plentiful substances can trigger IgE-mediated allergies in humans. While profilins are considered minor allergens, these ubiquitous proteins are primary molecules involved in cross-reactivity and pollen-food allergy syndrome. Here we report the first crystal structures of murine Fab/IgE, with its chains naturally paired, in complex with the allergen profilin from Hevea brasiliensis (Hev b 8). The crystallographic models revealed that the IgE's six complementarity-determining regions (CDRs) interact with the allergen, comprising a rigid paratope-epitope surface of 926 Ų, which includes an extensive network of interactions. Interestingly, we also observed previously unreported flexibility at Fab/IgE's elbow angle, which did not

SUBMITTER: Garcia-Ramirez B 

PROVIDER: S-EPMC9334453 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature