Background: Adults suffering from wheat-dependant, exercise-induced anaphylaxis (WDEIA) develop IgE directed against wheat ω5-gliadins (major allergens for this allergy) and against wheat low-molecular weight glutenin subunits (LMW-GS). However, the ability of LMW-GS to trigger an inflammatory response is still unknown. It also remains to be determined if IgE from these patients bind the same epitopes on LMW-GS and ω5-gliadins or if the epitopes are independent. Methods: WDEIA patients were selected and skin prick tests (SPTs) were performed on them using commercial gluten, wheat flour extracts, prolamin fractions and a purified natural LMW-GS P42. The IgE-binding ability of natural and recombinant wheat prolamins was verified by immunoblot experiments. Cross-reactivity between LMW-GS and ω5-gliadins was studied by immunoblot inhibition experiments, using purified natural ω5-gliadin as an inhibitor. Results: Patients developed positive SPTs with natural LMW-GS fractions and/or with the purified LMW-GS P42. Natural and recombinant LMW-GS were highly reactive with patient IgE in immunoblot experiments, as was ω5-gliadin. However, differences in reactivity were evident within the LMW-GS group. Except for one recombinant LMW-GS (P73), IgE cross-reactivity between LMW-GS and natural ω5-gliadin was only partial. Conclusion: LMW-GS are able to promote local inflammation and they share common epitopes with ω5-gliadins. The nature of these epitopes is discussed. LMW-GS also carried specific epitopes, completely independent from the ω5-gliadin epitopes. Thus, LMW-GS behaved partly as independent allergens.
