Purpose ω-5 gliadin is the major allergen that causes wheat-dependent exercise-induced anaphylaxis (WDEIA). Recently, a missing mutant wheat cultivar at 1B chromosome Glu-B3 and closely linked Gli-B1 loci was bred. This cultivar (ω5D) has a deficiency in ω-5 and γ-gliadins as well as some low-molecular-weight glutenins. We evaluated specific immunoglobulin E (sIgE) reactivity of the ω5D in WDEIA patients compared to wild-type cultivar. Methods Serum samples from 14 WDEIA and 7 classic wheat allergy patients were used to compare the allergenicity of ω5D and wild-type cultivars using immunoglobulin E immunoblotting, enzyme-linked immunosorbent assay (ELISA), and ImmunoCAP inhibition assays. Results Immunoblotting revealed that ω5D extracts had less sIgE binding to gliadins and glutenins in WDEIA sera than wild-type extracts. Immunoblot inhibition assay for gliadin sIgE reactivity also showed that ω5D gliadins had less allergenicity than wild-type gliadins. ELISA inhibition assay showed stronger allergenicity of gliadins than glutenins, although they had cross-reactivity. This assay also showed that the 50% inhibitory concentrations (IC50) of ω5D extracts against gliadin- or glutenin-sIgE reactivity were approximately 4-fold higher in WDEIA patients than those of wild-type extracts. The inhibition capacity of ω5D gliadins against recombinant ω-5 gliadin-sIgE reactivity was also lower in WDEIA patients than that of wild-type. Conclusions The allergenicity of the ω5D cultivar is markedly lower for WDEIA patients in the sIgE inhibition tests. These results suggest that the ω5D cultivar may be a safe alternative for WDEIA patients.
rs.com/artic le/uk-healt h-coron aviru s-brita in-life/uk-lockd own-life-binge -eatin g-more-alcoh olless-exerc ise-idUKK CN24S1BJ
Background: Sawtooth oak is a potent cause of tree pollinosis in Korea. However, molecular characteristics of the major allergen have not been elucidated. Objective: The study was to perform biochemical and allergenic characterization from sawtooth oak. Methods: Native Que ac 1 was purified and analyzed by 2D gel electrophoresis and LC-coupled ESI-MS/MS analysis. Polymorphisms of Que ac 1 were examined by RT-PCR, and a recombinant allergen of the major isoform was produced. IgE reactivities of the native and recombinant allergens were compared by ELISA. Results: At least 12 isoforms of Que ac 1 were identified by proteomic analysis, and 22 isoforms including two isoallergens were identified by RT-PCR. A major isoform Que ac 1.0101 (13.3%, 10/75) shared the lowest homology to Bet v 1 (58.1%) and the highest homology to Que r 1 (83.0%). Recombinant Que ac 1.0101, which exhibited a similar CD spectrum with native Que ac 1, was recognized by serum IgE from 91.3% of Korean oak pollinosis patients. Recombinant Que ac 1 inhibited 67.2% of IgE reactivity to sawtooth pollen extract, but native Que ac 1 and recombinant Bet v 1 inhibited 88.7% and 57.6% of the IgE reactivity, respectively. No difference in allergen potential was shown between Que ac 1 and Bet v 1 by basophil mediator release assay. Conclusion: Molecular properties of the major allergen Que ac 1 were characterized. Que ac 1 seems to be an allergen of regional importance homologous to Bet v 1 and may be useful for better diagnostics of pollinosis.
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