•The distribution of rice allergens in brown rice grains were examined.•The allergenicity of cosmetics and health foods containing rice bran were analyzed.•The 52-kDa globulin was found in rice bran ...and products containing rice bran.•The 52-kDa globulin is the most likely causative allergen of rice bran allergy.
To understand the allergenicity of rice bran, the distribution of rice allergens in brown rice grains was analysed and the allergenicity of cosmetics and health foods containing rice bran determined. RAG2 and a 19-kDa globulin were localized in polished rice, while a 52-kDa globulin was localized in rice bran. The 52-kDa globulin was also identified as the most likely causative allergen of rice bran allergy. Several products containing intact rice bran were found to contain the 52-kDa globulin. Our study provides the first data regarding cosmetics and health foods containing potential rice bran allergens. Western blot analysis using a rice-bran-allergic patient’s plasma showed that 52-kDa globulin was detected as an IgE-binding protein of rice bran and some rice bran-containing cosmetics and health foods. Our results indicate that patients with rice bran allergy need to be careful about using products containing intact rice bran as a constituent.
Buckwheat allergy is an immediate hypersensitivity reaction that includes anaphylaxis mediated by specific IgE antibodies. Several IgE-binding proteins in common buckwheat have been reported to be ...possible clinically relevant buckwheat allergens. Although common buckwheat is popularly consumed in Asia, buckwheat allergy is becoming a serious problem not only in Asia but also in Europe. In addition, common buckwheat has also been found to be a causative agent of allergic symptoms in animals. In recent years, in addition to conventional food allergy testing methods, the development of component-resolved diagnosis (CRD) has improved the diagnostic accuracy of food allergy. The identification of allergens is essential for the construction of CRD. In this review, we introduce the different types of buckwheat allergens and discuss how each buckwheat allergen contributes to the diagnosis of buckwheat allergy. We also present the analysis of buckwheat allergen that will help reduce the allergenicity of common buckwheat and reduce buckwheat allergen molecules. These findings may be beneficial in overcoming buckwheat allergies in humans and animals.
Scope
Buckwheat is a common food allergen frequently consumed in Asian countries, with Fag e 1 and Fag e 2 being the major buckwheat allergens. The purpose of this study is to prepare an oral ...immunotherapy agent by attenuating these allergens via phosphorylation. The immunomodulatory effects of phosphorylated Fag e 2 (P‐Fag e 2) in a mouse model of buckwheat allergy are evaluated.
Methods and results
Phosphorylated Fag e 1 (P‐Fag e 1) and P‐Fag e 2 are prepared by dry‐heating in the presence of pyrophosphate. Subsequent dot‐blot analysis using serum from food‐allergic patient indicates that both proteins exhibit reduced allergenicity upon phosphorylation. Mice subjected to oral administration of P‐Fag e 2 for 6 weeks exhibit decreased specific serum IgE and increased specific IgA after Fag e 2 sensitization compared to the sham‐treated mice. Moreover, the Peyer's patches (PP) of phosphorylated antigen‐fed mice show decreased IL‐4 production and induction of T follicular helper (Tfh) cells. Increased production of IL‐6 is observed in the CD11c+ cells isolated from the PPs of P‐Fag e 2‐fed mice.
Conclusion
These results indicate that attenuated allergens can suppress Th2‐induced allergic responses via induction of Tfh cells, which are regulated by IL‐6 secreted from dendritic cells.
Fag e 1 and Fag e 2 are major allergens in buckwheat. Phosphorylation of Fag e 1 and Fag e 2 result in reduced allergenicity owing to the masking effect of IgE‐binding epitopes. Mice fed phosphorylated‐Fag e 2 exhibit attenuated Th2‐mediated allergic reactions. Suppression of the allergic response is primarily due to induction of Tfh cells, which is regulated by IL‐6 secreted from dendritic cells.
We verified the possibility of tracing the geographical origin of durum wheat semolina used in pasta by examining the stable carbon, nitrogen, and oxygen isotope ratios (δ13C, δ15N, and δ18O) of ...wheat proteins. We determined the δ13C, δ15N, and δ18O values of the durum wheat semolina and pasta samples from Canada, Turkey, and Japan. The δ13C and δ15N values of the pasta made from Japanese durum wheat were lower than those of the other samples (p < 0.001 in both δ13C and δ15N). On the other hand, the δ18O values of the pasta made from Canadian durum wheat semolina were lower than those of the other samples (p < 0.001). These results show that stable isotope analysis is a potentially useful tool for tracing the geographical origin of durum wheat semolina in pasta. Furthermore, we examined an easier and more reasonable method of tracing the geographical origin of durum wheat semolina in pasta by using Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) of wheat protein fraction (glutenin fraction) extracted from pasta. SDS-PAGE of durum wheat semolina and pasta suggested that the manufacturing process of pasta had little influence on the proteins in the glutenin fraction extracted from pasta. Moreover, as a result of SDS-PAGE of durum wheat semolina and pasta made from Canadian, Turkish, and Japanese durum wheat semolina, each characteristic band was found in the glutenin fraction of Japanese samples (around 40 kD) and Turkish samples (around 110 kD). These results suggest that SDS-PAGE is also a potentially useful tool for tracing the geographical origin of durum wheat semolina in pasta.
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