In vitro assessment of allergenicity features and localization of probable IgE binding regions

Rice is cultivated as a staple grain crop in many countries, especially in Asia. In the present study, recombinant rice chitinase was expressed, purified and characterized by in silico and immunobiochemical methods. Rice chitinase was affinity purified and it resolved at 24 kDa on SDS-PAGE. Purified protein was analyzed for pepsin resistance, heat stability, and IgE binding using atopic patients' sera. Chitinase was resistant to pepsin digestion and heat treatment at 90 °C for 1 h. It showed significant IgE binding with 7 of 110 patients' sera positive to different food allergens. Homology modeled 3D structure of rice chitinase was used for B cell epitope prediction. In silico predicted B cell peptides were assessed for IgE binding by ELISA using food allergic patients' sera, epitope RC2 showed IgE binding comparable to chitinase. In conclusion, chitinase was identified as a potential allergen and may share cross reactive epitopes with food allergens.