SENSITIZATION MECHANISM OF FOOD ALLERGY BY PATHOGENESIS-RELATED PROTEINS DERIVED FROM PLANT FOODSTUFFS

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Recently, the pathogenesis-related proteins (PR-P or known as defense proteins, DF) were shown to play an important role in food allergy. Structural similarity present in these proteins must be responsible for the potential of cross reactivity. It is of very interesting to investigate why the PR-P or DF induces IgE antibodies and elicits allergic manifestation. This study aimed to investigate the relationship between the structure or/and function and the ability to induce IgE production after sensitization.We tried to screen the proteins in the extract of various plant foodstuffs which was recognized by IgE antibodies in sera of the patients allergic to plant food stuffs. Several unique proteins were found in plant foods as IgE binding allergenic proteins, which were identified to be pathogenesis-related proteins,. such as 18kDa allergenic protein homologous to Bet v1 (Birch pollen allergen) from potato, 20kDa allergenic protein of cyclophilin from carrot, 45kDa allergenic protein as suberization-associated peroxidase from tomato, 37kDa allergenic protein as glutathione S-transferase, and 25kDa feredoxine/NADH oxidoreductase fro turnip, respectively. Last two allergenic proteins were shown to increase in turnip plants grown under a mild chemical stress (salicylic acid treatment), indicating that these proteins were the pathogenesis proteins and the allergenicity would be increase by a stress loading. In addition, the recombinant pathogenesis protein, PR-5d which has an insecticide activity and will be planed to transfer into potato, did not show the binding ability to patients IgE antibodies. Now we have constructing a allergen database to be used for allergen investigators.