Project/Area Number |
12460059
|
Research Category |
Grant-in-Aid for Scientific Research (B)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
食品科学・栄養科学
|
Research Institution | Kyoto University |
Principal Investigator |
OGAWA Tadashi Graduate School of Agriculture Professor, 大学院・農学研究科, 教授 (80027193)
|
Co-Investigator(Kenkyū-buntansha) |
AIBARA Shigeo Graduate School of Agriculture Associated Professor, 大学院・農学研究科, 助教授 (20027197)
MORIYAMA Tatsuya Graduate School of Agriculture Assistant Professor, 大学院・農学研究科, 助手 (60239704)
SATO Humihiko Graduate School of Life Science Professor, 大学院・生命科学研究科, 教授 (10127087)
|
Project Period (FY) |
2000 – 2002
|
Project Status |
Completed (Fiscal Year 2002)
|
Budget Amount *help |
¥9,200,000 (Direct Cost: ¥9,200,000)
Fiscal Year 2002: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 2001: ¥2,600,000 (Direct Cost: ¥2,600,000)
Fiscal Year 2000: ¥5,500,000 (Direct Cost: ¥5,500,000)
|
Keywords | food allergy / allergen / pathogenesis-related protein / sensitization / IgE antibody / immunoblot / allergen database / 食品素材 / 食品アレルギー / 食品アレルゲン / 植物タンパク質 / アレルゲン性 / グリシニン / グルタチオン依存性アスコルビン酸還元酵素 / ニンジン / シクロフィリン / シクロスポリンA / Bet v7 |
Research Abstract |
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.
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