| Project/Area Number |
09460063
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
食品科学・栄養科学
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| Research Institution | KYOTO UNIVERSITY (1998)
The University of Tokushima (1997) |
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Principal Investigator |
OGAWA Tadashi KYOTO UNIVERSITY,Research Instiute for Food Science ; Professor, 食糧科学研究所, 教授 (80027193)
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| Co-Investigator(Kenkyū-buntansha) |
KIMOTO Masumi Okayama Prefectural University ; Associated professor, 保健福祉学科, 助教授 (40108866)
MORIYAMA Tatusya KYOTO UNIVERSITY,Research Institute for Food Science ; Assistant Professor, 食糧科学研究所, 助手 (60239704)
山西 倫太郎 徳島大学, 医学部, 助手 (30253206)
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| Project Period (FY) |
1997 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥7,000,000 (Direct Cost: ¥7,000,000)
Fiscal Year 1998: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1997: ¥6,200,000 (Direct Cost: ¥6,200,000)
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| Keywords | plant foodstuffs / allergen / epitope / sugar moiety / glycoprotein / allergic patient / soybean / potato patatin / 共通抗原 / 糖鎖アレルゲン / IgE抗体産生誘導 / 大豆アレルゲン / ホースラデイッシュペルオキシダーゼ / パタチン / 植物性食品 / 食物アレルギー / イムノブロット / IgE抗体 |
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| Research Abstract |
Patients allergic to plant foodstuffs are known to increase yearly. We have investigated the allergenic proteins in plant foodstuffs using patient's sera and revealed that patient's IgE are cross-reactive among many homlogous proteins which are widely distributed in paint kingdom. Some of the IgE-binding proteins derived from different foodstuffs are glycoproteins and react with antibody raised against horse radish peroxidase (anti HRP). This antiHRP is known to recognize a asparagine-conjugated and high mannose type sugar moiety on peroxidase. The binding activity of patient's IgE against plant's allergens was reduced remarkedly by the pre-treatment of allergenic proteins with antiHRP, suggesting that the epitopes of these allergens are homologous and to be high mannose type sugar moieties. If these sugar moieties are common epitopes of plant allergens, patient's IgE antibodies could react with many homologous proteins which have similar sugar moiety in plant foodstuffs and patients present allergic symptons against many plants beyond there classification, such as species, genus, and families. We investigate one of the plant allergen which has asparagine-conjugated high mannose type sugar moiety, Gly m Bd 28K and potato's allergen, patatin. Both the allergenic proteins found to have a common epitope against patient's IgE antibodies. Furthermore, we revealed that many other plant proteins might share the common epitopes against patient's sera.
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