| Project/Area Number |
15580112
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Food science
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| Research Institution | Okayama Prefectural University |
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Principal Investigator |
TSUJI Hideaki Okayama Prefectural University, Faculty of Health and Welfare Science, Department of Nutritional Science, Professor, 保健福祉学部, 教授 (20093875)
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| Co-Investigator(Kenkyū-buntansha) |
KIMOTO Masumi Okayama Prefectural University, Faculty of Health and Welfare Science, Department of Nutritional Science, Professor, 保健福祉学部, 教授 (40108866)
HIEMORI Miki Okayama Prefectural University, Faculty of Health and Welfare Science, Department of Nutritional Science, Assistant, 保健福祉学部, 助手 (80326412)
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| Project Period (FY) |
2003 – 2005
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| Project Status |
Completed (Fiscal Year 2005)
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| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2005: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 2004: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2003: ¥1,800,000 (Direct Cost: ¥1,800,000)
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| Keywords | Wheat allergen / Tri a Bd 27K / Tri a Bd 17K / Sugar chain / Allergenicity / Common antigen / Tri a Bd17K / Tri a Bd 36K / common epitope |
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| Research Abstract |
Many plant allergens have been found, and show more complex phase concerning their allergen investigation field. Crossreaction between the allergens have been very often observed. Therefore, the complex phase would be unified by the idea entitle "a common epitope". Asn-containing epitopes on the allergens is considering as one of common antigens.
We have elucidated the sugar moiety of soybean major allergen, Gly m Bd 28K and wheat major allergen Tri a Bd 17K.
In the present study, the properties of Tria Bd 27K, a major allergen, in wheat, has been investigated in details. First of all, monoclonal antibodies against the allergen have been producwed. The allergen in wheat was separated by two-dimensional electrophoresis with isoelectric electrophoresis and SDS-PAGE, and the proteins on the gel were detected by immnoblotting with the above-mentioned antibodies. Several spots showing the positive response for the antibodies were observed. The regions on the gel corresponding to the positive spots were cut out and subjected to N-terminal amino acid sequenceing. The proteins on the regions were shown to belong to the Tri a Bd 27k. This finding means that Tri a Bd 27K occur as polyforms. The above-mentioned spots reacted with a lectin, sensitive to fukose residue and the sera of patients positive to wheat. Furthermore, the Tri a Bd 27K sensitive to the lectin were cut out and subjected to sugar analyses. Subsequently, mannose, N-acetylglucosamin were detected, and the occurrence of galactose and fukose and xylose were alsoshowed. Interestingly, a recombinant Tri a Bd 27K expressed in Eschericia coli was not shown to be insetive to the sera of patients with wheat allergy.
The present findings demonstrate that most of IgE antibodies in the sera of the above patients, which were sensitive to the allergen, bind to the sugar moiety of the allergen.
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