Mapping and mutational analysis of the IgE-binding epitopes on Ara h 1, a legume vicilin protein and a major allergen in peanut hypersensitivity
Mapping and mutational analysis of the IgE-binding epitopes on Ara h 1, a legume vicilin protein and a major allergen in peanut hypersensitivity
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DOI：
10.1111/j.1432-1033.1997.t01-1-00334.x
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发表时间：
1997-04-15
期刊：
影响因子：
--
通讯作者：
Bannon, GA
中科院分区：
文献类型：
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作者：
Burks, AW;Shin, D;Bannon, GA
花生过敏是一个重大的健康问题，因为过敏反应的普遍性和潜在严重性。利用有记录的花生超敏反应患者的血清IgE和重叠肽来鉴定主要花生过敏原Ara h 1上的IgE结合表位。在Ara h 1蛋白的整个长度上鉴定出至少23种不同的线性IgE结合表位。所有表位的长度为6 - 10个氨基酸，但所有肽段之间没有明显的共有序列基序。其中四种肽似乎是免疫显性IgE结合表位，因为它们被超过80%的受试患者的血清识别，并且比其他任何Ara h 1表位结合更多的IgE。对免疫显性表位的突变分析表明，这些肽内的单个氨基酸变化对IgE结合特性有显著影响。对Ara h 1蛋白上表位核心氨基酸的IgE结合能力的鉴定和测定，将使我们有可能具体探讨花生超敏反应以及一般食物超敏反应的病理生理和免疫机制。
Peanut allergy is a significant health problem because of the prevelance and potential severity of the allergic reaction. Serum IgE from patients with documented peanut hypersensitivity reactions and overlapping peptides were used to identify the IgE-binding epitopes on the major peanut allergen, Are h 1. At least twenty-three different linear IgE-binding epitopes, located throughout the length of the Ara h 1 protein, were identified. All of the epitopes were 6-10 amino acids in length, but there was no obvious sequence motif shared by all peptides. Four of the peptides appeared to be immunodominant IgE-binding epitopes in that they were recognized by serum from more than 80% of the patients tested and bound more IgE than any of the other Ara h 1 epitopes. Mutational analysis of the immunodominant epitopes revealed that single amino acid changes within these peptides had dramatic effects on IgE-binding characteristics. The identification and determination of the IgE-binding capabilities of core amino acids in epitopes on the Ara h 1 protein will make it possible to address the pathophysiologic and immunologic mechanisms regarding peanut hypersensitivity reactions specifically and food hypersensitivity in general.