Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3
Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3
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DOI：
10.1159/000053642
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发表时间：
2000-12-01
影响因子：
2.8
通讯作者：
Markwell, JP
中科院分区：
文献类型：
--
作者：
Beardslee, TA;Zeece, MG;Markwell, JP
背景：蛋白质 IgE 表位的鉴定是了解过敏原与免疫系统相互作用的第一步。来自豆科植物的蛋白质在 IgE 结合测定中显示出体外交叉反应性，但这种交叉反应性很少具有临床意义。解决这一差异需要豆类家族蛋白过敏原的 IgE 表位图谱。方法：我们构建了代表大豆甘氨酸 G1 酸性链重叠区域的 6 个融合蛋白，这些融合蛋白用于免疫印迹和新型夹心 ELISA，其中使用大豆过敏个体的混合血清来揭示共同的 IgE 结合区域。该区域是使用重叠合成肽进行 IgE 表位作图的重点。结果：融合蛋白实验的数据揭示了由残基 F192-1265 组成的 IgE 结合区。对该区域的重叠合成肽的分析表明，大豆球蛋白G1酸性链的IgE表位由残基G217-V235和G253-1265组成。为甘氨酸 G1 酸性链鉴定的表位与先前为花生过敏原 Ara h 3 鉴定的 IgE 表位同源[1]，然而，通过丙氨酸扫描鉴定的花生表位中对 IgE 结合重要的残基与天然大豆表位不同。结论：针对大豆球蛋白 G1 酸性链鉴定的 IgE 表位显然代表了几种豆科植物种子储存蛋白的过敏原区域。我们的研究结果表明，IgE 表位的鉴定和豆类家族蛋白的结构分析将为食物过敏的研究提供有价值的信息。版权所有 (C) 2000 S. Karger AG，巴塞尔。
Background: The identification of IgE epitopes for proteins is the first step in understanding the interaction of allergens with the immune system. Proteins from the legume family have shown in vitro cross-reactivity in IgE-binding assays, but this cross-reactivity is rarely clinically significant. Resolution of this discrepancy requires IgE epitope mapping of legume family protein allergens. Methods: We constructed six fusion proteins representing overlapping regions of soybean glycinin G1 acidic chain, These fusion proteins were used in immunoblotting and a novel sandwich ELISA with pooled sera from soy-allergic individuals to reveal a common IgE-binding region, This region was the focus for IgE epitope mapping using overlapping synthetic peptides. Results: Data from the fusion protein experiments revealed an IgE-binding region consisting of residues F192-1265. Analysis of the overlapping synthetic peptides to this region indicated that IgE epitopes to glycinin G1 acidic chain consist of residues G217-V235 and G253-1265. The epitopes identified for glycinin G1 acidic chain are homologous to IgE epitopes previously identified for the peanut allergen Ara h 3 [1], However, residues identified by alanine scanning in the peanut epitopes as being important for IgE binding are different in the natural soybean epitopes. Conclusions: The IgE epitopes identified for glycinin G1 acidic chain apparently represent an allergenic region of several legume family seed storage proteins. Our findings indicate that the identification of IgE epitopes and structural analysis of legume family proteins will provide valuable information to the study of food allergies. Copyright (C) 2000 S. Karger AG, Basel.