Relevance of IgE binding to short peptides for the allergenic activity of food allergens
Relevance of IgE binding to short peptides for the allergenic activity of food allergens
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DOI：
10.1016/j.jaci.2009.05.031
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发表时间：
2009-08-01
影响因子：
14.2
通讯作者：
Vieths, Stefan
中科院分区：
文献类型：
--
作者：
Albrecht, Melanie;Kuehne, Yvonne;Vieths, Stefan
背景：分析IgE抗体与表位的结合为食物过敏诊断和管理以及低变应原候选疫苗的构建提供了信息，但序列表位对功能相关的IgE结合的贡献尚不完全清楚。目的：我们试图研究文献中描述的主要序列表位对2种食物过敏原IgE结合能力的影响。用酶联免疫吸附试验和介体释放试验评价代表已鉴定序列的合成可溶性多肽抑制IgE与亲本变应原结合的能力。对未折叠的重组(R)arah2的IgE结合能力进行了分析。结果：虽然检测到代表变应原序列片段的IgE结合肽，但在ELISA法和嗜碱性粒细胞活化试验中未观察到相关的抑制亲本变应原结合的能力。与折叠RARA h2相比，去折叠RARA h2的IgE结合能力降低，且不能诱导介质释放。在免疫CAP分析中，杂交原肌球蛋白与IgE的结合比RPEN A 1少，并显示出边际抑制能力。结论：作为PEN A 1和Ara h 2主要序列表位的多肽对所研究的过敏原的IgE结合贡献很小。(《过敏与免疫杂志》2009；124：328-36。)
Background: Analysis of IgE antibody binding to epitopes provides information for food allergy diagnosis and management and construction of hypoallergenic candidate vaccines, but the contribution of sequential epitopes to functionally relevant IgE binding is not fully understood.Objectives: We sought to study the impact of IgE-binding peptides described as major sequence epitopes in the literature on IgE-binding capacity of 2 selected food allergens.Methods: IgE-binding peptides of the food allergens Ara h 2 (peanut) and Pen a 1 (shrimp) were identified. Synthetic soluble peptides representing the identified sequences were assessed for their capacity to inhibit IgE binding to the parent allergens by means of ELISA and in mediator release assay. The IgE-binding capacity of unfolded recombinant (r) Ara h 2 was analyzed. A hybrid tropomyosin carrying the IgE-binding regions of Pen a 1 grafted into the structural context of the nonallergenic mouse tropornyosin was applied in ELISA inhibition experiments and ImmunoCAP analysis.Results: Although IgE-binding peptides representing sections of the allergen sequences were detected, no relevant capacity to inhibit the IgE binding to the parent allergen in ELISA or basophil activation test was observed. Unfolded rAra h 2 showed reduced IgE-binding capacity compared with folded rAra h 2 and failed to elicit mediator release. Hybrid tropomyosin bound less IgE than rPen a 1 in ImmunoCAP analysis and revealed marginal inhibitory capacity.Conclusion: Peptides identified as major sequence epitopes on Pen a 1 and Ara h 2 show little contribution to the IgE binding of the allergens studied. (J Allergy Clin Immunol 2009;124: 328-36.)