Molecular characterization of the IgE-binding epitopes in the fast ω-gliadins of Triticeae in relation to wheat-dependent, exercise-induced anaphylaxis
Molecular characterization of the IgE-binding epitopes in the fast ω-gliadins of Triticeae in relation to wheat-dependent, exercise-induced anaphylaxis
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DOI：
10.1016/j.gene.2016.06.040
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发表时间：
2016-10-10
期刊：
影响因子：
3.5
通讯作者：
Kong, Lingrang
中科院分区：
文献类型：
--
作者：
Du, Xuye;Tang, Heng;Kong, Lingrang
快速ω-醇溶蛋白是小麦贮藏蛋白的次要组分，但却是引发小麦过敏的主要抗原。利用PCR技术从小麦及其近缘种中克隆了66个具有独特特性的新的全长快速ω-醇溶蛋白基因。它们的编码区长度为177 ~ 987 bp，编码4.28 ~ 37.56 kDa的蛋白质。根据N-末端前3个氨基酸的序列，将这些基因分为SRL-、TRQ-、GRL-、NRL-、SRP-和SRM-型6个亚类。通过多重比对发现，这些基因之间存在显著差异，这是由于重复结构域的插入或缺失所致。对66个快速ω-醇溶蛋白的IgE结合表位分析表明，它们含有0-24个IgE结合表位。系统发育树显示，快、慢ω-醇溶蛋白可分为两大类，其分化时间为2164万年前。快速ω-醇溶蛋白基因的序列数据有助于研究不同类型ω-醇溶蛋白的起源和进化，同时也为合成单克隆抗体检测小麦抗原含量提供了基础。(C)© 2016 Elsevier B. V.版权所有。
Fast omega-gliadins were minor components of wheat storage proteins but a major antigen triggering allergy to wheat. Sixty-six novel full-length fast omega-gliadin genes with unique characteristics were cloned and sequenced from wheat and its relative species using a PCR-based strategy. Their coding regions ranged from 177 bp to 987 bp in length and encoded 4.28 kDa to 37.56 kDa proteins. On the base of first three deduced amino acids at the N-terminal, these genes could be classified into the six subclasses of SRL-, TRQ-, GRL-, NRL-, SRP- and SRM-type omega-gliadin genes. Compared by multiple alignments, these genes were significantly different from each other, due to the insertion or deletion at the repetitive domain. An analysis of the IgE-binding epitopes of the 66 deduced fast omega-gliadins demonstrated that they contained 0-24 IgE-binding epitopes. The phylogenetic tree demonstrated that the fast omega-gliadins and slow omega-gliadins were separated into two groups and their divergence time was 21.64 million years ago. Sequence data of the fast omega-gliadin genes assist in the study of the origins and evolutions of the different types of omega-gliadins while also providing a basis for the synthesis of monoclonal antibodies to detect wheat antigen content. (C) 2016 Elsevier B.V. All rights reserved.