Detecting potential IgE-reactive sites on food proteins using a sequence and structure database, SDAP-food

Detecting potential IgE-reactive sites on food proteins using a sequence and structure database, SDAP-food
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DOI:
10.1021/jf034218r
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发表时间:
2003-07-30
影响因子:
6.1
通讯作者:
Schein, CH
Schein, CH
中科院分区:
农林科学1区
文献类型:
--
作者:
Ivanciuc, O;Mathura, V;Schein, CH

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食物过敏,包括口腔过敏综合征的高发病率,是引进新作物和食品时的主要考虑因素。开发了一个新的过敏蛋白结构数据库SDAP-Food,hftp://fermi.utmb.edu/SDAP/,以帮助预测新型食物蛋白的IgE结合潜力和已知过敏原之间的交叉反应性。该网站的目的是促进决策树方法的第一步,以确定一个给定的蛋白质的变应原性,基于序列和结构的相似性,以已知的过敏原及其IgE结合位点。然后可以使用免疫测试来确认预测。一个层次的程序,用于确定潜在的过敏原,使用基于物理特性的序列相似性指数,已被设计为识别类似于已知的IgE结合位点的区域。作为一个例子,SDAP工具被用于从山雪松花粉中发现与Jun α 3过敏原的IgE结合位点相似的食物过敏原序列。SDAP序列相似性搜索将Jun α 3表位与几种食物过敏原中的区域相匹配,包括樱桃(Pru α v 2)、苹果(Mal α d 2)和胡椒(Cap α 1),它们与Jun α 3一样是植物致病相关(PR-5)蛋白家族的成员。同源性建模,使用我们的EXDIS/DIAMOD/FANTOM程序套件,表明所有这些过敏原上的潜在表位区域的相似表面位置和结构。本文提出的定量方法可用作重组食品潜在过敏性筛选过程的一部分。
The high incidence of food allergies, including oral allergy syndrome, represent major considerations when introducing new crops and foods. A new structural database of allergenic proteins, SDAP-Food, hftp://fermi.utmb.edu/SDAP/, has been developed to aid in predicting the IgE-binding potential of novel food proteins and cross-reactivities among known allergens. The site is designed to facilitate the first steps of a decision tree approach to determine the allergenicity of a given protein, based on the sequence and structural similarity to known allergens and their IgE binding sites. Immunological tests can then be used to confirm the predictions. A hierarchical procedure for identifying potential allergens, using a physical property-based sequence similarity index, has been designed to identify regions that resemble known IgE binding sites. As an example, SDAP tools were used to find food allergen sequences similar to an IgE binding site of the Jun a 3 allergen from mountain cedar pollen. The SDAP sequence similarity search matched the Jun a 3 epitope to regions in several food allergens, including cherry (Pru av 2), apple (Mal d 2) and pepper (Cap a 1), which are, like Jun a 3, members of the plant pathogenesis-related (PR-5) protein family. Homology modeling, using our EXDIS/DIAMOD/FANTOM program suite, indicated a similar surface location and structure for the potential epitope region on all of these allergens. The quantitative approach presented here can be used as part of a screening process for potential allergenicity of recombinant food products.