脂钙素过敏原bod2的两种新变体

Jaakko Rautiainen , Seppo Auriola , Anita Konttinen , Tuomas Virtanen , Marja Rytkönen-Nissinen , Thomas Zeiler , Rauno Mäntyjärvi
{"title":"脂钙素过敏原bod2的两种新变体","authors":"Jaakko Rautiainen ,&nbsp;Seppo Auriola ,&nbsp;Anita Konttinen ,&nbsp;Tuomas Virtanen ,&nbsp;Marja Rytkönen-Nissinen ,&nbsp;Thomas Zeiler ,&nbsp;Rauno Mäntyjärvi","doi":"10.1016/S0378-4347(01)00369-3","DOIUrl":null,"url":null,"abstract":"<div><p>Allergens from various sources have been shown to comprise several isoforms. In the present study, a series of chromatographic steps was carried out to separate the lipocalin allergen Bos d 2 isoforms present in cow dander. Subsequent HPLC-MS–MS analyses revealed two new Bos d 2 variants. In one of the proteins, tyrosine (Y83) was substituted by aspartic acid, and in the other protein valine (V102) was replaced by alanine. We propose the three Bos d 2 variants be named as Bos d 2.0101 (previously sequenced Bos d 2), Bos d 2.0102 and Bos d 2.0103. Our results suggest that molecular polymorphism is a common property among lipocalin allergens. Since allergen isoforms may show variation in their IgE binding and/or T-cell reactivity, all of the many allergen forms should be taken into account when planning preparations for immunotherapy.</p></div>","PeriodicalId":15463,"journal":{"name":"Journal of Chromatography B: Biomedical Sciences and Applications","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2001-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0378-4347(01)00369-3","citationCount":"10","resultStr":"{\"title\":\"Two new variants of the lipocalin allergen Bos d 2\",\"authors\":\"Jaakko Rautiainen ,&nbsp;Seppo Auriola ,&nbsp;Anita Konttinen ,&nbsp;Tuomas Virtanen ,&nbsp;Marja Rytkönen-Nissinen ,&nbsp;Thomas Zeiler ,&nbsp;Rauno Mäntyjärvi\",\"doi\":\"10.1016/S0378-4347(01)00369-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Allergens from various sources have been shown to comprise several isoforms. In the present study, a series of chromatographic steps was carried out to separate the lipocalin allergen Bos d 2 isoforms present in cow dander. Subsequent HPLC-MS–MS analyses revealed two new Bos d 2 variants. In one of the proteins, tyrosine (Y83) was substituted by aspartic acid, and in the other protein valine (V102) was replaced by alanine. We propose the three Bos d 2 variants be named as Bos d 2.0101 (previously sequenced Bos d 2), Bos d 2.0102 and Bos d 2.0103. Our results suggest that molecular polymorphism is a common property among lipocalin allergens. Since allergen isoforms may show variation in their IgE binding and/or T-cell reactivity, all of the many allergen forms should be taken into account when planning preparations for immunotherapy.</p></div>\",\"PeriodicalId\":15463,\"journal\":{\"name\":\"Journal of Chromatography B: Biomedical Sciences and Applications\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2001-11-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0378-4347(01)00369-3\",\"citationCount\":\"10\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Chromatography B: Biomedical Sciences and Applications\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0378434701003693\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Chromatography B: Biomedical Sciences and Applications","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0378434701003693","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 10

摘要

来自不同来源的过敏原已被证明包含几种同种异构体。在本研究中,进行了一系列的色谱步骤来分离存在于牛皮屑中的脂钙素过敏原bo_2异构体。随后的HPLC-MS-MS分析揭示了两个新的bods2变体。其中一种蛋白质的酪氨酸(Y83)被天冬氨酸取代,另一种蛋白质的缬氨酸(V102)被丙氨酸取代。我们建议将这三个bod 2变体命名为bod 2.0101(先前测序的bod 2)、bod 2.0102和bod 2.0103。我们的研究结果表明,分子多态性是脂钙素过敏原的一个共同特性。由于过敏原同种异构体在IgE结合和/或t细胞反应性方面可能表现出差异,因此在计划免疫治疗的准备工作时,应考虑所有多种过敏原形式。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Two new variants of the lipocalin allergen Bos d 2

Allergens from various sources have been shown to comprise several isoforms. In the present study, a series of chromatographic steps was carried out to separate the lipocalin allergen Bos d 2 isoforms present in cow dander. Subsequent HPLC-MS–MS analyses revealed two new Bos d 2 variants. In one of the proteins, tyrosine (Y83) was substituted by aspartic acid, and in the other protein valine (V102) was replaced by alanine. We propose the three Bos d 2 variants be named as Bos d 2.0101 (previously sequenced Bos d 2), Bos d 2.0102 and Bos d 2.0103. Our results suggest that molecular polymorphism is a common property among lipocalin allergens. Since allergen isoforms may show variation in their IgE binding and/or T-cell reactivity, all of the many allergen forms should be taken into account when planning preparations for immunotherapy.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信