Bente Janssen-Weets, Antoine Lesur, Gunnar Dittmar, François Bernardin, Eva Zahradnik, Monika Raulf, François Hentges, Carsten Bindslev-Jensen, Markus Ollert, Christiane Hilger
{"title":"马毛提取物的蛋白质组分析无法证明存在低过敏性卷毛马品种","authors":"Bente Janssen-Weets, Antoine Lesur, Gunnar Dittmar, François Bernardin, Eva Zahradnik, Monika Raulf, François Hentges, Carsten Bindslev-Jensen, Markus Ollert, Christiane Hilger","doi":"10.1002/clt2.12329","DOIUrl":null,"url":null,"abstract":"<div>\n \n \n <section>\n \n <h3> Background</h3>\n \n <p>The American Bashkir Curly Horse is frequently advertised to horse-allergic riders and claimed to be a so-called hypoallergenic breed that elicits fewer symptoms. Previous studies quantifying selected allergens in different breeds did not find a reduced allergen content in Curly Horses. Here, we provide a comprehensive proteomic analysis of horse hair extracts and a molecular analysis of the major allergen Equ c 1 with the aim of identifying differences in the Curly Horse breed that might explain their presumed reduced allergenic potential.</p>\n </section>\n \n <section>\n \n <h3> Methods</h3>\n \n <p>Horse hair extracts were prepared from Curly and American Quarter Horse breeds, separated by gender and castration status, extracts from other breeds served as controls. Extracts and native Equ c 1 (nEqu c 1) were analyzed by mass spectrometry. IgE-binding capacities of nEqu c 1 and its recombinant variants were tested by ELISA using sera of patients sensitized to horses. Structures and ligand binding abilities were analyzed by computational modeling and fluorescence quenching assays.</p>\n </section>\n \n <section>\n \n <h3> Results</h3>\n \n <p>All known respiratory horse allergens are present in hair extracts of Curly and Quarter Horses and share identical allergen-specific peptides. Lipocalin allergens are the most abundant proteins in horse hair extracts and contain several post-translational modifications. We identified two new variants of Equ c 1 that have similar IgE-binding capacities but show structural differences in their binding cavities and altered ligand binding behavior. There are no differences in IgE-binding of Equ c 1 derived from Curly Horses compared to other horse breeds.</p>\n </section>\n \n <section>\n \n <h3> Conclusion</h3>\n \n <p>Our data do not support the claim that Curly Horses are less allergenic than other breeds.</p>\n </section>\n </div>","PeriodicalId":10334,"journal":{"name":"Clinical and Translational Allergy","volume":null,"pages":null},"PeriodicalIF":4.6000,"publicationDate":"2024-01-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/clt2.12329","citationCount":"0","resultStr":"{\"title\":\"Proteomic analysis of horse hair extracts provides no evidence for the existence of a hypoallergenic Curly Horse breed\",\"authors\":\"Bente Janssen-Weets, Antoine Lesur, Gunnar Dittmar, François Bernardin, Eva Zahradnik, Monika Raulf, François Hentges, Carsten Bindslev-Jensen, Markus Ollert, Christiane Hilger\",\"doi\":\"10.1002/clt2.12329\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div>\\n \\n \\n <section>\\n \\n <h3> Background</h3>\\n \\n <p>The American Bashkir Curly Horse is frequently advertised to horse-allergic riders and claimed to be a so-called hypoallergenic breed that elicits fewer symptoms. Previous studies quantifying selected allergens in different breeds did not find a reduced allergen content in Curly Horses. Here, we provide a comprehensive proteomic analysis of horse hair extracts and a molecular analysis of the major allergen Equ c 1 with the aim of identifying differences in the Curly Horse breed that might explain their presumed reduced allergenic potential.</p>\\n </section>\\n \\n <section>\\n \\n <h3> Methods</h3>\\n \\n <p>Horse hair extracts were prepared from Curly and American Quarter Horse breeds, separated by gender and castration status, extracts from other breeds served as controls. Extracts and native Equ c 1 (nEqu c 1) were analyzed by mass spectrometry. IgE-binding capacities of nEqu c 1 and its recombinant variants were tested by ELISA using sera of patients sensitized to horses. Structures and ligand binding abilities were analyzed by computational modeling and fluorescence quenching assays.</p>\\n </section>\\n \\n <section>\\n \\n <h3> Results</h3>\\n \\n <p>All known respiratory horse allergens are present in hair extracts of Curly and Quarter Horses and share identical allergen-specific peptides. Lipocalin allergens are the most abundant proteins in horse hair extracts and contain several post-translational modifications. We identified two new variants of Equ c 1 that have similar IgE-binding capacities but show structural differences in their binding cavities and altered ligand binding behavior. There are no differences in IgE-binding of Equ c 1 derived from Curly Horses compared to other horse breeds.</p>\\n </section>\\n \\n <section>\\n \\n <h3> Conclusion</h3>\\n \\n <p>Our data do not support the claim that Curly Horses are less allergenic than other breeds.</p>\\n </section>\\n </div>\",\"PeriodicalId\":10334,\"journal\":{\"name\":\"Clinical and Translational Allergy\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":4.6000,\"publicationDate\":\"2024-01-29\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://onlinelibrary.wiley.com/doi/epdf/10.1002/clt2.12329\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Clinical and Translational Allergy\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1002/clt2.12329\",\"RegionNum\":2,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"ALLERGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Clinical and Translational Allergy","FirstCategoryId":"3","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/clt2.12329","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"ALLERGY","Score":null,"Total":0}
引用次数: 0
摘要
背景 美国巴什基尔卷毛马经常向对马匹过敏的骑手做广告,声称它是一种所谓的低过敏性品种,引起的症状较少。以前对不同品种的选定过敏原进行量化的研究并未发现卷毛马的过敏原含量有所降低。在此,我们对马毛提取物进行了全面的蛋白质组分析,并对主要过敏原 Equ c 1 进行了分子分析,目的是找出卷毛马品种的差异,以解释其过敏可能性降低的原因。 方法 从按性别和阉割状态区分的卷毛马和美国季马品种中提取马毛萃取物,其他品种的萃取物作为对照。提取物和原生 Equ c 1(nEqu c 1)通过质谱法进行分析。使用对马过敏的患者血清,通过 ELISA 方法检测了 nEqu c 1 及其重组变体的 IgE 结合能力。通过计算建模和荧光淬灭试验分析了其结构和配体结合能力。 结果 所有已知的呼吸道马过敏原都存在于卷毛马和四角马的毛发提取物中,并且具有相同的过敏原特异性肽。脂联素过敏原是马毛提取物中含量最高的蛋白质,包含多种翻译后修饰。我们发现了 Equ c 1 的两种新变体,它们具有相似的 IgE 结合能力,但在结合腔结构上存在差异,配体结合行为也有所改变。与其他马种相比,来自卷毛马的 Equ c 1 的 IgE 结合能力没有差异。 结论 我们的数据并不支持卷毛马过敏性低于其他马种的说法。
Proteomic analysis of horse hair extracts provides no evidence for the existence of a hypoallergenic Curly Horse breed
Background
The American Bashkir Curly Horse is frequently advertised to horse-allergic riders and claimed to be a so-called hypoallergenic breed that elicits fewer symptoms. Previous studies quantifying selected allergens in different breeds did not find a reduced allergen content in Curly Horses. Here, we provide a comprehensive proteomic analysis of horse hair extracts and a molecular analysis of the major allergen Equ c 1 with the aim of identifying differences in the Curly Horse breed that might explain their presumed reduced allergenic potential.
Methods
Horse hair extracts were prepared from Curly and American Quarter Horse breeds, separated by gender and castration status, extracts from other breeds served as controls. Extracts and native Equ c 1 (nEqu c 1) were analyzed by mass spectrometry. IgE-binding capacities of nEqu c 1 and its recombinant variants were tested by ELISA using sera of patients sensitized to horses. Structures and ligand binding abilities were analyzed by computational modeling and fluorescence quenching assays.
Results
All known respiratory horse allergens are present in hair extracts of Curly and Quarter Horses and share identical allergen-specific peptides. Lipocalin allergens are the most abundant proteins in horse hair extracts and contain several post-translational modifications. We identified two new variants of Equ c 1 that have similar IgE-binding capacities but show structural differences in their binding cavities and altered ligand binding behavior. There are no differences in IgE-binding of Equ c 1 derived from Curly Horses compared to other horse breeds.
Conclusion
Our data do not support the claim that Curly Horses are less allergenic than other breeds.
期刊介绍:
Clinical and Translational Allergy, one of several journals in the portfolio of the European Academy of Allergy and Clinical Immunology, provides a platform for the dissemination of allergy research and reviews, as well as EAACI position papers, task force reports and guidelines, amongst an international scientific audience.
Clinical and Translational Allergy accepts clinical and translational research in the following areas and other related topics: asthma, rhinitis, rhinosinusitis, drug hypersensitivity, allergic conjunctivitis, allergic skin diseases, atopic eczema, urticaria, angioedema, venom hypersensitivity, anaphylaxis, food allergy, immunotherapy, immune modulators and biologics, animal models of allergic disease, immune mechanisms, or any other topic related to allergic disease.