دورية أكاديمية
Proteomic analysis of horse hair extracts provides no evidence for the existence of a hypoallergenic Curly Horse breed
| العنوان: | Proteomic analysis of horse hair extracts provides no evidence for the existence of a hypoallergenic Curly Horse breed |
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| المؤلفون: | Janssen-Weets, Bente, Lesur, Antoine, Dittmar, Gunnar, Bernardin, François, Zahradnik, Eva, Raulf, Monika, Hentges, François, Bindslev-Jensen, Carsten, Ollert, Markus, Hilger, Christiane |
| المصدر: | Janssen-Weets , B , Lesur , A , Dittmar , G , Bernardin , F , Zahradnik , E , Raulf , M , Hentges , F , Bindslev-Jensen , C , Ollert , M & Hilger , C 2024 , ' Proteomic analysis of horse hair extracts provides no evidence for the existence of a hypoallergenic Curly Horse breed ' , Clinical and Translational Allergy , vol. 14 , no. 2 , e12329 . https://doi.org/10.1002/clt2.12329Test |
| سنة النشر: | 2024 |
| المجموعة: | University of Southern Denmark: Research Output / Syddansk Universitet |
| مصطلحات موضوعية: | American Bashkir Curly Horse, Equ c 1, horse allergens, horse proteome, hypoallergenic breeds |
| الوصف: | 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. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| العلاقة: | https://portal.findresearcher.sdu.dk/da/publications/719e84c8-7ba2-4ca4-8acc-d23469d723ccTest |
| DOI: | 10.1002/clt2.12329 |
| الإتاحة: | https://doi.org/10.1002/clt2.12329Test https://portal.findresearcher.sdu.dk/da/publications/719e84c8-7ba2-4ca4-8acc-d23469d723ccTest https://findresearcher.sdu.dk/ws/files/255354967/Clinical_Translational_All_-_2024_-_Janssen_Weets_-_Proteomic_analysis_of_horse_hair_extracts_provides_no_evidence_for.pdfTest |
| حقوق: | info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsbas.1030AF20 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1002/clt2.12329 |
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