Two new variants of the lipocalin allergen Bos d 2 |
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Authors: | Jaakko Rautiainen Seppo Auriola Anita Konttinen Tuomas Virtanen Marja Rytknen-Nissinen Thomas Zeiler Rauno Mntyjrvi |
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Institution: | Jaakko Rautiainen, Seppo Auriola, Anita Konttinen, Tuomas Virtanen, Marja Rytkönen-Nissinen, Thomas Zeiler,Rauno Mäntyjärvi |
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Abstract: | 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. |
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Keywords: | Lipocalins Allergen |
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