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- W2080372885 abstract "RATIONALE: Ara h 1 is a major peanut allergen known to bind higher IgE following the roasting process. Here, we will examine the contribution of the structural and chemical modifications to alterations in IgE binding properties of Ara h 1. METHODS: Ara h 1 purified from raw and roasted peanuts and, heat denatured raw or dithiotheratol treated Ara h 1 were subjected IgE binding with sera from peanut allergic and sensitized individuals using spot blot analysis. Circular dichroism (CD) spectroscopy was used to monitor or confirm changes in the secondary structure between raw, roasted and denatured Ara h 1. RESULTS: The structures of Ara h 1 purified from raw and roasted are very similar with an alpha plus beta secondary structure, but differ significantly in IgE binding. Treatment of raw Ara h 1 with heat resulted in significant loss of alpha helices, while treatment with the reducing agent while notable, was not as significant. The structure of the heat denatured Ara h 1 shifts strongly toward a random coil/undordered structure. Majority of IgE in allergic and non allergic patients’ sera bound from highest to lowest to roasted, raw and denatured Ara h 1 (roasted > raw> denatured), respectively. CONCLUSION: In raw Ara h 1, the structural epitopes, particularly the ones located in the alpha helical sections, are more important to IgE binding than the liner epitopes. Meanwhile, enhanced IgE binding to roasted Ara h 1 is more likely to be due to chemical modifications than structural changes." @default.
- W2080372885 created "2016-06-24" @default.
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- W2080372885 date "2010-02-01" @default.
- W2080372885 modified "2023-09-25" @default.
- W2080372885 title "Differences In IgE Binding To Raw, Roasted And Denatured Ara h 1, A Major Peanut Allergen" @default.
- W2080372885 doi "https://doi.org/10.1016/j.jaci.2009.12.875" @default.
- W2080372885 hasPublicationYear "2010" @default.
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