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W2000272180 abstract "BACKGROUND: Ara h 2 purified from roasted peanut binds higher IgE levels than Ara h 2 purified from raw peanuts and in most cases roasted peanut extracts cause higher skin prick test (SPT) in patients and sensitized mice. METHODS: Circular dichroism (CD) spectroscopy was used to compare the secondary structure of Ara h 2 purified from raw and roasted peanuts. Immunoblot analysis was performed using serum from peanut allergic and sensitized patients to compare the IgE binding to different concentrations of Ara h 2 purified from raw and roasted peanuts, which were either native or denatured with a reducing agent. Unfolding of the proteins was monitored using CD spectroscopy. RESULTS: While the secondary structure of Ara h 2 purified from roasted peanuts did not show large changes in comparison to raw Ara h 2, the IgE binding to increased significantly with roasting. Unfolding the proteins demonstrated a reduction in IgE binding to both raw and roasted Ara h 2 indicating that structural epitopes are important for IgE binding to this allergen. CONCLUSIONS: These observations suggest that the chemical modifications incurred by roasting are more important for IgE binding than processing induced structural changes, and that structural epitopes are also major contributors to overall IgE binding to Ara h 2. Understanding the differences in IgE binding to various processed forms of foods by allergic versus sensitized patient sera may be useful in development of more specific diagnostic tools and potentially processes that can result in reduced allergenicity of a food." @default.
W2000272180 created "2016-06-24" @default.
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W2000272180 date "2010-02-01" @default.
W2000272180 modified "2023-09-27" @default.
W2000272180 title "The Role of Chemical Modifications And Structural Changes in IgE Binding By Ara h 2" @default.
W2000272180 doi "https://doi.org/10.1016/j.jaci.2009.12.881" @default.
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