Abstract
Ara h 2 is a relevant peanut allergen linked to severe allergic reactions. The interaction of Ara h 2 with components of the sensitization phase of food allergy (e.g., dendritic cells) has not been investigated, and could be key to understanding the allergenic potential of this allergen. In this study, we aimed to analyze such interactions and the possible mechanism involved. Ara h 2 was purified from two forms of peanut, raw and roasted, and labeled with a fluorescent dye. Human monocyte-derived dendritic cells (MDDCs) were obtained, and experiments of Ara h 2 internalization by MDDCs were carried out. The role of the mannose receptor in the internalization of Ara h 2 from raw and roasted peanuts was also investigated. Results showed that Ara h 2 internalization by MDDCs was both time and dose dependent. Mannose receptors in MDDCs had a greater implication in the internalization of Ara h 2 from roasted peanuts. However, this receptor was also important in the internalization of Ara h 2 from raw peanuts, as opposed to other allergens such as raw Ara h 3.
Highlights
Peanut allergy is a relevant health issue in many areas of the world [1,2]
In order to study the differences in the uptake and internalization of Ara h 2 from raw and roasted peanuts by monocyte-derived dendritic cells (MDDCs), Ara h 2 was purified from both forms of peanut and labeled with a fluorescent dye
Mannan strongly contributed to the the internalization of raw-Ara h 2 and roast-Ara h 2 when the allergens were incubated with MDDCs decrease in the internalization of both allergens by MDDCs at thetotime of 120 min,internalization that decrease for 120 min
Summary
Peanut allergy is a relevant health issue in many areas of the world [1,2]. Among the allergenic components of peanut, Ara h 2 has been described as a potent allergen. Ara h 2 can be modified by thermal treatments in several ways. Some treatments such as boiling are able to potentiate the transfer of Ara h 2 and other related allergens like Ara h 6 and Ara h 7 from the kernel to the cooking water, partially reducing the specific allergenic content of peanuts kernels boiled under specific conditions [6,7,8]. Ara h 2 purified from roasted peanuts was found to have higher IgE-binding properties than Ara h 2 purified from the raw form. In addition to the increase in the allergenic potential of peanut, it has been observed that roasting enhances the trypsin inhibitor activity of Ara h 2 [12]. The chemical reactions that occur in peanuts during roasting, such as
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