Structure, Stability, and IgE Binding of the Peach Allergen Peamaclein (Pru p 7)
Tuppo, Lisa; Spadaccini, Roberta; Alessandri, Claudia; Wienk, Hans; Boelens, Rolf; Giangrieco, Ivana; Tamburrini, Maurizio; Mari, Adriano; Picone, Delia; Ciardiello, Maria Antonietta
(2014) Biopolymers, volume 102, issue 5, pp. 416 - 425
(Article)
Abstract
Knowledge of the structural properties of allergenic proteins is a necessary prerequisite to better understand the molecular bases of their action, and also to design targeted structural/functional modifications. Peamaclein is a recently identified 7 kDa peach allergen that has been associated with severe allergic reactions in sensitive subjects. This protein
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represents the first component of a new allergen family, which has no 3D structure available yet. Here, we report the first experimental data on the 3D-structure of Peamaclein. Almost 75% of the backbone resonances, including two helical stretches in the N-terminal region, and four out of six cysteine pairs have been assigned by 2D-NMR using a natural protein sample. Simulated gastrointestinal digestion experiments have highlighted that Peamaclein is even more resistant to digestion than the peach major allergen Pru p 3. Only the heat-denatured protein becomes sensitive to intestinal proteases. Similar to Pru p 3, Peamaclein keeps its native 3D-structure up to 90 degrees C, but it becomes unfolded at temperatures of 100-120 degrees C. Heat denaturation affects the immunological properties of both peach allergens, which lose at least partially their IgE-binding epitopes. In conclusion, the data collected in this study provide a first set of information on the molecular properties of Peamaclein. Future studies could lead to the possible use of the denatured form of this protein as a vaccine, and of the inclusion of cooked peach in the diet of subjects allergic to Peamaclein. (C) 2014 Wiley Periodicals, Inc.
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Keywords: Peamaclein, Pru p 7, NMR, simulated gastrointestinal digestion, heat stability, allergen, IgE binding, LIPID TRANSFER PROTEINS, NMR-SPECTROSCOPY, FOOD, EPITOPES, PRU-P-3, IDENTIFICATION, REACTIVITY, DIGESTION, FEATURES, FAMILY
ISSN: 0006-3525
Publisher: John Wiley and Sons Inc.
(Peer reviewed)
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