Pine nut allergy: Clinical features and major allergens characterization

July 28, 2017

Title

Pine nut allergy: Clinical features and major allergens characterization

Author

Beatriz Cabanillas, Hsiaopo Cheng, Casey C. Grimm, Barry K. Hurlburt, Julia Rodríguez, Jesús F. Crespo, Soheila J. Maleki

Year

2012

Journal

Molecular Nutrition & Food Research

Abstract

The aims of this study were to evaluate IgE-mediated hypersensitivity to pine nut with details of clinical reactions and to characterize major pine nut allergens. The study included ten consecutive teenagers and adults diagnosed with IgE-mediated clinical allergy to pine nut. Two major pine nut allergens were purified and identified and the secondary structures and susceptibility to digestion were characterized. Severe reactions represent 80% of allergic reactions to pine nut in this study. Moreover, 70% of the patients were monosensitized to this nut. Two major allergens with molecular weights of 6 and 50 kDa were purified and identified as albumin and vicilin, respectively. The 6 kDa protein (albumin), rich in α-helix content, was far more stable to peptic and tryptic digestion as compared with 50 kDa protein (vicilin), which was quickly broken down. The secondary structure of the purified 50 kDa protein showed 41% β-sheet, 5% α-helix, and 54% random coil and/or loops. Eighty percent of allergic reactions to pine nut in the ten patients included in this study were severe. Most patients (70%) were monosensitized to this nut. Two major allergens with molecular weights of 6 and 50 kDa were purified and identified as albumin and vicilin, respectively.

Instrument

J-815

Keywords

Circular dichroism, Secondary structure, Agricultural and environmental, Biochemistry, Food science, Antibodies