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Pine nut allergy: Clinical features and major allergens characterization
Author(s) -
Cabanillas Beatriz,
Cheng Hsiaopo,
Grimm Casey C.,
Hurlburt Barry K.,
Rodríguez Julia,
Crespo Jesús F.,
Maleki Soheila J.
Publication year - 2012
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.201200245
Subject(s) - vicilin , nut , allergy , brazil nut , glutelin , albumin , allergen , digestion (alchemy) , medicine , food science , chemistry , immunology , storage protein , biochemistry , chromatography , gene , structural engineering , engineering
Scope The aims of this study were to evaluate I g E ‐mediated hypersensitivity to pine nut with details of clinical reactions and to characterize major pine nut allergens. Methods and results The study included ten consecutive teenagers and adults diagnosed with I g E ‐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. Conclusion 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.