1. Epitope mapping of the major allergen 2S albumin from pine nut.
- Author
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Crespo JF, Bueno C, Villalba M, Monaci L, Cuadrado C, Novak N, and Cabanillas B
- Subjects
- 2S Albumins, Plant immunology, 2S Albumins, Plant metabolism, Adolescent, Adult, Allergens immunology, Amino Acid Sequence, Arachis immunology, Arachis metabolism, Epitopes immunology, Female, Humans, Immunoglobulin E blood, Immunoglobulin E immunology, Male, Nut Hypersensitivity immunology, Nut Hypersensitivity pathology, Nuts immunology, Nuts metabolism, Peptide Library, Pinus immunology, 2S Albumins, Plant chemistry, Allergens chemistry, Epitope Mapping methods, Epitopes chemistry, Pinus metabolism
- Abstract
The epitopes of the major allergen of pine nut, Pin p 1, were analyzed using a peptide library and sera from patients with clinical allergy to pine nut in order to deepen into the allergenic characteristics of Pin p 1. Analyses of epitope similarities and epitopes location in a 3D-model were also performed. Results showed that three main regions of Pin p 1 containing 5 epitopes were recognized by patient sera IgE. The epitopes of Pin p 1 had important similarities with epitopes of allergenic 2S albumins from peanut (Ara h 2 and 6) and Brazil nut (Ber e 1). The epitopes of Pin p 1 were found in α-helices and coils in the 3D protein structure. Interestingly, all epitopes were found to be well-exposed in the protein surface, which suggests facile access for IgE-binding to the structure of Pin p 1 which is known to be highly resistant., (Copyright © 2020 Elsevier Ltd. All rights reserved.)
- Published
- 2021
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