Epitope mapping of the major allergen 2S albumin from pine nut

Food Chem. 2021 Mar 1:339:127895. doi: 10.1016/j.foodchem.2020.127895. Epub 2020 Aug 19.

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.

Keywords: Food allergy; IgE; Pin p 1; Pinus pinea L; Protein; Tree nut.

MeSH terms

  • 2S Albumins, Plant / chemistry*
  • 2S Albumins, Plant / immunology
  • 2S Albumins, Plant / metabolism
  • Adolescent
  • Adult
  • Allergens / chemistry*
  • Allergens / immunology
  • Amino Acid Sequence
  • Arachis / immunology
  • Arachis / metabolism
  • Epitope Mapping / methods*
  • Epitopes / chemistry*
  • 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
  • Pinus / metabolism*

Substances

  • 2S Albumins, Plant
  • Allergens
  • Epitopes
  • Peptide Library
  • Immunoglobulin E