Changes in Serum Protein–Peptide Patterns in Atopic Children Allergic to Plant Storage Proteins

Abstract

Next to cow’s milk and eggs, plant foods, i.e., legumes, tree nuts and cereal grains, most often sensitise atopic children. Storage proteins constitutes the most relevant protein fraction of plant foods, causing primary sensitisation. They exhibit strong allergenic properties and immunogenicity. Our goal was to analyse sensitisation to 26 plant storage proteins in a group of 76 children aged 0–5 years with chronic symptoms of atopic dermatitis using Allergy Explorer ALEX2 and to discover changes in serum protein–peptide patterns in allergic patients with the use of MALDI-TOF-MS. We reported that 25% of children were allergic to 2S albumins, 19.7% to 7S globulins, 13.2% to 11S globulins and 1.3% to cereal prolamins. The most common allergenic molecules were Ara h 1 (18.4%), Ara h 2 (17.1%), Ara h 6 (15.8%) and Ara h 3 (11.8%) from peanuts, and the mean serum sIgE concentrations in allergic patients were 10.93 kUA/L, 15.353 kUA/L, 15.359 kUA/L and 9.038 kUA/L, respectively. In children allergic to storage proteins compared to the other patients (both allergic and non-allergic), the cell cycle control protein 50A, testis-expressed sequence 13B, DENN domain-containing protein 5A and SKI family transcriptional corepressor 2 were altered. Our results indicate that the IgE-mediated allergy to storage proteins is a huge problem in a group of young, atopic children, and show the potential of proteomic analysis in the prediction of primary sensitisation to plant foods. It is the next crucial step for understanding the molecular consequences of allergy to storage proteins.

Identification, Characterization, Cloning, and Cross-Reactivity of Zan b 2, a Novel Pepper Allergen of 11S Legumin

“…Many members of the seed storage proteins were identified as allergens . 11S legumin is an important allergen in this family, and approximately 13.2% of atopic children were allergic to 11S globulins . The 11S legumin is usually a hexameric protein composed of six monomeric subunits (around 50–60 kDa) with a hydrophobic signal peptide that was removed post-translationally.…”

“…6 11S legumin is an important allergen in this family, and approximately 13.2% of atopic children were allergic to 11S globulins. 7 The 11S legumin is usually a hexameric protein composed of six monomeric subunits (around 50−60 kDa) with a hydrophobic signal peptide that was removed post-translationally. Each monomer is formed by a disulfide bond between an acidic (∼30−40 kDa) and an alkaline (∼20−30 kDa) subunit.…”