Common food allergens and their IgE-binding epitopes

Abstract

Food allergy is an adverse immune response to certain kinds of food. Although any food can cause allergic reactions, chicken egg, cow's milk, wheat, shellfish, fruit, and buckwheat account for 75% of food allergies in Japan. Allergen-specific immunoglobulin E (IgE) antibodies play a pivotal role in the development of food allergy. Recent advances in molecular biological techniques have enabled the efficient analysis of food allergens. As a result, many food allergens have been identified, and their molecular structure and IgE-binding epitopes have also been identified. Studies of allergens have demonstrated that IgE antibodies specific to allergen components and/or the peptide epitopes are good indicators for the identification of patients with food allergy, prediction of clinical severity and development of tolerance. In this review, we summarize our current knowledge regarding the allergens and IgE epitopes in the well-researched allergies to chicken egg, cow's milk, wheat, shrimp, and peanut.

IgE reactivity to hen egg white allergens in dogs with cutaneous adverse food reactions

“…These results are probably because OM is resistant to heat or digestion (Urisu et al, 1997;Kovacs-Nolan et al, 2000), because OVA is the dominant protein in egg white (Benhamou et al, 2010), and because OT is a heat-labile and digestible allergen (Matsuo et al, 2015). The findings of IgE reactivity to denatured OT in this study were similar to a previously reported immunoblotting analysis using human sera (Martos et al, 2013), and OT in which most of epitopes are probably conformational loses IgE-binding capacity when linearized (Mine and Yang, 2008;Järvinen et al, 2007).…”

Properties of Gluten Intolerance: Gluten Structure, Evolution, Pathogenicity and Detoxification Capabilities

“…Recently, it was shown that γ-, α/β-, ω5-, ω1,2-gliadins contain IgE-binding epitopes as well as HMW and LMW subunits of glutenin [99] (Table 4). Nevertheless, major allergenic protein of wheat is ω5-gliadin possessing N -terminal sequence SRLL, which can be crucial for allergy pathogenesis, and repetitive region consists almost entirely of peptides FPQQQ and QQIPQQ [14].…”

Food allergen detection by mass spectrometry: the role of systems biology

“…Selection of protein and peptide targets necessarily begins with the selection of one or more food allergens of interest as shown in Figure 1. For the big eight food allergens, which are responsible for a majority of allergic reactions, the proteins responsible for clinical reactivity are generally well understood 68,69 and are often abundant within the food. For example, 94% of egg-allergic individuals were sensitized to egg white protein Gal d 2 (ovalbumin), 70 which comprises 54% of egg white protein; 71 45–87.5% of peanut-allergic individuals were sensitized to Ara h 3 (an 11S globulin), 72,73 which comprises ~30% of peanut protein; 74 85–100% of peanut-allergic individuals were sensitized to Ara h 2 (a 2S albumin), 72,75 which comprises roughly 10% of peanut protein; 74 and over 85% of milk-allergic individuals were sensitized to the dominant casein protein fraction in milk.…”