“…Our results demonstrated a significant increase in immunogenicity for epitope 2 containing proline hydroxylations, confirming reports in literature (Fig. S7) 33 . Taken together, our study showed that the nanoallergen platform enabled a quantitative measure of immunogenicity for each IgE binding epitope of Ara h2 for this patient.Figure 4Nanoallergens demonstrate immunogenicity of Ara h2 IgE binding epitopes 1–8 with patient sera.…”
Current methods for detection and diagnosis of allergies do not provide epitope specific immunogenic information and hence lack critical information that could aid in the prediction of clinical responses. To address this issue, we developed a nanoparticle based platform, called nanoallergens that enable multivalent display of potential allergy epitopes for determining the immunogenicity of each IgE binding epitope. By synthesizing nanoallergens that present various epitopes from the major peanut allergen, Ara h2, we directly determined the immunogenicity of each epitope, alone and in combination with other epitopes, using patient sera. This information provided insights on which epitopes are most critical for physiological responses to Ara h2 and revealed the importance of both high and low affinity epitopes for allergic responses. We anticipate the nanoallergen platform to be used to provide information regarding allergic reactions and therefore potentially aid in more accurate diagnosis and design of personalized treatment options.
“…Our results demonstrated a significant increase in immunogenicity for epitope 2 containing proline hydroxylations, confirming reports in literature (Fig. S7) 33 . Taken together, our study showed that the nanoallergen platform enabled a quantitative measure of immunogenicity for each IgE binding epitope of Ara h2 for this patient.Figure 4Nanoallergens demonstrate immunogenicity of Ara h2 IgE binding epitopes 1–8 with patient sera.…”
Current methods for detection and diagnosis of allergies do not provide epitope specific immunogenic information and hence lack critical information that could aid in the prediction of clinical responses. To address this issue, we developed a nanoparticle based platform, called nanoallergens that enable multivalent display of potential allergy epitopes for determining the immunogenicity of each IgE binding epitope. By synthesizing nanoallergens that present various epitopes from the major peanut allergen, Ara h2, we directly determined the immunogenicity of each epitope, alone and in combination with other epitopes, using patient sera. This information provided insights on which epitopes are most critical for physiological responses to Ara h2 and revealed the importance of both high and low affinity epitopes for allergic responses. We anticipate the nanoallergen platform to be used to provide information regarding allergic reactions and therefore potentially aid in more accurate diagnosis and design of personalized treatment options.
“…12,39,173,174 In addition, posttranslational proline hydroxylation of Ara h 2 contributes to linear IgE epitopes. 202 Ara h 6 shares 55% identity with the AA sequence of Ara h 2 and some of the IgE epitopes of Ara h 6 are cross-reactive with those of Ara h 2. 173 As with Ara h 2, the resistance of Ara h 6 to heat and digestive enzymes was reported.…”
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.
“…This fraction also contains important highly immunoreactive peptides. It has been demonstrated that some Ara h 2 peptides of size <3 kDa can cross‐link IgE/FcεRI complexes and degranulate cells, and that Ara h 1, when digested to small peptide fragments, retains both the sensitizing and the IgE‐reacting potential because of the peptide's ability to aggregate …”
Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
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