IgE Epitope Mapping Using Peptide Microarray Immunoassay.

Methods Mol Biol

Pediatric Allergy and Immunology, Icahn School of Medicine at Mount Sinai, Box 1089, One Gustave L. Levy Place, New York, NY, 10029-6574, USA.

Published: August 2016

IgE epitope mapping of food allergens contributes to a better understanding of the pathogenesis of food allergy and may become an additional tool for food allergy diagnosis/prognosis. Microarray platforms which allow for simultaneous screening of a large number of peptides corresponding to the sequences of food allergens are ideally suited for large-scale IgE epitope mapping. Here we describe the method of performing a reliable and sensitive peptide microarray immunoassay, which was developed in our lab and results in the identification of candidate IgE epitope biomarkers useful in determining allergic disease severity and prognosis, as well as in the prediction of treatment outcomes. A gastric digestion model that can be applied to prescreen peptides and reduce costs in the peptide microarray is also described in this chapter.

Download full-text PDF

Source
http://dx.doi.org/10.1007/978-1-4939-3037-1_19DOI Listing

Publication Analysis

Top Keywords

ige epitope
16
epitope mapping
12
peptide microarray
12
microarray immunoassay
8
food allergens
8
food allergy
8
ige
4
mapping peptide
4
microarray
4
immunoassay ige
4

Similar Publications

Novel Diagnostics in Food Allergy.

J Allergy Clin Immunol

December 2024

Department of Women and Children's Health (Pediatric Allergy), School of Life Course Sciences, Faculty of Life Sciences and Medicine, King's College London, London, United Kingdom; Peter Gorer Department of Immunobiology, School of Immunology and Microbial Sciences, King's College London, London, United Kingdom; Children's Allergy Service, Evelina London Children's Hospital, Guy's and St Thomas' Hospital, London, United Kingdom. Electronic address:

Food allergy is increasing in prevalence, and poses significant challenges for individuals and their families, adversely impacting their quality of life. Misdiagnosis can lead to unnecessary dietary and social limitations, and increased food allergy risk, while failure to diagnose may result in life-threatening anaphylaxis. Therefore, a precise diagnosis is of the utmost importance; however, barriers exist at every stage of the diagnostic process.

View Article and Find Full Text PDF

Protein extraction from edible insects: Implications for IgE-binding capacity.

Food Chem

December 2024

REQUIMTE-LAQV, Faculdade de Farmácia, Universidade do Porto, Rua de Jorge Viterbo Ferreira, 228, 4050-313 Porto, Portugal. Electronic address:

Edible insects are attracting increasing interest as sustainable alternative protein sources. Despite being considered a safe food for most population, their consumption can pose health risks for allergic patients. This work focused on isolating proteins from the four-European Union approved insects (Tenebrio molitor, Alphitobius diaperinus, Acheta domesticus, and Locusta migratoria) and evaluating their potential immunoglobulin E (IgE)-reactivity with crustacean-allergic patients' sera.

View Article and Find Full Text PDF

Hazelnuts are frequently involved in IgE-mediated reactions and are the main cause of nut allergies in Europe. Most food products are processed before human consumption. Food processing can modify the structure, properties, and function of proteins, and as a result, the IgE-binding capacity of allergens can be affected.

View Article and Find Full Text PDF

Localization and antigenicity reduction of immunodominant conformational IgE epitopes on αs1-casein.

Int J Biol Macromol

December 2024

College of Food Science and Engineering, Ocean University of China, Qingdao 266000, China. Electronic address:

αs1-Casein (αs1-CN) is the major allergen in cow milk; however, the understanding of its conformational epitopes remains limited due to the absence of a well-defined three-dimensional structure, which has impeded efforts to effectively reduce its antigenicity. This study employed molecular dynamics simulations (MD), ELISA, cell assays and peptidomes analysis to investigate the critical conformational epitopes of αs1-Casein. MD and immunological analyses identified a dominant conformational epitope encompassing the regions S55-E75 & Y154-T174 & F179-W199, which exhibited strong binding affinity to IgE and triggered the releasing of β-hexosaminidase, histamine and IL-6 in KU812 cells, thereby inducing allergic responses.

View Article and Find Full Text PDF

The influence on the structure and allergenicity of milk β-lactoglobulin by methylglyoxal during thermal processing.

Food Res Int

November 2024

College of Food Science and Engineering, Qingdao Agricultural University,Qingdao 266109, China; Qingdao Institute of Special Food, Qingdao 266109, China. Electronic address:

This study aims to investigate the effects of the typical glycation intermediate methylglyoxal (MGO) on the structure and allergenicity of milk β-lactoglobulin (βLG) during thermal processing. Structural changes were assessed using SDS-PAGE, intrinsic fluorescence, circular dichroism, and HPLC-MS/MS. Allergenicity was evaluated through in vitro and in vivo experiments.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!