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.
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http://dx.doi.org/10.1007/978-1-4939-3037-1_19 | DOI Listing |
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.
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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.
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December 2024
Department Diagnostics, Fraunhofer Institute for Cell Therapy and Immunology (IZI), Perlickstr. 1, 04103 Leipzig, Germany.
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 PDFInt 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 PDFFood 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.
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