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Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation
The aim of this study was to identify short digestion-resistant peptides (SDRPs) released by pepsin digestion of the whole cow’s milk and examine their IgE reactivity and allergenicity. Raw milk was subjected to simulated gastric digestion. SDRPs were fractionated from the digests and identified by...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7692894/ https://www.ncbi.nlm.nih.gov/pubmed/33143174 http://dx.doi.org/10.3390/foods9111576 |
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author | Radosavljević, Jelena Apostolović, Danijela Mihailović, Jelena Atanasković-Marković, Marina Burazer, Lidija van Hage, Marianne Ćirković Veličković, Tanja |
author_facet | Radosavljević, Jelena Apostolović, Danijela Mihailović, Jelena Atanasković-Marković, Marina Burazer, Lidija van Hage, Marianne Ćirković Veličković, Tanja |
author_sort | Radosavljević, Jelena |
collection | PubMed |
description | The aim of this study was to identify short digestion-resistant peptides (SDRPs) released by pepsin digestion of the whole cow’s milk and examine their IgE reactivity and allergenicity. Raw milk was subjected to simulated gastric digestion. SDRPs were fractionated from the digests and identified by MS. Milk SDRPs were evaluated for aggregability, propensity to compete for IgE binding with individual milk allergens, and ability to bind IgG4 from allergic and milk-tolerant individuals. The majority of milk SDRPs originated from caseins (97% of peptides) and overlapped with the known IgE epitopes of cow’s milk allergens. SDRPs competed with milk proteins for binding to human IgE and readily formed aggregates. The average peptide length was 10.6 ± 3.5 amino acids. The ability to provoke allergenic in vivo responses was confirmed by skin-prick testing (SPT) in five milk-allergic subjects. This was attributed to the peptide ability to aggregate into non-covalent complexes. SDRPs are able to induce response in SPT, but only in 50% of the sera SDRPs were able to inhibit IgG4 binding to caseins. Hence, SDRPs corresponding to the mainly continuous epitopes of milk proteins induce allergenic in vivo responses in milk-allergic subjects due to aggregation. |
format | Online Article Text |
id | pubmed-7692894 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76928942020-11-28 Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation Radosavljević, Jelena Apostolović, Danijela Mihailović, Jelena Atanasković-Marković, Marina Burazer, Lidija van Hage, Marianne Ćirković Veličković, Tanja Foods Article The aim of this study was to identify short digestion-resistant peptides (SDRPs) released by pepsin digestion of the whole cow’s milk and examine their IgE reactivity and allergenicity. Raw milk was subjected to simulated gastric digestion. SDRPs were fractionated from the digests and identified by MS. Milk SDRPs were evaluated for aggregability, propensity to compete for IgE binding with individual milk allergens, and ability to bind IgG4 from allergic and milk-tolerant individuals. The majority of milk SDRPs originated from caseins (97% of peptides) and overlapped with the known IgE epitopes of cow’s milk allergens. SDRPs competed with milk proteins for binding to human IgE and readily formed aggregates. The average peptide length was 10.6 ± 3.5 amino acids. The ability to provoke allergenic in vivo responses was confirmed by skin-prick testing (SPT) in five milk-allergic subjects. This was attributed to the peptide ability to aggregate into non-covalent complexes. SDRPs are able to induce response in SPT, but only in 50% of the sera SDRPs were able to inhibit IgG4 binding to caseins. Hence, SDRPs corresponding to the mainly continuous epitopes of milk proteins induce allergenic in vivo responses in milk-allergic subjects due to aggregation. MDPI 2020-10-30 /pmc/articles/PMC7692894/ /pubmed/33143174 http://dx.doi.org/10.3390/foods9111576 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Radosavljević, Jelena Apostolović, Danijela Mihailović, Jelena Atanasković-Marković, Marina Burazer, Lidija van Hage, Marianne Ćirković Veličković, Tanja Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation |
title | Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation |
title_full | Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation |
title_fullStr | Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation |
title_full_unstemmed | Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation |
title_short | Digestomics of Cow’s Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation |
title_sort | digestomics of cow’s milk: short digestion-resistant peptides of casein form functional complexes by aggregation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7692894/ https://www.ncbi.nlm.nih.gov/pubmed/33143174 http://dx.doi.org/10.3390/foods9111576 |
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