Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation
Аутори
Radosavljević, JelenaApostolović, Danijela
Mihailović, Jelena
Atanasković-Marković, Marina
Burazer, Lidija
van Hage, Marianne
Ćirković-Veličković, Tanja
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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 t...o 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.
Кључне речи:
milk / allergenicity / allergy / pepsin / casein / IgE / digestion-resistant peptides / gastric simulated digestionИзвор:
Foods, 2020, 9, 11Издавач:
- MDPI, Basel
Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200168 (Универзитет у Београду, Хемијски факултет) (RS-200168)
- Belgian Special Research Fund BOF StG [01N01718]
- Serbian Academy of Sciences and Arts GA [F-26]
- FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics (EU-810752)
- Swedish Research Council
- Stockholm County Council (ALF Project)
- Swedish Asthma and Allergy Association's Research Foundation
- Swedish Heart-Lung Foundation
- Swedish Cancer and Allergy Foundation
- Konsul Th C Berg's Foundation
- King Gustaf V's 80-year Foundation
- Magnus Bergvall Foundation
- Lars Hierta Memorial Foundation
- Karolinska Institutet
Напомена:
- Supplementary information: https://hdl.handle.net/21.15107/rcub_intor_645
Повезане информације:
- Повезани садржај
https://hdl.handle.net/21.15107/rcub_intor_645
Институција/група
TorlakTY - JOUR AU - Radosavljević, Jelena AU - Apostolović, Danijela AU - Mihailović, Jelena AU - Atanasković-Marković, Marina AU - Burazer, Lidija AU - van Hage, Marianne AU - Ćirković-Veličković, Tanja PY - 2020 UR - http://intor.torlakinstitut.com/handle/123456789/547 AB - 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. PB - MDPI, Basel T2 - Foods T1 - Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation IS - 11 VL - 9 DO - 10.3390/foods9111576 ER -
@article{ author = "Radosavljević, Jelena and Apostolović, Danijela and Mihailović, Jelena and Atanasković-Marković, Marina and Burazer, Lidija and van Hage, Marianne and Ćirković-Veličković, Tanja", year = "2020", abstract = "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.", publisher = "MDPI, Basel", journal = "Foods", title = "Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation", number = "11", volume = "9", doi = "10.3390/foods9111576" }
Radosavljević, J., Apostolović, D., Mihailović, J., Atanasković-Marković, M., Burazer, L., van Hage, M.,& Ćirković-Veličković, T.. (2020). Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation. in Foods MDPI, Basel., 9(11). https://doi.org/10.3390/foods9111576
Radosavljević J, Apostolović D, Mihailović J, Atanasković-Marković M, Burazer L, van Hage M, Ćirković-Veličković T. Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation. in Foods. 2020;9(11). doi:10.3390/foods9111576 .
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" in Foods, 9, no. 11 (2020), https://doi.org/10.3390/foods9111576 . .