Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing
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2014
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Prikaz svih podataka o dokumentuApstrakt
Cross-linking of proteins has been exploited by the food industry to change food texture and functionality but the effects of these manipulations on food allergenicity still remain unclear. To model the safety assessment of these food biopolymers, we created cross-linked bovine beta-lactoglobulin (CL-BLG) by laccase treatment. The purpose of the present study was to compare the immunogenicity and allergenicity of CL-BLG with native BLG in a mouse model of food allergy. First, BALB/c mice were intragastrically sensitized and orally challenged with BLG or CL-BLG and BLG-specific serum antibodies and splenic leukocyte cytokine production and cell proliferation were measured. Hereafter, epithelial protein uptake was monitored in vitro and in vivo and the effects of BLG cross-linking on interactions with dendritic cells were analyzed in vitro. Sensitization of mice with CL-BLG resulted in higher levels of IgE, IgG1, and IgG2a. In contrast, a subsequent oral challenge with CL-BLG resulted in... lower mast cell degranulation. Cross-linking of BLG reduced its epithelial uptake but promoted sampling through Peyer's patches. Differences in endocytosis by dendritic cells (DCs) and in vitro endolysosomal processing were observed between BLG and CL-BLG. CL-BLG primed DCs induced higher Th2 response in vitro. Cross-linking of BLG increased its sensitizing capacity, implying that the assessment of highly polymerized food proteins is of clinical importance in food allergy. Moreover, manufacturers of foods or therapeutic proteins should pay considerate attention to the health risk of protein aggregation.
Ključne reči:
protein cross-linking / protein aggregation / food processing / allergic sensitization / beta-lactoglobulin / mouse model of food allergyIzvor:
Toxicological Sciences, 2014, 140, 1, 224-235Izdavač:
- Oxford Univ Press, Oxford
Finansiranje / projekti:
- Molekularne osobine i modifikacije nekih respiratornih i nutritivnih alergena (RS-MESTD-Basic Research (BR or ON)-172024)
- Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-FP7-256716)
Napomena:
- Free full text: https://doi.org/10.1093/toxsci/kfu062
DOI: 10.1093/toxsci/kfu062
ISSN: 1096-6080
PubMed: 24743699
WoS: 000339722100019
Scopus: 2-s2.0-84903848519
Kolekcije
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Stojadinović, Marija M. AU - Pieters, Raymond AU - Smit, Joost AU - Ćirković-Veličković, Tanja PY - 2014 UR - https://cherry.chem.bg.ac.rs/handle/123456789/1823 AB - Cross-linking of proteins has been exploited by the food industry to change food texture and functionality but the effects of these manipulations on food allergenicity still remain unclear. To model the safety assessment of these food biopolymers, we created cross-linked bovine beta-lactoglobulin (CL-BLG) by laccase treatment. The purpose of the present study was to compare the immunogenicity and allergenicity of CL-BLG with native BLG in a mouse model of food allergy. First, BALB/c mice were intragastrically sensitized and orally challenged with BLG or CL-BLG and BLG-specific serum antibodies and splenic leukocyte cytokine production and cell proliferation were measured. Hereafter, epithelial protein uptake was monitored in vitro and in vivo and the effects of BLG cross-linking on interactions with dendritic cells were analyzed in vitro. Sensitization of mice with CL-BLG resulted in higher levels of IgE, IgG1, and IgG2a. In contrast, a subsequent oral challenge with CL-BLG resulted in lower mast cell degranulation. Cross-linking of BLG reduced its epithelial uptake but promoted sampling through Peyer's patches. Differences in endocytosis by dendritic cells (DCs) and in vitro endolysosomal processing were observed between BLG and CL-BLG. CL-BLG primed DCs induced higher Th2 response in vitro. Cross-linking of BLG increased its sensitizing capacity, implying that the assessment of highly polymerized food proteins is of clinical importance in food allergy. Moreover, manufacturers of foods or therapeutic proteins should pay considerate attention to the health risk of protein aggregation. PB - Oxford Univ Press, Oxford T2 - Toxicological Sciences T1 - Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing VL - 140 IS - 1 SP - 224 EP - 235 DO - 10.1093/toxsci/kfu062 ER -
@article{ author = "Stojadinović, Marija M. and Pieters, Raymond and Smit, Joost and Ćirković-Veličković, Tanja", year = "2014", abstract = "Cross-linking of proteins has been exploited by the food industry to change food texture and functionality but the effects of these manipulations on food allergenicity still remain unclear. To model the safety assessment of these food biopolymers, we created cross-linked bovine beta-lactoglobulin (CL-BLG) by laccase treatment. The purpose of the present study was to compare the immunogenicity and allergenicity of CL-BLG with native BLG in a mouse model of food allergy. First, BALB/c mice were intragastrically sensitized and orally challenged with BLG or CL-BLG and BLG-specific serum antibodies and splenic leukocyte cytokine production and cell proliferation were measured. Hereafter, epithelial protein uptake was monitored in vitro and in vivo and the effects of BLG cross-linking on interactions with dendritic cells were analyzed in vitro. Sensitization of mice with CL-BLG resulted in higher levels of IgE, IgG1, and IgG2a. In contrast, a subsequent oral challenge with CL-BLG resulted in lower mast cell degranulation. Cross-linking of BLG reduced its epithelial uptake but promoted sampling through Peyer's patches. Differences in endocytosis by dendritic cells (DCs) and in vitro endolysosomal processing were observed between BLG and CL-BLG. CL-BLG primed DCs induced higher Th2 response in vitro. Cross-linking of BLG increased its sensitizing capacity, implying that the assessment of highly polymerized food proteins is of clinical importance in food allergy. Moreover, manufacturers of foods or therapeutic proteins should pay considerate attention to the health risk of protein aggregation.", publisher = "Oxford Univ Press, Oxford", journal = "Toxicological Sciences", title = "Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing", volume = "140", number = "1", pages = "224-235", doi = "10.1093/toxsci/kfu062" }
Stojadinović, M. M., Pieters, R., Smit, J.,& Ćirković-Veličković, T.. (2014). Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing. in Toxicological Sciences Oxford Univ Press, Oxford., 140(1), 224-235. https://doi.org/10.1093/toxsci/kfu062
Stojadinović MM, Pieters R, Smit J, Ćirković-Veličković T. Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing. in Toxicological Sciences. 2014;140(1):224-235. doi:10.1093/toxsci/kfu062 .
Stojadinović, Marija M., Pieters, Raymond, Smit, Joost, Ćirković-Veličković, Tanja, "Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing" in Toxicological Sciences, 140, no. 1 (2014):224-235, https://doi.org/10.1093/toxsci/kfu062 . .