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Glycation of the major milk allergen β-lactoglobulin changes its allergenicity by alterations in cellular uptake and degradation

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Abstract
Scope: During food processing, the Maillard reaction (MR) may occur, resulting in the formation of glycated proteins. Glycated proteins are of particular importance in food allergies because glycation may influence interactions with the immune system. This study compared native and extensively glycated milk allergen beta-lactoglobulin (BLG), in their interactions with cells crucially involved in allergy. Methods and results: BLG was glycated in MR and characterized. Native and glycated BLG were tested in experiments of epithelial transport, uptake and degradation by DCs, T-cell cytokine responses, and basophil cell degranulation using ELISA and flow cytometry. Glycation of BLG induced partial unfolding and reduced its intestinal epithelial transfer over a Caco-2 monolayer. Uptake of glycated BLG by bone marrow-derived dendritic cells (BMDC) was increased, although both BLG forms entered BMDC via the same mechanism, receptor-mediated endocytosis. Once inside the BMDC, glycated BLG was degraded faster, which might have led to observed lower cytokine production in BMDC/CD4(+) T-cells coculture. Finally, glycated BLG was less efficient in induction of degranulation of BLG-specific IgE sensitized basophil cells. Conclusions: This study suggests that glycation of BLG by MR significantly alters its fate in processes involved in immunogenicity and allergenicity, pointing out the importance of food processing in food allergy.
Keywords
MAILLARD REACTION, END-PRODUCTS, WHEY-PROTEIN, SCAVENGER RECEPTORS, DENDRITIC CELLS, FOOD ALLERGY, SENSITIZATION, RECOGNITION, TROPOMYOSIN, OVALBUMIN, beta-lactoglobulin, food allergens, food processing, Maillard reaction, uptake and degradation by DCs

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Citation

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MLA
Perusko, Marija et al. “Glycation of the Major Milk Allergen Β-lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation.” MOLECULAR NUTRITION & FOOD RESEARCH 62.17 (2018): n. pag. Print.
APA
Perusko, M., van Roest, M., Stanic-Vucinic, D., Simons, P. J., Pieters, R. H., Cirkovic Velickovic, T., & Smit, J. J. (2018). Glycation of the major milk allergen β-lactoglobulin changes its allergenicity by alterations in cellular uptake and degradation. MOLECULAR NUTRITION & FOOD RESEARCH, 62(17).
Chicago author-date
Perusko, Marija, Manon van Roest, Dragana Stanic-Vucinic, Peter J Simons, Raymond HH Pieters, Tanja Cirkovic Velickovic, and Joost J Smit. 2018. “Glycation of the Major Milk Allergen Β-lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation.” Molecular Nutrition & Food Research 62 (17).
Chicago author-date (all authors)
Perusko, Marija, Manon van Roest, Dragana Stanic-Vucinic, Peter J Simons, Raymond HH Pieters, Tanja Cirkovic Velickovic, and Joost J Smit. 2018. “Glycation of the Major Milk Allergen Β-lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation.” Molecular Nutrition & Food Research 62 (17).
Vancouver
1.
Perusko M, van Roest M, Stanic-Vucinic D, Simons PJ, Pieters RH, Cirkovic Velickovic T, et al. Glycation of the major milk allergen β-lactoglobulin changes its allergenicity by alterations in cellular uptake and degradation. MOLECULAR NUTRITION & FOOD RESEARCH. 2018;62(17).
IEEE
[1]
M. Perusko et al., “Glycation of the major milk allergen β-lactoglobulin changes its allergenicity by alterations in cellular uptake and degradation,” MOLECULAR NUTRITION & FOOD RESEARCH, vol. 62, no. 17, 2018.
@article{8615089,
  abstract     = {Scope: During food processing, the Maillard reaction (MR) may occur, resulting in the formation of glycated proteins. Glycated proteins are of particular importance in food allergies because glycation may influence interactions with the immune system. This study compared native and extensively glycated milk allergen beta-lactoglobulin (BLG), in their interactions with cells crucially involved in allergy. 
Methods and results: BLG was glycated in MR and characterized. Native and glycated BLG were tested in experiments of epithelial transport, uptake and degradation by DCs, T-cell cytokine responses, and basophil cell degranulation using ELISA and flow cytometry. Glycation of BLG induced partial unfolding and reduced its intestinal epithelial transfer over a Caco-2 monolayer. Uptake of glycated BLG by bone marrow-derived dendritic cells (BMDC) was increased, although both BLG forms entered BMDC via the same mechanism, receptor-mediated endocytosis. Once inside the BMDC, glycated BLG was degraded faster, which might have led to observed lower cytokine production in BMDC/CD4(+) T-cells coculture. Finally, glycated BLG was less efficient in induction of degranulation of BLG-specific IgE sensitized basophil cells. 
Conclusions: This study suggests that glycation of BLG by MR significantly alters its fate in processes involved in immunogenicity and allergenicity, pointing out the importance of food processing in food allergy.},
  articleno    = {1800341},
  author       = {Perusko, Marija and van Roest, Manon and Stanic-Vucinic, Dragana and Simons, Peter J and Pieters, Raymond HH and Cirkovic Velickovic, Tanja and Smit, Joost J},
  issn         = {1613-4125},
  journal      = {MOLECULAR NUTRITION & FOOD RESEARCH},
  keywords     = {MAILLARD REACTION,END-PRODUCTS,WHEY-PROTEIN,SCAVENGER RECEPTORS,DENDRITIC CELLS,FOOD ALLERGY,SENSITIZATION,RECOGNITION,TROPOMYOSIN,OVALBUMIN,beta-lactoglobulin,food allergens,food processing,Maillard reaction,uptake and degradation by DCs},
  language     = {eng},
  number       = {17},
  pages        = {12},
  title        = {Glycation of the major milk allergen β-lactoglobulin changes its allergenicity by alterations in cellular uptake and degradation},
  url          = {http://dx.doi.org/10.1002/mnfr.201800341},
  volume       = {62},
  year         = {2018},
}

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