Jean-Claude Tabet: CURRICULUM VITAE

Fenaille, François

doi:10.1177/1469066719840089

Cited by 1 publication

(1 citation statement)

References 333 publications

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“…[36] Furthermore, in our basophil activation experiments, glycation of BLG reduced its capacity to crosslink FcεRI receptors on RBL cells. In extensively glycated BLG, all residues containing free amino group (16 lysines, two arginines, and Nterminal amino group of Leu 1) seem to be glycated, [38,39] while all of the BLG-specific chimeric human IgE monoclonal antibodies used in this study recognize peptides containing at least 1-2 residues with possible glycation sites. [27] Therefore, it is highly likely that extensive BLG glycation reduced mAb IgE binding by changing epitope structure, and led to reduced basophil activation.…”

Section: Discussionmentioning

confidence: 98%

Glycation of the Major Milk Allergen β‐Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation

Peruško¹,

Roest

Stanić-Vučinić

et al. 2018

Molecular Nutrition Food Res

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ScopeDuring food processing, the Maillard reaction (МR) 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 β‐lactoglobulin (BLG), in their interactions with cells crucially involved in allergy.Methods and resultsBLG 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.ConclusionsThis 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.

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Section: Discussionmentioning

confidence: 98%