Allergenicity suppression of tropomyosin from Exopalaemon modestus by glycation with saccharides of different molecular sizes

• Published in: Food chemistry 2019-08, Vol.288, p.268-275
• Main Authors: Zhang, Ziye, Xiao, Hang, Zhou, Peng
• Format: Article
• Language: English
• Subjects: Adolescent; Allergenicity; Allergens - immunology; Animals; Caco-2; Caco-2 Cells; Cell Line; Cell Proliferation - drug effects; Child, Preschool; Exo m 1; Exopalaemon modestus; Female; Glycation; Glycosylation; Humans; Immunoglobulin E - blood; Interleukin-8 - metabolism; KU812 basophil; Male; Maltose - metabolism; Middle Aged; Oligosaccharides - metabolism; Palaemonidae - metabolism; Trisaccharides - metabolism; Tropomyosin; Tropomyosin - immunology; Tropomyosin - metabolism; Tropomyosin - pharmacology
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2019.03.019

•Glycation of tropomyosin could destruct and mask epitopes.•Glycated tropomyosin by maltose insignificantly suppressed allergenicity.•Saccharides of larger molecular sizes reduced tropomyosin allergenicity.•Larger saccharides suppressed allergy reactivity of Caco-2 and KU812 cells. The allergenicity suppression of tropomyosin (TM) from Exopalaemon modestus by glycation with saccharides of different molecular sizes (glucose, maltose, maltotriose, maltopentaose and maltoheptaose) was investigated using immunoblotting, human colon epithelial cell line (Caco-2) and human basophil cell line (KU812). Glycation of TM by glucose, maltotriose, maltopentaose and maltoheptaose significantly destructed and masked TM epitopes to obtain lower allergenicity, while glycation of TM by maltose had insignificant suppression on TM allergenicity. In addition, the glycated TM by glucose, maltotriose, maltopentaose and maltoheptaose inhibited the proliferation and IL-8 secretion of Caco-2, and the CD63 and CD203c expression, MAPK signaling of KU812 basophils, while the glycated TM by maltose had insignificant suppression on the allergy reactivities of Caco-2 cells and KU812 basophils. Glycation of TM by saccharides with larger molecular sizes (such as maltoheptaose) could provide new insight into the desensitization of shrimp-induced food allergy.