Effect of the structure and potential allergenicity of glycated tropomyosin, the shrimp allergen

The aim is to elucidate whether the structural changes of shrimp tropomyosin (TM) following ribose treatment affected its potential allergenicity. The structural changes of glycated TM were analysed by fluorescence, ultraviolet spectrum (UV), circular dichroism (CD) and liquid chromatography-tandem mass spectrometry (LC-MS/MS), and the changes in allergenicity were investigated by enzyme-linked immunosorbent assay (ELISA) and RBL-2H3 cell model. The result indicated that ribose could cause the conformational structural changes of TM. Moreover, the phenylalanine, isoleucine and DL-methionine residues were altered by ribose by LC-MS/MS analysis. These modified amino acids also appeared in the shrimp allergic epitopes region. Furthermore, the glycated TM (4000 mmol L-1 ribose) could significantly decrease the IgE-binding capacity and inhibit the release of cytokines and mediators from RBL-2H3 cells. These findings suggest that ribose-induced glycation could damage the allergic epitope of TM, decreasing the potential allergenicity and could be considered for alleviating TM-induced food allergy.