Comparative Analysis of Glycosylation Affecting Sensitization by Regulating the Cross-Reactivity of Parvalbumins in Turbot (Scophthalmus maximus), Conger Eel (Conger myriaster) and Sea Bass (Micropterus salmoides)

Parvalbumin (PV) is the most common allergen in fish. Some patients with fish allergy are allergic to only one species of fish but are tolerant to others; however, the underlying mechanism has not been identified. This study showed that three types of glycated fishes' PV showed a similar decrease in immunoglobulin E (IgE) binding. Glycosylation could improve the simulated gastric fluid (SGF) and simulated intestinal fluid (SIF) digestion resistance of fishes' PV. We also discovered that the cross-reactivity between eel and turbot was weaker than that of bass; glycosylation can reduce cross-reactivity between eel/bass and turbot by downregulating Th2 cytokines and upregulating Th1 cytokines as well as downregulating the expression of G-T PV, G-E PV, G-B PV of IL-4 (94.31 +/- 3.16, 73.26 +/- 0.91, 94.95 +/- 3.03 ng/mL), and IL-13 (38.84 +/- 0.75, 33.77 +/- 0.71, 36.51 +/- 0.50 ng/mL) and upregulating the expression of IFN-gamma (318.01 +/- 3.46, 387.15 & PLUSMN; 3.30, 318.01 +/- 4.21 ng/mL) compared with T PV, respectively. This study showed that glycosylation affected sensitization by regulating the cross-reactivity of parvalbumins.

Automated summary

This study investigated the effect of glycosylation on the allergenicity of fish parvalbumin (PV). Glycosylation was found to decrease the binding of immunoglobulin E (IgE) to PV and improve its resistance to digestion. Moreover, glycosylation was shown to reduce cross-reactivity between different species of fish.