Mapping and IgE-binding capacity analysis of heat/digested stable epitopes of mud crab allergens

Abstract

Mud crab (Scylla paramamosain) is widely consumed after thermal processing. It is necessary to comprehensively evaluate of the allergenic potential and epitopes of allergens in high temperature–pressure (HTP) treated S. paramamosain. Tropomyosin and arginine kinase presented higher prevalence (30.77% and 42.13%) than the other three important crab allergens by component-resolved diagnosis. The surface expression of basophils CD63 and CD203c were decreased in HTP treated crab, an effect that was even more evident after digestion and absorption by the intestinal Caco-2 cell model. Of the 35 stable epitope, six were for the first time identified in shellfish. Seven heat/digested stable peptides of tropomyosin retained IgE-binding capacity and were shown to interact with MHC-II. Five epitopes (amino acids 19–29, 99–109, 153–162, 170–188 and 211–221) were the first identified in crab. The study provides insight into prevention and therapy of crab allergy, as well as helps to reduce crab allergenicity during thermal processing.