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IgE Epitope Analysis for Scy p 1 and Scy p 3, the Heat-Stable Myofibrillar Allergens in Mud Crab
Meng-Si Li1, Fei Xia1, Qingmei Liu1
1College of Ocean Food and Biological Engineering, Xiamen Key Laboratory of Marine Functional Food, Fujian Provincial Engineering Technology Research Center of Marine Functional Food, National & Local Joint Engineering Research Center of Processing Technology for Aquatic Products, Jimei University, Xiamen, Fujian 361021, China.
Abstract:
Tropomyosin (Scy p 1) and myosin light chain (Scy p 3) are investigated to be important heat-stable allergens in Scylla paramamosain. However, the epitopes of Scy p 1 and Scy p 3 are limited. In this study, recombinant Scy p 1 and Scy p 3 had similar IgE-binding capacity to natural proteins. Mimotopes of Scy p 1 and Scy p 3 were analyzed by bioinformatics, phage display, and one-bead-one-compound technology. Ten linear epitopes of Scy p 1 and seven linear epitopes of Scy p 3 were identified by synthetic peptides and inhibition dot blot. Meanwhile, three conformational epitopes of Scy p 1 and seven conformational epitopes of Scy p 3 were verified by site-directed mutagenesis and the serological test. Furthermore, strong IgE-binding epitopes of Scy p 1 and Scy p 3 were conserved in multiple crustaceans. Overall, these epitopes could enhance our understanding of crab allergens, which lay the foundation for a cross-reaction.
