NYMC Faculty Publications
IgE-Binding Epitope Mapping of Tropomyosin Allergen (Exo m 1) from Exopalaemon Modestus, the Freshwater Siberian Prawn
Author Type(s)
Faculty
DOI
10.1016/j.foodchem.2019.125603
Journal Title
Food Chemistry
First Page
125603
Last Page
125603
Document Type
Article
Publication Date
3-30-2020
Department
Pathology, Microbiology and Immunology
Abstract
Exopalaemon modestus (EM) is a shrimp delicacy that could cause food allergy, the major allergen of EM is Exo m 1. The amino acid (AA) sequence, IgE-binding epitopes and allergenic peptides in gastrointestinal (GI) digests of Exo m 1, and their effects on basophil function were investigated. Exo m 1 has an AA-sequence of high similarity with other shrimp tropomyosins, while not 100% matching. The IgE-binding epitopes of Exo m 1 are epitope 1 (43-59, VHNLQKRMQQLENDLDS), epitope 2 (85-105, VAALNRRIQLLEEDLERSEER), epitope 3 (131-164, ENRSLSDEERMDALENQLKEARFLAEEADRKYDE), epitope 4 (187-201, ESKIVELEEELRVVG) and epitope 5 (243-280, ERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSE). Among the thirty-three peptides of Exo m 1 identified in GI digests, two were highly recognized by IgE, twenty-four moderately or weakly bound IgE, and seven had no IgE-reactivities. These IgE-binding epitopes and GI digestion induced-allergenic peptides could activate basophil degranulation, and CD63 and CD203c expression, they could be potential peptide-based immunotherapy for shrimp allergic individuals.
Recommended Citation
Zhang, Z., Li, X., Xiao, H., Nowak-Wegrzyn, A., & Zhou, P. (2020). IgE-Binding Epitope Mapping of Tropomyosin Allergen (Exo m 1) from Exopalaemon Modestus, the Freshwater Siberian Prawn. Food Chemistry, 309, 125603-125603. https://doi.org/10.1016/j.foodchem.2019.125603
