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
Keywords
Adult, Allergens, Animals, Basophils, Child, Child, Preschool, Epitope Mapping, Epitopes, Female, Fresh Water, Humans, Immunoglobulin E, Infant, Male, Palaemonidae, Peptides, Sequence Homology, Amino Acid, Shellfish Hypersensitivity, Tropomyosin
Disciplines
Medicine and Health Sciences
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