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.

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