IgE-binding epitope mapping of tropomyosin allergen (Exo m 1) from Exopalaemon modestus, the freshwater Siberian prawn

Ziye Zhang; Xiu-Min Li; Hang Xiao; Anna Nowak-Wegrzyn; Peng Zhou

doi:10.1016/j.foodchem.2019.125603

IgE-binding epitope mapping of tropomyosin allergen (Exo m 1) from Exopalaemon modestus, the freshwater Siberian prawn

Food Chem. 2020 Mar 30:309:125603. doi: 10.1016/j.foodchem.2019.125603. Epub 2019 Oct 16.

Authors

Ziye Zhang¹, Xiu-Min Li², Hang Xiao³, Anna Nowak-Wegrzyn⁴, Peng Zhou⁵

Affiliations

¹ State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu Province 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu Province 214122, China; Department of Food Science, University of Massachusetts, Amherst, MA 01003, USA.
² Department of Microbiology and Immunology and Department of Otolaryngology, School of Medicine, New York Medical College, Valhalla, NY 10595, USA.
³ Department of Food Science, University of Massachusetts, Amherst, MA 01003, USA.
⁴ Allergy and Immunology, Department of Pediatrics, New York University School of Medicine Langone Health, New York, NY, USA; Department of Pediatrics, Gastroenterology and Nutrition, Collegium Medicum, University of Warmia and Mazury, Olsztyn, Poland.
⁵ State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu Province 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu Province 214122, China. Electronic address: zhoupeng@jiangnan.edu.cn.

PMID: 31707198
DOI: 10.1016/j.foodchem.2019.125603

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.

Keywords: Basophil; Epitope mapping; Exo m 1; Exopalaemon modestus; Gastrointestinal digestion.

MeSH terms

Adult
Allergens / chemistry
Allergens / immunology*
Allergens / metabolism
Animals
Basophils / immunology
Child
Child, Preschool
Epitope Mapping
Epitopes / chemistry
Epitopes / metabolism*
Female
Fresh Water
Humans
Immunoglobulin E / metabolism
Infant
Male
Palaemonidae / immunology*
Peptides / chemistry
Peptides / immunology
Sequence Homology, Amino Acid
Shellfish Hypersensitivity / immunology*
Tropomyosin / chemistry
Tropomyosin / immunology*
Tropomyosin / metabolism

Substances

Allergens
Epitopes
Peptides
Tropomyosin
Immunoglobulin E