Identification of allergens for food-dependent exercise-induced anaphylaxis to shrimp

Shrimp is a causative food that elicits food-dependent exercise-induced anaphylaxis (FDEIA). In this study, we sought to identify IgE-binding allergens in patients with shrimp-FDEIA. Sera were obtained from eight patients with shrimp-FDEIA and two healthy control subjects. Proteins were extracted fr...

Full description

Saved in:
Bibliographic Details
Published in:Scientific reports 2021-03, Vol.11 (1), p.5400-5400, Article 5400
Main Authors: Akimoto, Shiori, Yokooji, Tomoharu, Ogino, Ryohei, Chinuki, Yuko, Taogoshi, Takanori, Adachi, Atsuko, Morita, Eishin, Matsuo, Hiroaki
Format: Article
Language:English
Subjects:
692/308/53/2421
692/4017
Allergens
Ammonium
Ammonium sulfate
Anaphylaxis
Food
Food allergies
High-performance liquid chromatography
Humanities and Social Sciences
Hydrophobicity
Immunoglobulin E
Ions
Liquid chromatography
Litopenaeus vannamei
Mass spectrometry
Mass spectroscopy
multidisciplinary
Proteins
Science
Science (multidisciplinary)
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Shrimp is a causative food that elicits food-dependent exercise-induced anaphylaxis (FDEIA). In this study, we sought to identify IgE-binding allergens in patients with shrimp-FDEIA. Sera were obtained from eight patients with shrimp-FDEIA and two healthy control subjects. Proteins were extracted from four shrimp species by homogenization in Tris buffer. Immunoblot analysis revealed that IgE from patient sera bound strongly to a 70-kDa and a 43-kDa protein in a preparation of Tris-soluble extracts from Litopenaeus vannamei . Mass spectrometry identified the 70-kDa and 43-kDa proteins as a P75 homologue and fructose 1,6-bisphosphate aldolase (FBPA), respectively. To confirm that the putative shrimp allergens were specifically recognized by serum IgE from shrimp-FDEIA patients, the two proteins were purified by ammonium sulfate precipitation followed by reversed-phase HPLC and/or anion-exchange hydrophobic interaction chromatography and then subjected to immunoblot analysis. Purified P75 homologue and FBPA were positively bound by serum IgE from one and three, respectively, of the eight patients with shrimp-FDEIA, but not by sera from control subjects. Thus, P75 homologue and FBPA are identified as IgE-binding allergens for shrimp-FDEIA. These findings could be useful for the development of diagnostic tools and desensitization therapy for shrimp-FDEIA patients.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-021-84752-2