Cargando…

Cross-Serological Reaction of Glandless Cottonseed Proteins to Peanut and Tree Nut Allergic IgE

Food allergy is a potentially life-threatening health concern caused by immunoglobulin E (IgE) antibodies that mistakenly recognize normally harmless food proteins as threats. Peanuts and tree nuts contain several seed storage proteins that commonly act as allergens. Glandless cottonseed, lacking th...

Descripción completa

Detalles Bibliográficos
Autores principales: Mattison, Christopher P., He, Zhongqi, Zhang, Dunhua, Dupre, Rebecca, Lloyd, Steven W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9967559/
https://www.ncbi.nlm.nih.gov/pubmed/36838575
http://dx.doi.org/10.3390/molecules28041587
_version_ 1784897294896726016
author Mattison, Christopher P.
He, Zhongqi
Zhang, Dunhua
Dupre, Rebecca
Lloyd, Steven W.
author_facet Mattison, Christopher P.
He, Zhongqi
Zhang, Dunhua
Dupre, Rebecca
Lloyd, Steven W.
author_sort Mattison, Christopher P.
collection PubMed
description Food allergy is a potentially life-threatening health concern caused by immunoglobulin E (IgE) antibodies that mistakenly recognize normally harmless food proteins as threats. Peanuts and tree nuts contain several seed storage proteins that commonly act as allergens. Glandless cottonseed, lacking the toxic compound gossypol, is a new food source. However, the seed storage proteins in cottonseed may act as allergens. To assess this risk, glandless cottonseed protein extracts were evaluated for IgE binding by peanut and tree nut allergic volunteers. ELISA demonstrated that 25% of 32 samples had significant binding to cottonseed extracts. Immunoblot analysis with pooled sera indicated that IgE recognized a pair of bands migrating at approximately 50 kDa. Excision of these bands and subsequent mass-spectrometric analysis demonstrated peptide matches to cotton C72 and GC72 vicilin and legumin A and B proteins. Further, in silico analysis indicated similarity of the cotton vicilin and legumin proteins to peanut vicilin (Ara h 1) and cashew nut legumin (Ana o 2) IgE-binding epitopes among others. The observations suggest both the cotton vicilin and legumin proteins were recognized by the nut allergic IgE, and they should be considered for future allergen risk assessments evaluating glandless cottonseed protein products.
format Online
Article
Text
id pubmed-9967559
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-99675592023-02-27 Cross-Serological Reaction of Glandless Cottonseed Proteins to Peanut and Tree Nut Allergic IgE Mattison, Christopher P. He, Zhongqi Zhang, Dunhua Dupre, Rebecca Lloyd, Steven W. Molecules Article Food allergy is a potentially life-threatening health concern caused by immunoglobulin E (IgE) antibodies that mistakenly recognize normally harmless food proteins as threats. Peanuts and tree nuts contain several seed storage proteins that commonly act as allergens. Glandless cottonseed, lacking the toxic compound gossypol, is a new food source. However, the seed storage proteins in cottonseed may act as allergens. To assess this risk, glandless cottonseed protein extracts were evaluated for IgE binding by peanut and tree nut allergic volunteers. ELISA demonstrated that 25% of 32 samples had significant binding to cottonseed extracts. Immunoblot analysis with pooled sera indicated that IgE recognized a pair of bands migrating at approximately 50 kDa. Excision of these bands and subsequent mass-spectrometric analysis demonstrated peptide matches to cotton C72 and GC72 vicilin and legumin A and B proteins. Further, in silico analysis indicated similarity of the cotton vicilin and legumin proteins to peanut vicilin (Ara h 1) and cashew nut legumin (Ana o 2) IgE-binding epitopes among others. The observations suggest both the cotton vicilin and legumin proteins were recognized by the nut allergic IgE, and they should be considered for future allergen risk assessments evaluating glandless cottonseed protein products. MDPI 2023-02-07 /pmc/articles/PMC9967559/ /pubmed/36838575 http://dx.doi.org/10.3390/molecules28041587 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Mattison, Christopher P.
He, Zhongqi
Zhang, Dunhua
Dupre, Rebecca
Lloyd, Steven W.
Cross-Serological Reaction of Glandless Cottonseed Proteins to Peanut and Tree Nut Allergic IgE
title Cross-Serological Reaction of Glandless Cottonseed Proteins to Peanut and Tree Nut Allergic IgE
title_full Cross-Serological Reaction of Glandless Cottonseed Proteins to Peanut and Tree Nut Allergic IgE
title_fullStr Cross-Serological Reaction of Glandless Cottonseed Proteins to Peanut and Tree Nut Allergic IgE
title_full_unstemmed Cross-Serological Reaction of Glandless Cottonseed Proteins to Peanut and Tree Nut Allergic IgE
title_short Cross-Serological Reaction of Glandless Cottonseed Proteins to Peanut and Tree Nut Allergic IgE
title_sort cross-serological reaction of glandless cottonseed proteins to peanut and tree nut allergic ige
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9967559/
https://www.ncbi.nlm.nih.gov/pubmed/36838575
http://dx.doi.org/10.3390/molecules28041587
work_keys_str_mv AT mattisonchristopherp crossserologicalreactionofglandlesscottonseedproteinstopeanutandtreenutallergicige
AT hezhongqi crossserologicalreactionofglandlesscottonseedproteinstopeanutandtreenutallergicige
AT zhangdunhua crossserologicalreactionofglandlesscottonseedproteinstopeanutandtreenutallergicige
AT duprerebecca crossserologicalreactionofglandlesscottonseedproteinstopeanutandtreenutallergicige
AT lloydstevenw crossserologicalreactionofglandlesscottonseedproteinstopeanutandtreenutallergicige