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...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-02-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/28/4/1587 |
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| author | Christopher P. Mattison Zhongqi He Dunhua Zhang Rebecca Dupre Steven W. Lloyd |
| author_facet | Christopher P. Mattison Zhongqi He Dunhua Zhang Rebecca Dupre Steven W. Lloyd |
| author_sort | Christopher P. Mattison |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-11T08:22:05Z |
| format | Article |
| id | doaj.art-5d8a0340296346c18f352669a82e820e |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-11T08:22:05Z |
| publishDate | 2023-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-5d8a0340296346c18f352669a82e820e2023-11-16T22:20:32ZengMDPI AGMolecules1420-30492023-02-01284158710.3390/molecules28041587Cross-Serological Reaction of Glandless Cottonseed Proteins to Peanut and Tree Nut Allergic IgEChristopher P. Mattison0Zhongqi He1Dunhua Zhang2Rebecca Dupre3Steven W. Lloyd4USDA-ARS, Southern Regional Research Center, New Orleans, LA 70124, USAUSDA-ARS, Southern Regional Research Center, New Orleans, LA 70124, USAUSDA-ARS, Aquatic Animal Health Research Unit, Auburn, AL 36832, USAUSDA-ARS, Southern Regional Research Center, New Orleans, LA 70124, USAUSDA-ARS, Southern Regional Research Center, New Orleans, LA 70124, USAFood 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.https://www.mdpi.com/1420-3049/28/4/1587glandlesscottonseedcross-reactionvicilinleguminimmunoglobulin E (IgE) |
| spellingShingle | Christopher P. Mattison Zhongqi He Dunhua Zhang Rebecca Dupre Steven W. Lloyd Cross-Serological Reaction of Glandless Cottonseed Proteins to Peanut and Tree Nut Allergic IgE Molecules glandless cottonseed cross-reaction vicilin legumin immunoglobulin E (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 | glandless cottonseed cross-reaction vicilin legumin immunoglobulin E (IgE) |
| url | https://www.mdpi.com/1420-3049/28/4/1587 |
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