Purification of soybean cupins and comparison of IgE binding with peanut allergens in a population of allergic subjects
Copyright © 2020 Elsevier Ltd. All rights reserved..
Identification, purification and characterization of allergens is crucial to the understanding of IgE-mediated disease. Immunologic and structural studies with purified allergens is essential for understanding relative immunogenicity and cross-reactivity. In this work, the complex soybean 7S vicilins (Gly m 5) with three subunits and 11S legumins (Gly m 6) with five subunits were purified and characterized along with purified peanut allergens (Ara h 1, 2, 3, and 6) by label-free liquid chromatography-tandem mass spectrometry (LC-MS/MS). Individual subjects plasma IgE binding was tested from subjects allergic to soybeans and or peanuts by immunoblotting, ImmunoCAP™ and ISAC™ ImmunoCAP chip, comparing these soybean proteins with those of purified peanut allergens; vicilin (Ara h 1), 2S albumin (Ara h 2 and Ara h 6) and 11S globulin (Ara h 3). Results show differences between methods and subjects demonstrating the complexity of finding answers to questions of cross-reactivity.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:147 |
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| Enthalten in: |
Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association - 147(2021) vom: 03. Jan., Seite 111866 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Ramadan, Samah [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 14.06.2021 Date Revised 13.12.2023 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.fct.2020.111866 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM317845748 |
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| 520 | |a Copyright © 2020 Elsevier Ltd. All rights reserved. | ||
| 520 | |a Identification, purification and characterization of allergens is crucial to the understanding of IgE-mediated disease. Immunologic and structural studies with purified allergens is essential for understanding relative immunogenicity and cross-reactivity. In this work, the complex soybean 7S vicilins (Gly m 5) with three subunits and 11S legumins (Gly m 6) with five subunits were purified and characterized along with purified peanut allergens (Ara h 1, 2, 3, and 6) by label-free liquid chromatography-tandem mass spectrometry (LC-MS/MS). Individual subjects plasma IgE binding was tested from subjects allergic to soybeans and or peanuts by immunoblotting, ImmunoCAP™ and ISAC™ ImmunoCAP chip, comparing these soybean proteins with those of purified peanut allergens; vicilin (Ara h 1), 2S albumin (Ara h 2 and Ara h 6) and 11S globulin (Ara h 3). Results show differences between methods and subjects demonstrating the complexity of finding answers to questions of cross-reactivity | ||
| 650 | 4 | |a Journal Article | |
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| 650 | 7 | |a Antigens, Plant |2 NLM | |
| 650 | 7 | |a Globulins |2 NLM | |
| 650 | 7 | |a Seed Storage Proteins |2 NLM | |
| 650 | 7 | |a Soybean Proteins |2 NLM | |
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| 700 | 1 | |a El-Halawany, El-Sayed F |e verfasserin |4 aut | |
| 700 | 1 | |a Luan, Fulei |e verfasserin |4 aut | |
| 700 | 1 | |a Baumert, Joseph L |e verfasserin |4 aut | |
| 700 | 1 | |a Johnson, Philip |e verfasserin |4 aut | |
| 700 | 1 | |a Osman, Yehia |e verfasserin |4 aut | |
| 700 | 1 | |a Goodman, Richard E |e verfasserin |4 aut | |
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