Purification of soybean cupins and comparison of IgE binding with peanut allergens in a population of allergic subjects
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 vicilin...
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| Veröffentlicht in: | Food and chemical toxicology 2021-01, Vol.147, p.111866-111866, Article 111866 |
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| container_title | Food and chemical toxicology |
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| creator | Ramadan, Samah Marsh, Justin El-Sherbeny, Ghada A. El-Halawany, El-Sayed F. Luan, Fulei Baumert, Joseph L. Johnson, Philip Osman, Yehia Goodman, Richard E. |
| description | 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. |
| doi_str_mv | 10.1016/j.fct.2020.111866 |
| format | Article |
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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.</description><identifier>ISSN: 0278-6915</identifier><identifier>EISSN: 1873-6351</identifier><identifier>DOI: 10.1016/j.fct.2020.111866</identifier><identifier>PMID: 33217527</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Antigens, Plant - chemistry ; Antigens, Plant - immunology ; Ara h 1 ; Ara h 2 ; Ara h 3 ; Ara h 6 ; Arachis - chemistry ; Chromatography, Liquid ; Cross Reactions ; Globulins - chemistry ; Gly m 5 ; Gly m 6 ; Glycine max - chemistry ; Humans ; IgE immunoblotting ; Immunoglobulin E ; LC-MS/MS ; Peanut Hypersensitivity ; Protein Binding ; Seed Storage Proteins - chemistry ; Soybean Proteins - chemistry ; Tandem Mass Spectrometry</subject><ispartof>Food and chemical toxicology, 2021-01, Vol.147, p.111866-111866, Article 111866</ispartof><rights>2020 Elsevier Ltd</rights><rights>Copyright © 2020 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c353t-de0446e1540ef83d8cc978d09e9ad26e3c063db6f3e0bdcd79067eeee0cb62193</citedby><cites>FETCH-LOGICAL-c353t-de0446e1540ef83d8cc978d09e9ad26e3c063db6f3e0bdcd79067eeee0cb62193</cites><orcidid>0000-0002-0462-8933 ; 0000-0003-0641-5437 ; 0000-0001-8243-2285</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.fct.2020.111866$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33217527$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ramadan, Samah</creatorcontrib><creatorcontrib>Marsh, Justin</creatorcontrib><creatorcontrib>El-Sherbeny, Ghada A.</creatorcontrib><creatorcontrib>El-Halawany, El-Sayed F.</creatorcontrib><creatorcontrib>Luan, Fulei</creatorcontrib><creatorcontrib>Baumert, Joseph L.</creatorcontrib><creatorcontrib>Johnson, Philip</creatorcontrib><creatorcontrib>Osman, Yehia</creatorcontrib><creatorcontrib>Goodman, Richard E.</creatorcontrib><title>Purification of soybean cupins and comparison of IgE binding with peanut allergens in a population of allergic subjects</title><title>Food and chemical toxicology</title><addtitle>Food Chem Toxicol</addtitle><description>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.</description><subject>Amino Acid Sequence</subject><subject>Antigens, Plant - chemistry</subject><subject>Antigens, Plant - immunology</subject><subject>Ara h 1</subject><subject>Ara h 2</subject><subject>Ara h 3</subject><subject>Ara h 6</subject><subject>Arachis - chemistry</subject><subject>Chromatography, Liquid</subject><subject>Cross Reactions</subject><subject>Globulins - chemistry</subject><subject>Gly m 5</subject><subject>Gly m 6</subject><subject>Glycine max - chemistry</subject><subject>Humans</subject><subject>IgE immunoblotting</subject><subject>Immunoglobulin E</subject><subject>LC-MS/MS</subject><subject>Peanut Hypersensitivity</subject><subject>Protein Binding</subject><subject>Seed Storage Proteins - chemistry</subject><subject>Soybean Proteins - chemistry</subject><subject>Tandem Mass Spectrometry</subject><issn>0278-6915</issn><issn>1873-6351</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFO4zAQhi3ECkqXB-CCfOSS4okbOxEnhMqChLR72D1bjj0prlI72Amob49RWI7MxRr5-39pPkIugK2AgbjerTozrkpW5h2gFuKILKCWvBC8gmOyYKWsC9FAdUrOUtoxxiRIcUJOOS9BVqVckLc_U3SdM3p0wdPQ0RQOLWpPzTQ4n6j2lpqwH3R0aQYetxvaOm-d39I3Nz7TIePTSHXfY9xizjhPNR3CMPVfrfOnMzRN7Q7NmH6SH53uE55_vkvy737z9-6hePr96_Hu9qkwvOJjYZGt1wKhWjPsam5rYxpZW9Zgo20pkBsmuG1Fx5G11ljZMCExDzOtKKHhS3I19w4xvEyYRrV3yWDfa49hSqpcCw45A5BRmFETQ0oROzVEt9fxoICpD99qp7Jv9eFbzb5z5vKzfmr3aL8S_wVn4GYGMB_56jCqZBx6g9bF7EHZ4L6pfwcgopKK</recordid><startdate>202101</startdate><enddate>202101</enddate><creator>Ramadan, Samah</creator><creator>Marsh, Justin</creator><creator>El-Sherbeny, Ghada A.</creator><creator>El-Halawany, El-Sayed F.</creator><creator>Luan, Fulei</creator><creator>Baumert, Joseph L.</creator><creator>Johnson, Philip</creator><creator>Osman, Yehia</creator><creator>Goodman, Richard E.</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-0462-8933</orcidid><orcidid>https://orcid.org/0000-0003-0641-5437</orcidid><orcidid>https://orcid.org/0000-0001-8243-2285</orcidid></search><sort><creationdate>202101</creationdate><title>Purification of soybean cupins and comparison of IgE binding with peanut allergens in a population of allergic subjects</title><author>Ramadan, Samah ; Marsh, Justin ; El-Sherbeny, Ghada A. ; El-Halawany, El-Sayed F. ; Luan, Fulei ; Baumert, Joseph L. ; Johnson, Philip ; Osman, Yehia ; Goodman, Richard E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c353t-de0446e1540ef83d8cc978d09e9ad26e3c063db6f3e0bdcd79067eeee0cb62193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Amino Acid Sequence</topic><topic>Antigens, Plant - chemistry</topic><topic>Antigens, Plant - immunology</topic><topic>Ara h 1</topic><topic>Ara h 2</topic><topic>Ara h 3</topic><topic>Ara h 6</topic><topic>Arachis - chemistry</topic><topic>Chromatography, Liquid</topic><topic>Cross Reactions</topic><topic>Globulins - chemistry</topic><topic>Gly m 5</topic><topic>Gly m 6</topic><topic>Glycine max - chemistry</topic><topic>Humans</topic><topic>IgE immunoblotting</topic><topic>Immunoglobulin E</topic><topic>LC-MS/MS</topic><topic>Peanut Hypersensitivity</topic><topic>Protein Binding</topic><topic>Seed Storage Proteins - chemistry</topic><topic>Soybean Proteins - chemistry</topic><topic>Tandem Mass Spectrometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ramadan, Samah</creatorcontrib><creatorcontrib>Marsh, Justin</creatorcontrib><creatorcontrib>El-Sherbeny, Ghada A.</creatorcontrib><creatorcontrib>El-Halawany, El-Sayed F.</creatorcontrib><creatorcontrib>Luan, Fulei</creatorcontrib><creatorcontrib>Baumert, Joseph L.</creatorcontrib><creatorcontrib>Johnson, Philip</creatorcontrib><creatorcontrib>Osman, Yehia</creatorcontrib><creatorcontrib>Goodman, Richard E.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Food and chemical toxicology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ramadan, Samah</au><au>Marsh, Justin</au><au>El-Sherbeny, Ghada A.</au><au>El-Halawany, El-Sayed F.</au><au>Luan, Fulei</au><au>Baumert, Joseph L.</au><au>Johnson, Philip</au><au>Osman, Yehia</au><au>Goodman, Richard E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification of soybean cupins and comparison of IgE binding with peanut allergens in a population of allergic subjects</atitle><jtitle>Food and chemical toxicology</jtitle><addtitle>Food Chem Toxicol</addtitle><date>2021-01</date><risdate>2021</risdate><volume>147</volume><spage>111866</spage><epage>111866</epage><pages>111866-111866</pages><artnum>111866</artnum><issn>0278-6915</issn><eissn>1873-6351</eissn><abstract>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). 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| subjects | Amino Acid Sequence Antigens, Plant - chemistry Antigens, Plant - immunology Ara h 1 Ara h 2 Ara h 3 Ara h 6 Arachis - chemistry Chromatography, Liquid Cross Reactions Globulins - chemistry Gly m 5 Gly m 6 Glycine max - chemistry Humans IgE immunoblotting Immunoglobulin E LC-MS/MS Peanut Hypersensitivity Protein Binding Seed Storage Proteins - chemistry Soybean Proteins - chemistry Tandem Mass Spectrometry |
| title | Purification of soybean cupins and comparison of IgE binding with peanut allergens in a population of allergic subjects |
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