Immunoglobulin E cross-reactivity between lupine conglutins and peanut allergens in serum of lupine-allergic individuals
Lupine is used increasingly in food products. The development of lupine allergy in peanut-allergic patients is believed to occur as a result of cross-reactivity between lupine and peanut proteins. To investigate the degree of immunoglobulin (Ig) E cross-reactivity between allergens in lupine and pea...
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| Veröffentlicht in: | Journal of investigational allergology & clinical immunology 2009, Vol.19 (4), p.283-291 |
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| creator | Dooper, M M B W Plassen, C Holden, L Lindvik, H Faeste, C K |
| description | Lupine is used increasingly in food products. The development of lupine allergy in peanut-allergic patients is believed to occur as a result of cross-reactivity between lupine and peanut proteins.
To investigate the degree of immunoglobulin (Ig) E cross-reactivity between allergens in lupine and peanut.
We investigated IgE cross-reactivity between lupine alpha-, beta-, gamma-, and delta-conglutins and the major peanut allergens Ara h 1, Ara h 2 and Ara h 3 using enzyme-linked immunosorbent assay with sera from patients with coexisting peanut and lupine allergy.
Peanut proteins inhibited IgE binding towards alpha- conglutins, delta-conglutins, and, to a lesser degree, beta-conglutins, while no IgE cross-reaction with delta-conglutin was observed. Ara h 2 most potently inhibited IgE binding to lupine and delta-conglutins, while Ara h 1 most potently cross-reacted with beta-conglutin. Ara h 3 was apparently not involved in these mechanisms.
The present study reveals IgE cross-reactivity between the 2S albumins Ara h 2 and delta-conglutin, and the 7S vicilin-like Ara h 1 and beta-conglutin, which are possibly based on homologies between phylogenetically related proteins. Ara h 2 was the most potent inhibitor of IgE binding to lupine conglutins. |
| format | Article |
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To investigate the degree of immunoglobulin (Ig) E cross-reactivity between allergens in lupine and peanut.
We investigated IgE cross-reactivity between lupine alpha-, beta-, gamma-, and delta-conglutins and the major peanut allergens Ara h 1, Ara h 2 and Ara h 3 using enzyme-linked immunosorbent assay with sera from patients with coexisting peanut and lupine allergy.
Peanut proteins inhibited IgE binding towards alpha- conglutins, delta-conglutins, and, to a lesser degree, beta-conglutins, while no IgE cross-reaction with delta-conglutin was observed. Ara h 2 most potently inhibited IgE binding to lupine and delta-conglutins, while Ara h 1 most potently cross-reacted with beta-conglutin. Ara h 3 was apparently not involved in these mechanisms.
The present study reveals IgE cross-reactivity between the 2S albumins Ara h 2 and delta-conglutin, and the 7S vicilin-like Ara h 1 and beta-conglutin, which are possibly based on homologies between phylogenetically related proteins. Ara h 2 was the most potent inhibitor of IgE binding to lupine conglutins.</description><identifier>ISSN: 1018-9068</identifier><identifier>PMID: 19639724</identifier><language>eng</language><publisher>Spain</publisher><subject>2S Albumins, Plant - immunology ; Adolescent ; Allergens - immunology ; Antigens, Plant - immunology ; Arachis - immunology ; Arachis hypogaea ; Binding, Competitive ; Child ; Cross Reactions ; Enzyme-Linked Immunosorbent Assay ; Epitopes ; Female ; Food Hypersensitivity - blood ; Food Hypersensitivity - immunology ; Glycoproteins - immunology ; Humans ; Immunoglobulin E - blood ; Immunoglobulin E - immunology ; Lupinus - immunology ; Male ; Peanut Hypersensitivity - blood ; Peanut Hypersensitivity - immunology ; Plant Proteins - immunology ; Seed Storage Proteins - immunology ; Sequence Homology, Amino Acid</subject><ispartof>Journal of investigational allergology & clinical immunology, 2009, Vol.19 (4), p.283-291</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19639724$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dooper, M M B W</creatorcontrib><creatorcontrib>Plassen, C</creatorcontrib><creatorcontrib>Holden, L</creatorcontrib><creatorcontrib>Lindvik, H</creatorcontrib><creatorcontrib>Faeste, C K</creatorcontrib><title>Immunoglobulin E cross-reactivity between lupine conglutins and peanut allergens in serum of lupine-allergic individuals</title><title>Journal of investigational allergology & clinical immunology</title><addtitle>J Investig Allergol Clin Immunol</addtitle><description>Lupine is used increasingly in food products. The development of lupine allergy in peanut-allergic patients is believed to occur as a result of cross-reactivity between lupine and peanut proteins.
To investigate the degree of immunoglobulin (Ig) E cross-reactivity between allergens in lupine and peanut.
We investigated IgE cross-reactivity between lupine alpha-, beta-, gamma-, and delta-conglutins and the major peanut allergens Ara h 1, Ara h 2 and Ara h 3 using enzyme-linked immunosorbent assay with sera from patients with coexisting peanut and lupine allergy.
Peanut proteins inhibited IgE binding towards alpha- conglutins, delta-conglutins, and, to a lesser degree, beta-conglutins, while no IgE cross-reaction with delta-conglutin was observed. Ara h 2 most potently inhibited IgE binding to lupine and delta-conglutins, while Ara h 1 most potently cross-reacted with beta-conglutin. Ara h 3 was apparently not involved in these mechanisms.
The present study reveals IgE cross-reactivity between the 2S albumins Ara h 2 and delta-conglutin, and the 7S vicilin-like Ara h 1 and beta-conglutin, which are possibly based on homologies between phylogenetically related proteins. Ara h 2 was the most potent inhibitor of IgE binding to lupine conglutins.</description><subject>2S Albumins, Plant - immunology</subject><subject>Adolescent</subject><subject>Allergens - immunology</subject><subject>Antigens, Plant - immunology</subject><subject>Arachis - immunology</subject><subject>Arachis hypogaea</subject><subject>Binding, Competitive</subject><subject>Child</subject><subject>Cross Reactions</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Epitopes</subject><subject>Female</subject><subject>Food Hypersensitivity - blood</subject><subject>Food Hypersensitivity - immunology</subject><subject>Glycoproteins - immunology</subject><subject>Humans</subject><subject>Immunoglobulin E - blood</subject><subject>Immunoglobulin E - immunology</subject><subject>Lupinus - immunology</subject><subject>Male</subject><subject>Peanut Hypersensitivity - blood</subject><subject>Peanut Hypersensitivity - immunology</subject><subject>Plant Proteins - immunology</subject><subject>Seed Storage Proteins - immunology</subject><subject>Sequence Homology, Amino Acid</subject><issn>1018-9068</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kDtPwzAUhT2AaCn8BeQJpkh-xU5GVBWoVIkF5shJrisjxwl-AP33BLVdmY50z3e-4V6gJSW0KmoiqwW6jvGDEK5kpa7QgtaS14qJJfrZDkP2496NbXbW4w3uwhhjEUB3yX7ZdMAtpG8Aj12erAfcjX7vcrI-Yu17PIH2OWHtHIQ9zMdZEiHkAY_mNCmOpe3mrp-dfdYu3qBLMwfcnnKF3p82b-uXYvf6vF0_7oqJCZoKaLWUTJMWKiq5UYb2fa2p7CrGORVSm1qwjjLDKsEMFUxqVhJjakKppC3hK_Rw9E5h_MwQUzPY2IFz2sOYY6NEqQhh_I-8_5eUquRSknIG705gbgfomynYQYdDc_4q_wVrMHSb</recordid><startdate>2009</startdate><enddate>2009</enddate><creator>Dooper, M M B W</creator><creator>Plassen, C</creator><creator>Holden, L</creator><creator>Lindvik, H</creator><creator>Faeste, C K</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>7T5</scope><scope>H94</scope></search><sort><creationdate>2009</creationdate><title>Immunoglobulin E cross-reactivity between lupine conglutins and peanut allergens in serum of lupine-allergic individuals</title><author>Dooper, M M B W ; Plassen, C ; Holden, L ; Lindvik, H ; Faeste, C K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p241t-eba662a0be8163f7f1dd9a16c8233146af942c12f2842f1426a250ff901161b03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>2S Albumins, Plant - immunology</topic><topic>Adolescent</topic><topic>Allergens - immunology</topic><topic>Antigens, Plant - immunology</topic><topic>Arachis - immunology</topic><topic>Arachis hypogaea</topic><topic>Binding, Competitive</topic><topic>Child</topic><topic>Cross Reactions</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Epitopes</topic><topic>Female</topic><topic>Food Hypersensitivity - blood</topic><topic>Food Hypersensitivity - immunology</topic><topic>Glycoproteins - immunology</topic><topic>Humans</topic><topic>Immunoglobulin E - blood</topic><topic>Immunoglobulin E - immunology</topic><topic>Lupinus - immunology</topic><topic>Male</topic><topic>Peanut Hypersensitivity - blood</topic><topic>Peanut Hypersensitivity - immunology</topic><topic>Plant Proteins - immunology</topic><topic>Seed Storage Proteins - immunology</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dooper, M M B W</creatorcontrib><creatorcontrib>Plassen, C</creatorcontrib><creatorcontrib>Holden, L</creatorcontrib><creatorcontrib>Lindvik, H</creatorcontrib><creatorcontrib>Faeste, C K</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>Journal of investigational allergology & clinical immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dooper, M M B W</au><au>Plassen, C</au><au>Holden, L</au><au>Lindvik, H</au><au>Faeste, C K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immunoglobulin E cross-reactivity between lupine conglutins and peanut allergens in serum of lupine-allergic individuals</atitle><jtitle>Journal of investigational allergology & clinical immunology</jtitle><addtitle>J Investig Allergol Clin Immunol</addtitle><date>2009</date><risdate>2009</risdate><volume>19</volume><issue>4</issue><spage>283</spage><epage>291</epage><pages>283-291</pages><issn>1018-9068</issn><abstract>Lupine is used increasingly in food products. The development of lupine allergy in peanut-allergic patients is believed to occur as a result of cross-reactivity between lupine and peanut proteins.
To investigate the degree of immunoglobulin (Ig) E cross-reactivity between allergens in lupine and peanut.
We investigated IgE cross-reactivity between lupine alpha-, beta-, gamma-, and delta-conglutins and the major peanut allergens Ara h 1, Ara h 2 and Ara h 3 using enzyme-linked immunosorbent assay with sera from patients with coexisting peanut and lupine allergy.
Peanut proteins inhibited IgE binding towards alpha- conglutins, delta-conglutins, and, to a lesser degree, beta-conglutins, while no IgE cross-reaction with delta-conglutin was observed. Ara h 2 most potently inhibited IgE binding to lupine and delta-conglutins, while Ara h 1 most potently cross-reacted with beta-conglutin. Ara h 3 was apparently not involved in these mechanisms.
The present study reveals IgE cross-reactivity between the 2S albumins Ara h 2 and delta-conglutin, and the 7S vicilin-like Ara h 1 and beta-conglutin, which are possibly based on homologies between phylogenetically related proteins. Ara h 2 was the most potent inhibitor of IgE binding to lupine conglutins.</abstract><cop>Spain</cop><pmid>19639724</pmid><tpages>9</tpages></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | 2S Albumins, Plant - immunology Adolescent Allergens - immunology Antigens, Plant - immunology Arachis - immunology Arachis hypogaea Binding, Competitive Child Cross Reactions Enzyme-Linked Immunosorbent Assay Epitopes Female Food Hypersensitivity - blood Food Hypersensitivity - immunology Glycoproteins - immunology Humans Immunoglobulin E - blood Immunoglobulin E - immunology Lupinus - immunology Male Peanut Hypersensitivity - blood Peanut Hypersensitivity - immunology Plant Proteins - immunology Seed Storage Proteins - immunology Sequence Homology, Amino Acid |
| title | Immunoglobulin E cross-reactivity between lupine conglutins and peanut allergens in serum of lupine-allergic individuals |
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