IgE Binding to Pepsin-Digested Food Extracts
Background: Pepsin resistance of allergens like lipid transfer protein and 2S albumin has been suggested as explanation for the severity of symptoms often induced by these allergens. Component-resolved diagnosis with purified labile and stable allergens has therefore been proposed to better characte...
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Veröffentlicht in: | International Archives of Allergy and Immunology 2005-11, Vol.138 (3), p.203-208 |
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creator | Akkerdaas, Jaap H. Wensing, Marjolein Asero, Riccardo Rivas, Montserrat Fernandez Knulst, André C. Bolhaar, Suzanne Hefle, Susan L. Aalberse, Rob C. van Ree, Ronald |
description | Background: Pepsin resistance of allergens like lipid transfer protein and 2S albumin has been suggested as explanation for the severity of symptoms often induced by these allergens. Component-resolved diagnosis with purified labile and stable allergens has therefore been proposed to better characterize the risk involved in a positive in vitroIgE test. However, for many foods, purified allergens are not (yet) available. Objective: It was the aim of this study to evaluate the potential of pepsin-digested whole-food extracts to distinguish between IgE responses to stable (potentially severe) and labile (mild) allergens. Methods: Sera (n = 143) from Italian, Spanish and Dutch patients with hazelnut and/or apple ingestion-related symptoms were analyzed for residual IgE binding to pepsin-resistant hazelnut and/or apple allergens. Control and pepsin-digested hazelnut and apple extracts were used for radioallergosorbent test analysis and immunoblot analysis. Results: Pepsin digestion of food extracts, like from hazelnut and apple used for in vitro diagnostic tests, provides a way to distinguish sensitization to pepsin-resistant allergens from that to pepsin-susceptible allergens. In this selected group of patients, IgE reactivity to pepsin-digested extracts correlated with sensitization to the stable allergen lipid transfer protein. The analysis further revealed that the use of soluble pepsin can result in false-positive in vitro tests (2/143). Conclusion: Pepsin-digested food extracts are a convenient tool to identify patients with IgE antibodies against potentially dangerous stable allergens, in particular for those foods where the relevant stable allergens have not yet been identified. This can increase the clinical prognostic value of food allergy serology. |
doi_str_mv | 10.1159/000088720 |
format | Article |
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Component-resolved diagnosis with purified labile and stable allergens has therefore been proposed to better characterize the risk involved in a positive in vitroIgE test. However, for many foods, purified allergens are not (yet) available. Objective: It was the aim of this study to evaluate the potential of pepsin-digested whole-food extracts to distinguish between IgE responses to stable (potentially severe) and labile (mild) allergens. Methods: Sera (n = 143) from Italian, Spanish and Dutch patients with hazelnut and/or apple ingestion-related symptoms were analyzed for residual IgE binding to pepsin-resistant hazelnut and/or apple allergens. Control and pepsin-digested hazelnut and apple extracts were used for radioallergosorbent test analysis and immunoblot analysis. Results: Pepsin digestion of food extracts, like from hazelnut and apple used for in vitro diagnostic tests, provides a way to distinguish sensitization to pepsin-resistant allergens from that to pepsin-susceptible allergens. In this selected group of patients, IgE reactivity to pepsin-digested extracts correlated with sensitization to the stable allergen lipid transfer protein. The analysis further revealed that the use of soluble pepsin can result in false-positive in vitro tests (2/143). Conclusion: Pepsin-digested food extracts are a convenient tool to identify patients with IgE antibodies against potentially dangerous stable allergens, in particular for those foods where the relevant stable allergens have not yet been identified. This can increase the clinical prognostic value of food allergy serology.</description><identifier>ISSN: 1018-2438</identifier><identifier>EISSN: 1423-0097</identifier><identifier>EISSN: 1365-2567</identifier><identifier>DOI: 10.1159/000088720</identifier><identifier>PMID: 16205098</identifier><language>eng</language><publisher>Basel, Switzerland: Karger</publisher><subject>Allergens - analysis ; Allergens - immunology ; Allergens - metabolism ; Allergic diseases ; Allergies ; Biological and medical sciences ; Diagnostic tests ; Digestive allergic diseases ; Enzymes ; Food ; Food Hypersensitivity - immunology ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Humans ; Immunoglobulin E - immunology ; Immunopathology ; Malus ; Malus - immunology ; Medical sciences ; Nut Hypersensitivity - immunology ; Nuts - immunology ; Original Paper ; Pepsin A - metabolism ; Proteins ; Radioallergosorbent Test</subject><ispartof>International Archives of Allergy and Immunology, 2005-11, Vol.138 (3), p.203-208</ispartof><rights>2005 S. Karger AG, Basel</rights><rights>2005 INIST-CNRS</rights><rights>Copyright (c) 2005 S. Karger AG, Basel.</rights><rights>Copyright (c) 2005 S. Karger AG, Basel</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-99bc3597facbe265a96d6abd701a44c369b1eedadb987f0b66d4bdc4d4ce34113</citedby><cites>FETCH-LOGICAL-c391t-99bc3597facbe265a96d6abd701a44c369b1eedadb987f0b66d4bdc4d4ce34113</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,2423,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17224271$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16205098$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Akkerdaas, Jaap H.</creatorcontrib><creatorcontrib>Wensing, Marjolein</creatorcontrib><creatorcontrib>Asero, Riccardo</creatorcontrib><creatorcontrib>Rivas, Montserrat Fernandez</creatorcontrib><creatorcontrib>Knulst, André C.</creatorcontrib><creatorcontrib>Bolhaar, Suzanne</creatorcontrib><creatorcontrib>Hefle, Susan L.</creatorcontrib><creatorcontrib>Aalberse, Rob C.</creatorcontrib><creatorcontrib>van Ree, Ronald</creatorcontrib><title>IgE Binding to Pepsin-Digested Food Extracts</title><title>International Archives of Allergy and Immunology</title><addtitle>Int Arch Allergy Immunol</addtitle><description>Background: Pepsin resistance of allergens like lipid transfer protein and 2S albumin has been suggested as explanation for the severity of symptoms often induced by these allergens. Component-resolved diagnosis with purified labile and stable allergens has therefore been proposed to better characterize the risk involved in a positive in vitroIgE test. However, for many foods, purified allergens are not (yet) available. Objective: It was the aim of this study to evaluate the potential of pepsin-digested whole-food extracts to distinguish between IgE responses to stable (potentially severe) and labile (mild) allergens. Methods: Sera (n = 143) from Italian, Spanish and Dutch patients with hazelnut and/or apple ingestion-related symptoms were analyzed for residual IgE binding to pepsin-resistant hazelnut and/or apple allergens. Control and pepsin-digested hazelnut and apple extracts were used for radioallergosorbent test analysis and immunoblot analysis. Results: Pepsin digestion of food extracts, like from hazelnut and apple used for in vitro diagnostic tests, provides a way to distinguish sensitization to pepsin-resistant allergens from that to pepsin-susceptible allergens. In this selected group of patients, IgE reactivity to pepsin-digested extracts correlated with sensitization to the stable allergen lipid transfer protein. The analysis further revealed that the use of soluble pepsin can result in false-positive in vitro tests (2/143). Conclusion: Pepsin-digested food extracts are a convenient tool to identify patients with IgE antibodies against potentially dangerous stable allergens, in particular for those foods where the relevant stable allergens have not yet been identified. This can increase the clinical prognostic value of food allergy serology.</description><subject>Allergens - analysis</subject><subject>Allergens - immunology</subject><subject>Allergens - metabolism</subject><subject>Allergic diseases</subject><subject>Allergies</subject><subject>Biological and medical sciences</subject><subject>Diagnostic tests</subject><subject>Digestive allergic diseases</subject><subject>Enzymes</subject><subject>Food</subject><subject>Food Hypersensitivity - immunology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Humans</subject><subject>Immunoglobulin E - immunology</subject><subject>Immunopathology</subject><subject>Malus</subject><subject>Malus - immunology</subject><subject>Medical sciences</subject><subject>Nut Hypersensitivity - immunology</subject><subject>Nuts - immunology</subject><subject>Original Paper</subject><subject>Pepsin A - metabolism</subject><subject>Proteins</subject><subject>Radioallergosorbent Test</subject><issn>1018-2438</issn><issn>1423-0097</issn><issn>1365-2567</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqF0M1LwzAYBvAgipvTg2dBiqAgWM1X83HUuelgoAc9lzRJS-fWzqQF_e_NbNnAi7m8Ofx4kvcB4BTBW4QSeQfDEYJjuAeGiGISQyj5frhDJGJMiRiAI-8XEAYs2CEYIIZhAqUYgptZMYkeysqUVRE1dfRq176s4seysL6xJprWtYkmX41TuvHH4CBXS29P-jkC79PJ2_g5nr88zcb381gTiZpYykyTRPJc6cxilijJDFOZ4RApSjVhMkPWGmUyKXgOM8YMzYymhmpLKEJkBK663LWrP9vwkXRVem2XS1XZuvUpE5xwCsm_EHGcCIFxgBd_4KJuXRWWSDFGAmL0m3bdIe1q753N07UrV8p9pwimm6LTbdHBnveBbbayZif7ZgO47IHyWi1zpypd-p3jGFPMN7uede5DucK6Leie-QEaO4sL</recordid><startdate>200511</startdate><enddate>200511</enddate><creator>Akkerdaas, Jaap H.</creator><creator>Wensing, Marjolein</creator><creator>Asero, Riccardo</creator><creator>Rivas, Montserrat Fernandez</creator><creator>Knulst, André C.</creator><creator>Bolhaar, Suzanne</creator><creator>Hefle, Susan L.</creator><creator>Aalberse, Rob C.</creator><creator>van Ree, Ronald</creator><general>Karger</general><general>S. Karger AG</general><scope>IQODW</scope><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>3V.</scope><scope>7T5</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>200511</creationdate><title>IgE Binding to Pepsin-Digested Food Extracts</title><author>Akkerdaas, Jaap H. ; Wensing, Marjolein ; Asero, Riccardo ; Rivas, Montserrat Fernandez ; Knulst, André C. ; Bolhaar, Suzanne ; Hefle, Susan L. ; Aalberse, Rob C. ; van Ree, Ronald</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-99bc3597facbe265a96d6abd701a44c369b1eedadb987f0b66d4bdc4d4ce34113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Allergens - analysis</topic><topic>Allergens - immunology</topic><topic>Allergens - metabolism</topic><topic>Allergic diseases</topic><topic>Allergies</topic><topic>Biological and medical sciences</topic><topic>Diagnostic tests</topic><topic>Digestive allergic diseases</topic><topic>Enzymes</topic><topic>Food</topic><topic>Food Hypersensitivity - immunology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Humans</topic><topic>Immunoglobulin E - immunology</topic><topic>Immunopathology</topic><topic>Malus</topic><topic>Malus - immunology</topic><topic>Medical sciences</topic><topic>Nut Hypersensitivity - immunology</topic><topic>Nuts - immunology</topic><topic>Original Paper</topic><topic>Pepsin A - metabolism</topic><topic>Proteins</topic><topic>Radioallergosorbent Test</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Akkerdaas, Jaap H.</creatorcontrib><creatorcontrib>Wensing, Marjolein</creatorcontrib><creatorcontrib>Asero, Riccardo</creatorcontrib><creatorcontrib>Rivas, Montserrat Fernandez</creatorcontrib><creatorcontrib>Knulst, André C.</creatorcontrib><creatorcontrib>Bolhaar, Suzanne</creatorcontrib><creatorcontrib>Hefle, Susan L.</creatorcontrib><creatorcontrib>Aalberse, Rob C.</creatorcontrib><creatorcontrib>van Ree, Ronald</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Immunology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>International Archives of Allergy and Immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Akkerdaas, Jaap H.</au><au>Wensing, Marjolein</au><au>Asero, Riccardo</au><au>Rivas, Montserrat Fernandez</au><au>Knulst, André C.</au><au>Bolhaar, Suzanne</au><au>Hefle, Susan L.</au><au>Aalberse, Rob C.</au><au>van Ree, Ronald</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>IgE Binding to Pepsin-Digested Food Extracts</atitle><jtitle>International Archives of Allergy and Immunology</jtitle><addtitle>Int Arch Allergy Immunol</addtitle><date>2005-11</date><risdate>2005</risdate><volume>138</volume><issue>3</issue><spage>203</spage><epage>208</epage><pages>203-208</pages><issn>1018-2438</issn><eissn>1423-0097</eissn><eissn>1365-2567</eissn><abstract>Background: Pepsin resistance of allergens like lipid transfer protein and 2S albumin has been suggested as explanation for the severity of symptoms often induced by these allergens. Component-resolved diagnosis with purified labile and stable allergens has therefore been proposed to better characterize the risk involved in a positive in vitroIgE test. However, for many foods, purified allergens are not (yet) available. Objective: It was the aim of this study to evaluate the potential of pepsin-digested whole-food extracts to distinguish between IgE responses to stable (potentially severe) and labile (mild) allergens. Methods: Sera (n = 143) from Italian, Spanish and Dutch patients with hazelnut and/or apple ingestion-related symptoms were analyzed for residual IgE binding to pepsin-resistant hazelnut and/or apple allergens. Control and pepsin-digested hazelnut and apple extracts were used for radioallergosorbent test analysis and immunoblot analysis. Results: Pepsin digestion of food extracts, like from hazelnut and apple used for in vitro diagnostic tests, provides a way to distinguish sensitization to pepsin-resistant allergens from that to pepsin-susceptible allergens. In this selected group of patients, IgE reactivity to pepsin-digested extracts correlated with sensitization to the stable allergen lipid transfer protein. The analysis further revealed that the use of soluble pepsin can result in false-positive in vitro tests (2/143). Conclusion: Pepsin-digested food extracts are a convenient tool to identify patients with IgE antibodies against potentially dangerous stable allergens, in particular for those foods where the relevant stable allergens have not yet been identified. This can increase the clinical prognostic value of food allergy serology.</abstract><cop>Basel, Switzerland</cop><pub>Karger</pub><pmid>16205098</pmid><doi>10.1159/000088720</doi><tpages>6</tpages></addata></record> |
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subjects | Allergens - analysis Allergens - immunology Allergens - metabolism Allergic diseases Allergies Biological and medical sciences Diagnostic tests Digestive allergic diseases Enzymes Food Food Hypersensitivity - immunology Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Immunoglobulin E - immunology Immunopathology Malus Malus - immunology Medical sciences Nut Hypersensitivity - immunology Nuts - immunology Original Paper Pepsin A - metabolism Proteins Radioallergosorbent Test |
title | IgE Binding to Pepsin-Digested Food Extracts |
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