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
Hauptverfasser: Akkerdaas, Jaap H., Wensing, Marjolein, Asero, Riccardo, Rivas, Montserrat Fernandez, Knulst, André C., Bolhaar, Suzanne, Hefle, Susan L., Aalberse, Rob C., van Ree, Ronald
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container_end_page 208
container_issue 3
container_start_page 203
container_title International Archives of Allergy and Immunology
container_volume 138
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
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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. 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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. 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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.</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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source MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; Karger Journals; IngentaConnect Free/Open Access Journals; PubMed Central; Alma/SFX Local Collection
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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