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Quantitative IgE inhibition experiments with purified recombinant allergens indicate pollen-derived allergens as the sensitizing agents responsible for many forms of plant food allergy - 04/09/11

Doi : 10.1016/S0091-6749(00)90186-6 
Lili Kazemi-Shirazi, MDa,b, Gabrielle Pauli, MDd, Ashok Purohit, MDd, Susanne Spitzauer, MDc, Renate Fröschlc, Karin Hoffmann-Sommergruber, PhDa, Heimo Breiteneder, PhDa, Otto Scheiner, PhDa, Dietrich Kraft, MDa, Rudolf Valenta, MDa
Vienna, Austria, and Strasbourg, France 
From athe Institute of General and Experimental Pathology, bthe Department of Internal Medicine IV, Division of Gastroenterology and Hepatology, and cthe Clinical Institute of Medical and Chemical Laboratory Diagnostics, AKH, University of Vienna; and dService de Pneumologie and INSERM U-425, Hospital Civil, University of Strasbourg 

Abstract

Background: Type I allergic symptoms in the oropharyngeal mucosa upon contact with plant-derived food in patients with pollen allergies have been termed oral allergy syndrome (OAS). IgE cross-reactivity between pollen and food allergens represents the molecular basis for this phenomenon. The sensitizing allergen source (pollen or plant food) in OAS is a controversial issue. Objective: We sought to determine the primary sensitizing molecules in patients with OAS. Methods: We used recombinant birch pollen (rBet v 1 and rBet v 2) and plant food allergens (apple, rMal d 1; celery, rApi g 1; and carrot, rDau c 1), as well as natural pollen (birch and timothy grass) and plant food (apple, peach, kiwi, hazelnut, celery, and carrot) allergens, to identify cross-reactive allergens by using qualitative immunoblot inhibitions. In addition, we determined the percentage of plant food–specific IgE that can be preadsorbed with recombinant and natural pollen allergens by quantitative RAST inhibitions by using sera from 71 patients with OAS. Results: Preincubation of sera with recombinant and natural pollen allergens led to an almost complete inhibition of IgE binding to plant food allergens in Western blots, as well as in RAST inhibition experiments. In contrast, recombinant plant food allergens poorly inhibited IgE binding to Bet v 1. Conclusion: Most IgE epitopes in plant food recognized by patients with OAS are resembled by pollen allergens. Thus pollen allergens may be responsible for the elicitation and maintenance of OAS. (J Allergy Clin Immunol 2000;105:116-25.)

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Keywords : Food allergy, pollen allergy, cross-reactivity, recombinant allergens

Abbreviations : OAS:


Esquema


 Supported by a grant of the Austrian Ministry of Science and Transport, by grant Y078GEN of the Austrian Science Fund, and by the Interdisciplinary Cooperative Project program of the Austrian Ministry of Science and Transport.
 Reprint requests: Rudolf Valenta, MD, Molecular Immunopathology Group, Institute of General and Experimental Pathology, University of Vienna, Medical School, Vienna General Hospital, Waehringer Guertel 18-20, A-1090 Vienna, Austria.
 0091-6749/2000 $12.00 + 0  1/1/102872


© 2000  Mosby, Inc. Reservados todos los derechos.
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Vol 105 - N° 1P1

P. 116-125 - janvier 2000 Regresar al número
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