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Immediate-type hypersensitivity reaction to ingestion of mycoprotein (Quorn) in a patient allergic to molds caused by acidic ribosomal protein P2 - 29/08/11

Doi : 10.1067/mai.2003.1339 
Michael Hoff, MSca, Ralph M. Trüeb, MDb, Barbara K. Ballmer-Weber, MDb, Stefan Vieths, PhDa, Brunello Wuethrich, MDb
Langen, Germany, and Zurich, Switzerland 
From the a Department of Allergology, Paul-Ehrlich-Institut, Langen, Germany; and the b Allergy Unit, Department of Dermatology, University Hospital of Zurich, Zurich, Switzerland 

Abstract

Background: Quorn is the brand name for a line of foods made with so-called “mycoprotein,” which springs from the mold Fusarium venenatum . Since the introduction on the food market, there have been complaints from consumers reporting adverse gastrointestinal reactions after ingestion of mycoprotein. To date, it is not clear whether the reported symptoms are IgE-mediated. Objective: The aim of the study was to describe for the first time a case history of an asthmatic patient with severe hypersensitivity reactions to ingested mycoprotein and to identify and characterize the potential allergen that might be responsible for this. Methods: The sensitization pattern of the asthmatic subject was characterized, and food allergy to mycoprotein was assessed by double-blinded placebo-controlled food challenge. Afterward, specific IgE antibodies of the serum of this patient were used to screen a Fusarium culmorum cDNA expression library. The coding sequence of one enriched cDNA-clone was expressed in Escherichia coli to produce a recombinant protein that was further purified and immunologically characterized. Results: The patient showed high sensitization to many known aeroallergens but apart from Quorn not to any other tested food samples. The deduced amino acid sequence of the enriched cDNA-clone (Fus c 1) showed large identity to the 60S acidic ribosomal protein P2 which is highly conserved among several species and also described as minor allergen in other mold species. The frequency of IgE reactivity of sera from F culmorum -sensitized subjects to rFus c 1 was approximately 35%. By enzyme allergosorbent test inhibition, we found 65% inhibition of mycoprotein IgE reactivity by rFus c 1 . On the opposite we found reduced IgE reactivity of rFus c 1 of 68% by using mycoprotein as inhibitor. Conclusions: Sensitization to mold allergens by the respiratory tract and subsequent oral ingestion of cross-reactive proteins may lead to severe food-allergic reactions. Thus, the 60S acidic ribosomal protein P2 of F venenatum probably is the reason for the described severe hypersensitivity reactions of the patient to Quorn-mycoprotein because of its potential cross-reactivity to the F culmorum allergen Fus c 1. (J Allergy Clin Immunol 2003;111:1106-10.)

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Keywords : Case report, mold allergy, food allergy, cross-reactivity, DBPCFC, recombinant allergen

Abbreviations : DBPCFC, EAST, SPT


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 Supported by grant 115-1720-1/11 of the German Federal Ministry of Health.
 Reprint requests: Stefan Vieths, PhD, Paul-Ehrlich-Institut, Department of Allergology, Paul-Ehrlich-Str 51-59, D-63225 Langen, Germany.


© 2003  Mosby, Inc. Reservados todos los derechos.
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Vol 111 - N° 5

P. 1106-1110 - mai 2003 Regresar al número
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