Coordinated and standardized production, purification and characterization of natural and recombinant food allergens to establish a food allergen library

Abstract

Reliable diagnosis of food allergy is dependent on the analytes used. Approaches based on well-defined individual molecules of either natural or recombinant origin are likely to replace those based on food extracts in the future. Therefore, a library comprising well-characterized authentic natural and recombinant allergens was formed within the EC funded IP EuroPrevall. The advantages and disadvantages of including either natural or recombinant proteins are summarized, together with inclusion criteria such as purity and the implications of both allergenic and nonallergenic impurities for the performance of diagnostic assays. In order to harmonize quality criteria of the individual food allergens included in the library, as suite of characteristics and associated methodologies used to define them, was agreed. The application of these methods and impact on the quality and performance of the final purified food allergens included in the EuroPrevall allergen library is discussed.

Cloning, Expression and Patient IgE Reactivity of Recombinant Pru du 6, an 11S Globulin from Almond

“…Numerous studies have been directed toward the identification and immunological characterization of tree nut allergens [5,27,28,36,37,38,39,40,41,42]. An important approach in the analysis of allergens is the use of recombinant proteins, which have repeatedly shown their value in basic studies, diagnosis and the development of potential immunotherapeutic agents [for reviews, see [43,44,45,46,47]].…”

Expression of the soybean allergenic protein P34 in Escherichia coli and its indirect ELISA detection method

“…However, soybean is also one of the "the big eight" foods, identified as the most common sources of human food allergens, accounting for over 90 % of the documented food allergies worldwide (van Boxtel et al 2008;Batista et al 2007;Hoffmann-Sommergruber et al 2008;Yaklich et al 1999). Classic immunoglobulin-E (IgE)-mediated food allergies are classified as type-I immediate hypersensitivity reaction and around 1-2 % of adults and up to 5-7 % of children suffer from some type of food allergy with foods (Mills and Breiteneder 2005).…”

Responsiveness of the major birch allergen Bet v 1 scaffold to the gastric environment: Impact on structure and allergenic activity

“…Furthermore, there is evidence that interactions with lipid vesicles can protect Bet v 1 from proteolysis [6]. Thus, we have investigated the stability to gastric digestion of a panel of recombinant allergenic Bet v 1 homologues drawn from three different botanical families, the Rosaceae (Mal d 1, Pru p 1), Apiaceae (Api g 1) and Betulaceae (Cor a 1) available from the EuroPrevall allergen library [13]. Recombinant allergens were used in this study to provide sufficient quantities, since preparing them in a natural form from plant foods can be difficult due to their sometimes low abundance and lability.…”