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

Ana I. Sancho, Andrea Wangorsch, Bettina M. Jensen, Andrew Watson, Yuri Alexeev, Phil E. Johnson, Alan R. Mackie, Angela Neubauer, Gerald Reese, Barbara Ballmer-Weber, Karin Hoffmann-Sommergruber, Per S. Skov, Stefan Vieths, Elisabeth N Clare Mills

    Research output: Contribution to journalArticlepeer-review


    Scope: Four Bet v 1 homologous food allergens from celeriac (rApi g 1), apple (rMal d 1), peach (rPru p 1) and hazelnut (rCor a 1), were used to probe the structural responsiveness of the Bet v 1 scaffold to gastric digestion conditions and its impact on allergenicity. Methods and results: Low pH induced conformational changes of all homologues, which was reduced at physiological ionic strength for all except rPru p 1 as observed by circular dichroism (CD)-spectroscopy. The homologues were rapidly digested by pepsin, losing their IgE binding activity, although the kinetics and patterns of digestion varied subtly between homologues, rApi g 1 being the most stable. We have demonstrated for the first time that gastric phosphatidyl-choline (PC) induced conformational changes in all homologues but only rMal d 1 penetrated the PC vesicles as detected by fluorescence polarization, slowing its digestion and retaining more of its allergenic activity. PC enhanced basophil activation of all digested allergens except rApi g 1. Conclusion: The Bet v 1 scaffold is generally susceptible to low pH and pepsinolysis and interacts with PC vesicles, properties which can explain effects of the gastric environment on their allergenicity. These data show the importance of including surfactants in model digestion systems. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
    Original languageEnglish
    Pages (from-to)1690-1699
    Number of pages9
    JournalMolecular Nutrition and Food Research
    Issue number11
    Publication statusPublished - Nov 2011


    • Bet v 1 homologues
    • Food allergy
    • Lipid-protein interaction
    • Pepsinolysis
    • Phosphatidylcholine


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