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 journalArticle

16 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1690-1699
Number of pages10
JournalMolecular Nutrition and Food Research
Volume55
Issue number11
DOIs
StatePublished - Nov 1 2011

    Fingerprint

Keywords

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

ASJC Scopus subject areas

  • Biotechnology
  • Food Science

Cite this

Sancho, A. I., Wangorsch, A., Jensen, B. M., Watson, A., Alexeev, Y., Johnson, P. E., Mackie, A. R., Neubauer, A., Reese, G., Ballmer-Weber, B., Hoffmann-Sommergruber, K., Skov, P. S., Vieths, S., & Mills, E. N. C. (2011). Responsiveness of the major birch allergen Bet v 1 scaffold to the gastric environment: Impact on structure and allergenic activity. Molecular Nutrition and Food Research, 55(11), 1690-1699. https://doi.org/10.1002/mnfr.201100025