at Google ScholarTitle data
Neudecker, Philipp ; Schweimer, Kristian ; Nerkamp, Jörg ; Scheurer, Stephan ; Vieths, Stefan ; Sticht, Heinrich ; Rösch, Paul:
Allergic cross-reactivity made visible : solution structure of the major cherry allergen Pru av 1.
In: The Journal of Biological Chemistry.
Vol. 276
(2001)
Issue 25
.
- pp. 22756-22763.
ISSN 1083-351X
DOI: https://doi.org/10.1074/jbc.M101657200
Abstract in another language
Birch pollinosis is often accompanied by hypersensi- tivity to fruit as a consequence of the cross-reaction of pollen allergen-specific IgE antibodies with homologous food proteins. To provide a basis for examining the cross-reactivity on a structural level, we used hetero- nuclear multidimensional NMR spectroscopy to deter- mine the high-resolution three-dimensional structure of the major cherry allergen, Pru av 1, in solution. Based on a detailed comparison of the virtually identical struc- tures of Pru av 1 and Bet v 1, the major birch pollen allergen, we propose an explanation for a significant aspect of the observed cross-reactivity pattern among the family of allergens under consideration. The large hydrophobic cavity expected to be important for the still unknown physiological function of Bet v 1 is con- served in Pru av 1. Structural homology to a domain of human MLN64 associated with cholesterol transport suggests phytosteroids as putative ligands for Pru av 1. NMR spectroscopy provides experimental evidence that Pru av 1 interacts with phytosteroids, and molecular modeling shows that the hydrophobic cavity is large enough to accommodate two such molecules.