Publication Abstract from PubMed
Birch pollinosis is often accompanied by hypersensitivity 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 heteronuclear multidimensional NMR spectroscopy to determine 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 structures 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 conserved 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.
Allergic cross-reactivity made visible: solution structure of the major cherry allergen Pru av 1.,Neudecker P, Schweimer K, Nerkamp J, Scheurer S, Vieths S, Sticht H, Rosch P J Biol Chem. 2001 Jun 22;276(25):22756-63. Epub 2001 Apr 3. PMID:11287426[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
