Correlating IgE reactivity with three-dimensional structure
Keyword(s):
This Commentary discusses the work of Neudecker et al. in this issue of the Biochemical Journal in which site-directed mutagenesis and NMR spectroscopy have been used to analyse in detail the IgE-binding capacity of two cross-reactive allergens: Apg1.0101 from celery (Apium graveolens) and Pru av 1 from cherry (Prunus avium), which are both members of the pathogenesis-related allergen family. The study, showing that the IgE-binding epitopes are highly patient specific, will have a profound impact on our understanding of conformational IgE-binding epitopes, raising serious questions about the therapeutic usefulness of conventional site-directed-mutagenic approaches for the production of hypo-allergenic protein variants.