Correlating IgE reactivity with three-dimensional structure.
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ABSTRACT: 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.
SUBMITTER: Crameri R
PROVIDER: S-EPMC1223769 | biostudies-other | 2003 Nov
REPOSITORIES: biostudies-other
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