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PubMed · 14602045

Correlating IgE reactivity with three-dimensional structure.

Reto Crameri
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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.

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AllergensAntigensCross ReactionsEpitopes, B-LymphocyteHumansHypersensitivity, ImmediateImmunoglobulin EProtein ConformationVaccinesCommentJournal Article

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Reto Crameri. 2003-11-15. Correlating IgE reactivity with three-dimensional structure.. https://doi.org/10.1042/bj20031363

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