Correlating IgE reactivity with three-dimensional structure.
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.
Crameri
Reto
R
Swiss Institute of Allergy and Asthma Research (SIAF), Obere Strasse 22, CH-7270 Davos, Switzerland. crameri@siaf.unizh.ch
D000485:Allergens / Q000737:chemistry* / Q000276:immunology*; D000941:Antigens / Q000737:chemistry / Q000276:immunology; D003429:Cross Reactions; D018985:Epitopes, B-Lymphocyte / Q000737:chemistry / Q000276:immunology; D006801:Humans; D006969:Hypersensitivity, Immediate / Q000276:immunology / Q000628:therapy*; D007073:Immunoglobulin E / Q000276:immunology*; D011487:Protein Conformation; D014612:Vaccines
D000485:Allergens; D000941:Antigens; D018985:Epitopes, B-Lymphocyte; D014612:Vaccines; D007073:Immunoglobulin E