Sequence-specific 1H, 13C and 15N resonance assignments of the major cherry allergen Pru a 1.

Abstract

Key words: heteronuclear NMR, major cherry allergen, pathogenesis-related protein, sequence-specific resonanceassignmentBiological contextIn industrialized countries about 2–4% of the adultpopulation suffer from IgE-mediated allergies againstfoodstuff (Vieths, 1997). Food hypersensitivity oftenco-occurswith birchpollinosis, and upto 70%ofbirchpollen allergic patients show allergic reactions afterconsumption of fresh fruit or vegetables. Allergic re-actions against pollen lead to clinical syndromes likehay fever, asthma and dermatitis; after ingestion offoodstuff allergic reactions are most often located inthe oropharynx and include from itching and swellingof lips, tongue and throat, to anaphylactic shock.On the molecular level pollen-related food aller-gies can be explained by the cross-reaction of foodallergens with pollen-specific IgE-antibodies, consis-tent with a high sequence similarity of food and pollenallergens. The major birch (Betula verrucosa) pollenallergen Bet v 1 and Pru a 1, the major cherry (Prunusavium) allergen, have a sequence identity of nearly60%. Both are produced as 160-residue precursorproteins that are processed by cleavage of the NH