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Molecular characterization of Dau c 1, the Bet v 1 homologous protein from carrot and its cross-reactivity with Bet v 1 and Api g 1
Article first published online: 24 DEC 2001
DOI: 10.1046/j.1365-2222.1999.00529.x
Blackwell Science Ltd, Oxford
1365-2222/asset/cover.gif?v=1&s=363d6ac7042b7535760df61b7393fd8e0a08e85f "Clinical & Experimental Allergy")
Additional Information
How to Cite
HOFFMANN-SOMMERGRUBER, O'RIORDAIN, AHORN, EBNER, DA CAMARA MACHADO, PÜHRINGER, SCHEINER and BREITENEDER (1999), Molecular characterization of Dau c 1, the Bet v 1 homologous protein from carrot and its cross-reactivity with Bet v 1 and Api g 1. Clinical & Experimental Allergy, 29: 840–847. doi: 10.1046/j.1365-2222.1999.00529.x
Publication History
- Issue published online: 24 DEC 2001
- Article first published online: 24 DEC 2001
- Abstract
- Article
- References
- Cited By
Keywords:
- Dau c 1;
- Bet v 1;
- Api g 1;
- food allergen;
- carrot;
- IgE-binding;
- recombinant allergen
Background
Up to 70% of patients with birch pollen allergy exhibit the so-called oral allergy syndrome, an IgE-mediated food allergy. The most frequent and therefore best characterized pollen–fruit syndrome is apple allergy in patients suffering from tree pollen-induced pollinosis. The occurrence of adverse reactions to proteins present in vegetables such as celery and carrots in patients suffering from pollen allergy has also been reported. cDNAs for Bet v 1 homologous proteins have been cloned from celery, apple and cherry. Objective The aim of the study was to identify Bet v 1 homologues from carrot (Daucus carota), to isolate the respective cDNA, to compare the IgE-binding capacity of the natural protein to the recombinant allergen and determine the cross-reactivity to Api g 1 and Bet v 1.
Methods
Molecular characterization of the carrot allergen was performed using IgE-immunoblotting, cross-inhibition assays, N-terminal sequencing, PCR-based cDNA cloning and expression of the recombinant protein in Escherichia coli.
Results
A 16-kDa protein from carrot was identified as a major IgE-binding component and designated Dau c 1. Sequencing corresponding cDNAs revealed three extremely similar sequences (Dau c 1.1, 1.2 and 1.3) with an open reading frame of 462 bp coding for 154 amino acid residues.
Conclusions
Purified recombinant Dau c 1.2 was tested in immunoblots displaying IgE-binding capacity comparable to its natural counterpart. Cross-inhibition assays verified the existence of common B-cell epitopes present on Dau c 1, Api g 1 as well as on Bet v 1.