Abstract
Around 25% of food allergic persons in Central Europe suffer from carrot allergy caused by the major carrot allergen Dau c 1. Three different isoallergens, Dau c 1.01, Dau c 1.02 and Dau c 1.03 are identified. However, information about the qualitative and quantitative composition of natural (n)Dau c 1 is scarce. The new carrot allergen Dau c 1.0401 is identified on the mRNA and protein level by RT-PCR and mass spectrometry. It displays only around 60% sequence identity to the other known Dau c 1 isoallergens. NMR and CD-spectra are typical for a well-folded protein containing both α-helices and β-strands. It showed a poor refolding capacity after incubation at 95 °C. IgE-binding is impaired in immunoblots, whereas in inhibition assays IgE binding to soluble Dau c 1.0401 is detected and it clearly provoked a response in mediator release assays. Dau c 1.0401 is a new isoallergen which contributes to the allergenicity of carrots. The absence of immunoreactivity in immobilized assays indicates that IgE binding is impaired when the protein is blotted on a solid phase. Altogether, the results point out that its allergenicity can be reduced upon carrot processing.
Highlights
Survey[1] and around 24% of food-allergic persons in Central Europe suffer from alcarrot allergy caused by the major carrot allergen Dau c 1
Dau c 1.0401 is a new isoallergen which contributes to the allergenicity of carrots
Certain IgE antibodies against Bet v 1 recognize homologous allergens, causing crossreactivity
Summary
Dau c 1.0401 is a new isoallergen which contributes to the allergenicity of carrots. Introduction v 1-homologous allergens, Dau c 1 can induce food allergy independently from previous sensitization by Bet v 1.[14]. No studies exist on the qualitative and quantitative composition of Dau c 1 isoallergens and variants present in carrot. Peptide mass fingerprints (PMF) of purified natural (n)Dau c 1 isolated from carrot revealed that the protein mixture contains at least eight isoallergens/variants that have not been identified previously.[20] This study describes the detection and biochemical, biophysical and immunological characterization of a new Dau c 1 isoallergen, designated and accepted by the WHO/IUIS Allergen Nomeclature Sub-Committee as Dau c 1.0401
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