URN zum Zitieren der Version auf EPub Bayreuth: urn:nbn:de:bvb:703-epub-5748-0
Titelangaben
Jacob, Thessa ; Wangorsch, Andrea ; Vogel, Lothar ; Reuter, Andreas ; Mahler, Vera ; Wöhrl, Birgitta M.:
A Novel Isoallergen Dau c 1.0401 in Carrot : Stability, Allergenicity, and Comparison with Other Isoallergens.
In: Molecular Nutrition & Food Research.
Bd. 65
(2021)
Heft 7
.
- No. 2001110.
ISSN 1613-4133
DOI der Verlagsversion: https://doi.org/10.1002/mnfr.202001110
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Abstract
Scope: 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. Methods and Results: 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. Conclusion: 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.