| Autor: |
Jacob, Thessa, Wangorsch, Andrea, Vogel, Lothar, Reuter, Andreas, Mahler, Vera, Wöhrl, Birgitta M., Biochemie IV ‐ Biopolymere, Universität Bayreuth, Universitätsstr. 30, Bayreuth, D‐95447 Germany, Molecular Allergology, Paul‐Ehrlich‐Institut, Langen, D‐63225 Germany, Division Of Allergology, Paul‐Ehrlich‐Institut, Langen, D‐63225 Germany |
| Jazyk: |
angličtina |
| Rok vydání: |
2021 |
| Předmět: |
|
| DOI: |
10.15495/epub_ubt_00005748 |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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