Biochemie IV - Biopolymere, Universität Bayreuth, Universitätsstr. 30, Bayreuth, D-95447, Germany.
Molecular Allergology, Paul-Ehrlich-Institut, Langen, D-63225, Germany.
Mol Nutr Food Res. 2021 Apr;65(7):e2001110. doi: 10.1002/mnfr.202001110. Epub 2021 Mar 3.
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.
中欧约有 25%的食物过敏人群对胡萝卜过敏,这是由主要过敏原 Dau c 1 引起的。已鉴定出三种不同的同工过敏原 Dau c 1.01、Dau c 1.02 和 Dau c 1.03。然而,关于天然(n)Dau c 1 的定性和定量组成的信息却很少。
通过 RT-PCR 和质谱法在 mRNA 和蛋白质水平上鉴定出新的胡萝卜过敏原 Dau c 1.0401。它与其他已知的 Dau c 1 同工过敏原的序列同一性仅约为 60%。NMR 和 CD 谱是含有α-螺旋和β-链的折叠良好的蛋白质的典型特征。它在 95°C 孵育后显示出较差的重折叠能力。免疫印迹中 IgE 结合受损,而在抑制试验中,可溶性 Dau c 1.0401 与 IgE 结合被检测到,并在介质释放试验中明显引发了反应。
Dau c 1.0401 是一种新的同工过敏原,它导致胡萝卜的致敏性。固定化测定中无免疫反应性表明,当蛋白质印迹在固相上时,IgE 结合受到损害。总的来说,这些结果表明,在胡萝卜加工过程中可以降低其致敏性。