Institute of Molecular Biology, Medical University Innsbruck, Innrain 80, A-6020 Innsbruck, Austria.
Biol Chem. 2020 Sep 16;402(4):433-437. doi: 10.1515/hsz-2020-0185. Print 2021 Mar 26.
Although some progress has been achieved in understanding certain aspects of the allergenic mechanism of animal lipocalins, they still remain largely enigmatic. One possibility to unravel this property is to investigate their interaction with components of the immune system. Since these components are highly complex we intended to use a high-throughput technology for this purpose. Therefore, we used phage-display of a random peptide library for panning against the dog allergen Can f 1. By this method we identified a Can f 1 binding peptide corresponding to the antigen-binding site of a putative γδT-cell receptor. Additional biochemical investigations confirmed this interaction.
尽管在理解动物脂蛋白的某些过敏机制方面已经取得了一些进展，但它们仍然在很大程度上是神秘的。揭示这种特性的一种可能性是研究它们与免疫系统成分的相互作用。由于这些成分非常复杂，我们打算为此目的使用高通量技术。因此，我们使用噬菌体展示随机肽库对犬过敏原 Can f 1 进行淘选。通过这种方法，我们鉴定了一个与假定的γδT 细胞受体的抗原结合位点相对应的 Can f 1 结合肽。额外的生化研究证实了这种相互作用。
