Exploring the structure and function of PR-10 pollen and food allergens and their physiological ligands

植物致病相关蛋白PR-10在植物中广泛存在，并具有保守性。尽管它们在不同的植物家族中普遍存在，并在花粉和食物过敏中发挥重要作用，但它们在分子水平上的生理功能仍然难以捉摸。至少部分PR-10变应原似乎是植物对病原体或非生物胁迫刺激的免疫反应的一部分，这会导致植物激素和抗真菌代谢物的产生。草莓中的Fra1变应原似乎参与了类黄酮的生物合成，起到了载体蛋白的作用。然而，我们需要回答一些基本问题。例如，1型过敏性的一般结构基础尚不清楚。PR-10家族的一些成员不会引发过敏反应，尽管整体3D结构与那些被认为是过敏原的PR-10蛋白高度相似。此外，有人认为，与过敏原结合的配体可能对过敏反应很重要，甚至可能增强它们的过敏性。到目前为止，只有两种天然配体被鉴定出来，都是在拜罗伊特大学生物聚合物系。然而，我们对它们在体内的功能仍然知之甚少。因此，更好地了解致敏PR-10蛋白及其天然配体的生理作用可能有助于为变态反应治疗提供新的方面。该项目将有助于阐明PR-10变应原的结构和功能，识别新的同种变应原及其配体，并确定它们的致敏潜力。

Pathogenesis-related plant proteins PR-10 are conserved and ubiquitous in plants. In spite of their hig prevalence in different plant families and their important role in pollen and food allergies their physiological function on a molecular level remains elusive. At least some of the PR-10 allergens appear to be part of the plants' immune response against pathogens or abiotic stress stimuli, which leads to the production of phytohormones and antifungal metabolites. The Fra a 1 allergen from strawberries appears to be involved in flavonoid biosynthesis, functioning as a carrier protein. However, fundamental questions need to be answered. For example the general structural basis of type 1 allergenicity is not known. Some members of the PR-10 family do not trigger allergic reactions although the overall 3D structure is highly similar to those PR-10 proteins that are considered allergens. Furthermore, it was suggested that the ligands bound to the allergens might be important for the allergic reaction and might even enhance their allergenicity. So far only two natural ligands have been identified, both in the Department of Biopolymers at the University of Bayreuth. However, we still do not know much about their in vivo function. Therefore, a better understanding of the physiological roles of allergenic PR-10 proteins and their natural ligands may help to provide new aspects in allergy treatment. This project shall contribute to elucidate the structure and function of PR-10 allergens, to identify new isoallergens and their ligands as well as to determine their allergenic potential.