马铃薯Rpi-vnt1.1/GLYK免疫模块激活晚疫病抗性的分子机制研究

挖掘和利用马铃薯抗病基因是防治晚疫病的重要途径。抗病基因Rpi-vnt1.1编码的受体通过识别致病疫霉无毒蛋白AVRvnt1诱导晚疫病抗性，然而Rpi-vnt1.1激活植物免疫的具体机制仍不清楚。申请者前期发现Rpi-vnt1.1与甘油酸盐激酶GLYK在植物体内组成免疫模块，并与AVRvnt1互作；无AVRvnt1时，Rpi-vnt1.1处于非激活状态，在胞质中以单体和寡聚体存在，而有AVRvnt1时，Rpi-vnt1.1受到激活，其寡聚化水平显著上升，亚细胞定位从颗粒状变为团块状。本项目拟深入解析Rpi-vnt1.1复合体的形成与其蛋白寡聚化和团块状定位的关系，阐明Rpi-vnt1.1/GLYK免疫模块在抗病过程中的作用机制。研究成果有望揭示Rpi-vnt1.1/GLYK/AVRvnt1复合体的免疫激活机制，为合理利用Rpi-vnt1.1进行马铃薯晚疫病防治提供实践指导。

Exploiting potato resistance gene is an important way to control late blight disease. The NLR receptor encoded by Rpi-vnt1.1 recognizes the avirulence protein AVRvnt1 secreted by Phytophthora infestans and activates plant resistance. However, the mechanism of how Rpi-vnt1.1 activates plant immunity is still unknown. Previously, the applicant found that Rpi-vnt1.1 forms immune module with glycerate-3-kinase GLYK, these two proteins could interact with AVRvnt1 in vivo. Rpi-vnt1.1 is inactivated when there is no AVRvnt1, and shows monomer and polymer states, Rpi-vnt1.1 is activated when co-expressed with AVRvnt1, and shows increased oligmerization level and its granule-like localisation was transformed to lump-like. This project intends to dissect the relationship among protein complex formation, protein oligmerization and lump-like structure formation, and clarify the mechanism of resistance actived by Rpivnt1.1/GLYK immune module. The results are expected to dissect the molecular basis of immune response acitated by Rpi-vnt1.1/GLYK/AVRvnt1 protein complex, and provide guidance for late blight control by using Rpi-vnt1.1 based disease-resistant variety.