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水稻条纹病毒(Rice stripe virus,RSV)的外壳蛋白(coat protein,CP)参与病毒转录复制等多个过程,病毒蛋白之间的相互作用对病毒活性非常重要。本研究利用酵母双杂交技术(yeast two-hybrid,Y2H)和双分子荧光互补(bimolecular fluorescence complementation,Bi FC)技术进一步研究了CP的自身互作位点及其在亚细胞定位中的影响。结果发现,CP的C端307~318位氨基酸区域对其自身互作是必需的,缺失或破坏该结构会导致CP无法实现自身互作,其中4个氨基酸(L308,V309,F312和F313)是互作的关键位点。CP定位于细胞膜和细胞质并且在细胞质中聚集成团,而CP点突变在植物叶片中定位被改变,主要定位于细胞膜,细胞质中没有聚集状颗粒物,说明CP的自身互作与其在植物中的定位是有相关性的两个过程。研究结果有助于揭示CP在RSV侵染过程中所起的重要作用。
The coat protein (CP) of Rice stripe virus (RSV) is involved in many processes such as viral transcriptional replication. The interaction between viral proteins is very important for virus activity. In this study, yeast two-hybrid (Y2H) and bimolecular fluorescence complementation (Bi FC) techniques were used to further investigate the interaction between CP and its subcellular location. As a result, it was found that the C-terminal 307-318 amino acid region of CP was necessary for its own interaction. The deletion or disruption of this structure led to the failure of the CP to interact with itself. Four amino acids (L308, V309, F312 and F313) The key point of interaction. CP locates in the cell membrane and cytoplasm and accumulates into clusters in the cytoplasm. The CP point mutation is located in the plant leaves and is mainly located in the cell membrane. There is no aggregated particles in the cytoplasm, indicating that CP’s own interaction with its localization in plants There are two related processes. The results will help reveal the important role of CP in RSV infection.