Department of Plant Biochemistry, Centre for Plant Molecular Biology (ZMBP), Eberhard Karls University Tübingen, Tübingen, Germany.
CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.
Methods Mol Biol. 2024;2724:235-245. doi: 10.1007/978-1-0716-3485-1_17.
Protein-protein interactions constitute the interface between a virus and the cell it infects and are crucial determinants of the outcome of the viral infection. Multiple techniques have been developed to study how viral and host proteins interact in plants; among them, the split-luciferase complementation imaging assay stands out due to its capacity to detect protein-protein interactions in vivo, in the context of the infection, if desired, in an easy, fast, quantitative, and inexpensive manner. In this chapter, we use the interaction between the V2 protein from the geminivirus tomato yellow leaf curl virus (TYLCV) and Nicotiana benthamiana Argonaute 4 (AGO4) as an example to present how to perform this simple yet powerful assay using transient Agrobacterium tumefaciens-mediated transformation of N. benthamiana leaves to test the protein-protein interactions of choice.
蛋白质-蛋白质相互作用构成了病毒与其感染的细胞之间的界面，是病毒感染结果的关键决定因素。已经开发出多种技术来研究病毒和宿主蛋白在植物中的相互作用；其中，由于其能够以简单、快速、定量和廉价的方式在感染情况下在体内检测蛋白质-蛋白质相互作用，如果需要，分裂萤光素酶互补成像测定法引人注目。在本章中，我们以番茄黄卷叶病毒（TYLCV）的 V2 蛋白与本氏烟 Argonaute 4（AGO4）之间的相互作用为例，介绍如何使用瞬时农杆菌介导的本氏烟叶片转化来进行此简单而强大的测定，以测试所选的蛋白质-蛋白质相互作用。
