The p23 of Citrus Tristeza Virus Interacts with Host FKBP-Type Peptidyl-Prolylcis-Trans Isomerase 17-2 and Is Involved in the Intracellular Movement of the Viral Coat Protein
文献类型： 外文期刊
作者： Yang, Zuokun 1 ; Zhang, Yongle 1 ; Wang, Guoping 1 ; Wen, Shaohua 1 ; Wang, Yanxiang 1 ; Li, Liu 1 ; Xiao, Feng 1 ; Hong, 1 ;
作者机构： 1.Huazhong Agr Univ, Coll Plant Sci & Technol, Key Lab Plant Pathol Hubei Prov, Wuhan 430070, Peoples R China
2.Minist Agr, Key Lab Hort Crop Fruit Trees Biol & Germplasm Cr, Wuhan 430070, Peoples R China
3.Hubei Acad Agr Sci, Hubei Biopesticide Engn Res Ctr, Natl Biopesticide Engn Res Ctr, Wuhan 430064, Peoples R China
关键词： citrus tristeza virus; p23; coat protein; FK506-binding protein; protein-protein interaction
期刊名称：CELLS （ 影响因子：4.366； 五年影响因子：5.276 ）
ISSN：
年卷期： 2021 年 10 卷 4 期
页码：
收录情况： SCI
摘要： Citrus tristeza virus is a member of the genus Closterovirus in the family Closteroviridae. The p23 of citrus tristeza virus (CTV) is a multifunctional protein and RNA silencing suppressor. In this study, we identified a p23 interacting partner, FK506-binding protein (FKBP) 17-2, from Citrus aurantifolia (CaFKBP17-2), a susceptible host, and Nicotiana benthamiana (NbFKBP17-2), an experimental host for CTV. The interaction of p23 with CaFKBP17-2 and NbFKBP17-2 were individually confirmed by yeast two-hybrid (Y2H) and bimolecular fluorescence complementation (BiFC) assays. Subcellular localization tests showed that the viral p23 translocated FKBP17-2 from chloroplasts to the plasmodesmata of epidermal cells of N. benthamiana leaves. The knocked-down expression level of NbFKBP17-2 mRNA resulted in a decreased CTV titer in N. benthamiana plants. Further, BiFC and Y2H assays showed that NbFKBP17-2 also interacted with the coat protein (CP) of CTV, and the complexes of CP/NbFKBP17-2 rapidly moved in the cytoplasm. Moreover, p23 guided the CP/NbFKBP17-2 complexes to move along the cell wall. To the best of our knowledge, this is the first report of viral proteins interacting with FKBP17-2 encoded by plants. Our results provide insights for further revealing the mechanism of the CTV CP protein movement.
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