文献类型： 外文期刊

作者： Wang, Lishuang ¹ ; Tian, Peijie ¹ ; Yang, Xiuling ³ ; Zhou, Xueping ³ ; Zhang, Songbai ¹ ; Li, Chun ² ; Yang, Xuehui ² ;

作者机构： 1.Hunan Agr Univ, Coll Plant Protect, Changsha, Peoples R China

2.Guizhou Acad Agr Sci, Inst Plant Protect, Guiyang, Peoples R China

3.Chinese Acad Agr Sci CAAS, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing, Peoples R China

4.Hunan Acad Agr Sci, Inst Plant Protect, Changsha, Peoples R China

关键词： pepper vein yellows virus; Polerovirus; pathogenic factor; RNA silencing suppressor; subcellular localization

期刊名称：FRONTIERS IN MICROBIOLOGY （ 影响因子：5.64； 五年影响因子：6.32 ）

ISSN：

年卷期： 2021 年 12 卷

页码：

收录情况： SCI

摘要： Pepper vein yellows virus (PeVYV) is a newly recognized Polerovirus extracted from Chinese pepper. The symptoms of PeVYV-infested pepper plants comprise intervein yellow staining, leaf curl formation and other malformations, and leaf internodal shrinkage, but the roles of the viral proteins remain undetermined. The P0 protein of the genus Polerovirus has established post-transcriptional gene silencing (PTGS) activity. This investigation focused on the PeVYV-encoded P0 protein and assessed its potential virulence capacity, PTGS activity, and tendencies to localize in the nucleus. This study revealed that P0 influenced the pathogenic properties of a specific heterologous potato virus X. In addition, P0 proteins impaired local gene silencing, although they did not regulate generalized gene silencing within Nicotiana benthamiana 16c plants. Furthermore, P0 proteins localized mainly in the nucleus, particularly in the nucleolus. P0 deletion mutagenesis demonstrated that the F-box motif (56-72 amino acids, AAs) of P0 was essential for symptom determination, inhibition of PTGS, and subcellular localization. Mutation analysis of the F-box motif of P0 protein indicated that AA 57 of the P0 protein was a pivotal site in symptom development and that AA 56 of the P0 protein was indispensable for inhibiting PTGS and subcellular localization. The outcomes obtained here suggest that further studies should be conducted on the molecular mechanisms of amino acids of the F-box domain of P0 protein in the interaction of PeVYV with plants.