The Single Distinct Leader Protease Encoded by Alpinia oxyphylla Mosaic Virus (Genus Macluravirus) Suppresses RNA Silencing Through Interfering with Double-Stranded RNA Synthesis
文献类型： 外文期刊
作者： Hu, Weiyao 1 ; Dai, Zhaoji 1 ; Liu, Peilan 1 ; Deng, Changhui 1 ; Shen, Wentao 3 ; Li, Zengping 1 ; Cui, Hongguang 1 ;
作者机构： 1.Hainan Univ, Sanya Nanfan Res Inst, Key Lab Green Prevent & Control Trop Plant Dis & P, Minist Educ, Haikou 570228, Hainan, Peoples R China
2.Hainan Univ, Coll Plant Protect, Haikou 570228, Hainan, Peoples R China
3.Chinese Acad Trop Agr Sci, Inst Trop Biosci & Biotechnol, Haikou 571101, Hainan, Peoples R China
关键词： Alpinia oxyphylla; double-stranded RNA; HCPro; Macluravirus; Potyviridae; Potyvirus; RNA silencing; viral suppressor of RNA silencing
期刊名称：PHYTOPATHOLOGY （ 影响因子：3.2； 五年影响因子：3.9 ）
ISSN： 0031-949X
年卷期： 2023 年 113 卷 6 期
页码：
收录情况： SCI
摘要： The genomic 5 & PRIME;-terminal regions of viruses in the family Potyviridae (potyvirids) encode two types of leader proteases: serine-protease (P1) and cysteine-protease (HCPro), which differ greatly in the arrangement and sequence composition among inter-genus viruses. Most potyvirids have the same tandemly arranged P1 and HCPro, whereas viruses in the genus Macluravirus encode a single distinct leader protease, a truncated version of HCPro with yet-unknown functions. We investigated the RNA silencing suppression (RSS) activity and its underpinning mechanism of the distinct HCPro from alpinia oxyphylla mosaic macluravirus (aHCPro). Sequence analysis revealed that macluraviral HCPros have obvious truncations in the N-terminal and middle regions when aligned to their counterparts in potyviruses (well-characterized viral suppressors of RNA silencing). Nearly all defined elements essential for the RSS activity of potyviral counterparts are not distinguished in macluraviral HCPros. Here, we demonstrated that aHCPro exhibits a similar anti-silencing activity with the potyviral counterpart. However, aHCPro fails to block both the local and systemic spreading of RNA silencing. In line, aHCPro interferes with the dsRNA synthesis, an upstream step in the RNA silencing pathway. Affinity-purification and NanoLC-MS/MS analysis revealed that aHCPro has no association with core components or their potential interactors involving in dsRNA synthesis from the protein layer. Instead, the ectopic expression of aHCPro significantly reduces the transcript abundance of RDR2, RDR6, SGS3, and SDE5. This study represents the first report on the anti-silencing function of Macluravirus-encoded HCPro and the underlying molecular mechanism.
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