Decoy engineering of the receptor-like cytoplasmic kinase StPBS1 to defend against virus infection in potato.
Decoy engineering of the receptor-like cytoplasmic kinase StPBS1 to defend against virus infection in potato.
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类受体细胞质激酶 StPBS1 的诱饵工程可防御马铃薯病毒感染
DOI：
10.1111/mpp.13220
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发表时间：
2022-06
影响因子：
4.9
通讯作者：
Wuriyanghan, Hada
中科院分区：
文献类型：
--
作者：
Bai, Runyao;Li, Huanhuan;Du, Wenjia;Niu, Niu;Li, Wenxia;Gao, Qican;Yao, Chongyang;Zhou, Zikai;Bao, Wenhua;Che, Mingjia;Zhao, Yongxiu;Zhou, Bin;Wang, Yaohui;Wuriyanghan, Hada
关键词：
马铃薯Y病毒（PVY）是马铃薯（Solanum tuberosum）的重要病原体。尽管 PBS1-RPS5 免疫系统在拟南芥中已有详细记录，但在马铃薯中尚未有报道。在拟南芥中，细菌效应子 AvrPphB 裂解 AtPBS1 以触发免疫反应。在这里，我们证明 AvrPphB 触发的免疫反应是由 StPBS1 介导的，StPBS1 是马铃薯中 AtPBS1 的密切同源物。然而，StPBS1 的下游信号传导是由除 AtRPS5 和 HvPBR1 的马铃薯直系同源物以外的未知抗性 (R) 蛋白介导的，这对于大麦中的 HvPBS1 信号传导非常重要。 StPBS1 的免疫信号传导由 AvrPphB C 端裂解结构域和 STKPQ 基序介导，而 AtPBS1 介导的免疫则需要 AvrPphB 裂解片段和 SEMPH 基序。将 StPBS1 中 AvrPphB 的切割序列替换为 PVY NIa-Pro 蛋白酶的切割序列，得到 StPBS1NIa。 StPBS1NIa 过表达马铃薯对 PVY 感染表现出比 StPBS1 转基因品系更强的免疫力。 StPBS1NIa 在预期靶位点被 PVY 的 NIa-Pro 蛋白酶切割。因此，我们表征了 StPBS1 在马铃薯免疫中的功能，并通过诱饵工程 StPBS1NIa 的转化提供了一种 PVY 的生物技术控制方法。受体样细胞质激酶StPBS1经过诱饵工程设计，可识别马铃薯重要病原体马铃薯病毒Y的NIa蛋白酶，从而触发免疫并为入侵PVY提供生物技术控制方法。
Potato virus Y (PVY) is an important pathogen of potato (Solanum tuberosum). Although the PBS1–RPS5 immune system is well documented in Arabidopsis thaliana, it has not been reported in potato. In Arabidopsis, the bacterial effector AvrPphB cleaves AtPBS1 to trigger an immune response. Here, we show that the AvrPphB‐triggered immune response is mediated by StPBS1, a close homologue of AtPBS1 in potato. However, downstream signalling of StPBS1 was mediated by unknown resistance (R) proteins other than potato orthologues of AtRPS5 and HvPBR1, which is important for HvPBS1 signalling in barley. Immune signalling of StPBS1 is mediated by the AvrPphB C‐terminal cleavage domain and an STKPQ motif, in contrast to AtPBS1‐mediated immunity in which both AvrPphB cleavage fragments and an SEMPH motif are essential. The cleavage sequence of AvrPphB in StPBS1 was replaced with that of the PVY NIa‐Pro protease to obtain StPBS1NIa. StPBS1NIa overexpression potato displayed stronger immunity to PVY infection than did the StPBS1 transgenic lines. StPBS1NIa was cleaved at the expected target site by NIa‐Pro protease from PVY. Thus, we characterized the function of StPBS1 in potato immunity and provide a biotechnology control method for PVY via transformation of decoy‐engineered StPBS1NIa. The receptor‐like cytoplasmic kinase StPBS1 was decoy‐engineered to recognize NIa protease of potato virus Y, an important pathogen of potato, to trigger immunity and to provide a biotechnology control method for invading PVY.
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