Evolutionarily distinct Resistance proteins detect a pathogen effector through its association with different host targets.
Evolutionarily distinct Resistance proteins detect a pathogen effector through its association with different host targets.
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DOI：
10.1111/nph.17660
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发表时间：
2021-08
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影响因子：
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通讯作者：
Haixia Wang;F. Trusch;Dionne Turnbull;C. Aguilera-Galvez;Susan Breen;S. Naqvi;Jonathan D. G. Jones;I. Hein;Zhendong Tian;V. Vleeshouwers;Eleanor M. Gilroy;P. Birch
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文献类型：
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作者：
Haixia Wang;F. Trusch;Dionne Turnbull;C. Aguilera-Galvez;Susan Breen;S. Naqvi;Jonathan D. G. Jones;I. Hein;Zhendong Tian;V. Vleeshouwers;Eleanor M. Gilroy;P. Birch
持久抗病的关键是了解控制病原体识别的进化过程。我们确定了致病疫霉效应子 PiAVR2 如何被进化上不同的抗性蛋白 R2 和 Rpi-mcq1 识别。我们采用酵母 2 杂交、免疫共沉淀、病毒诱导的基因沉默、瞬时过表达和磷酸酶活性测定来研究 BSL 磷酸酶对 R2 和 Rpi-mcq1 介导的超敏反应 (HR) 的贡献。沉默 PiAVR2 目标 BSL1 会损害 R2 HR。仅当 BSL2 和 BSL3 沉默时，Rpi-mcq1 HR 才会受到影响。 BSL1 过表达会增加 R2 HR 并损害 Rpi-mcq1。然而，BSL2 或 BSL3 过表达会增强 Rpi-mcq1 并损害 R2 HR。冈田酸可抑制 BSL 磷酸酶活性，从而抑制这两种识别事件。此外，BSL1 磷酸酶死亡 (PD) 突变体的表达会抑制 R2 HR，而 BSL2-PD 和 BSL3-PD 突变体的表达会抑制 Rpi-mcq1 HR。在 PiAVR2 存在的情况下，R2 与 BSL1 相互作用，但不与 BSL2 和 BSL3 相互作用，而 Rpi-mcq1 和 BSL 之间未检测到相互作用。因此，BSL1 活性以及与 R2 的关联决定了 R2 对 PiAVR2 的识别，而 BSL2 和 BSL3 介导 Rpi-mcq1 对 PiAVR2 的感知。 R2 和 Rpi-mcq1 利用不同的机制根据与不同 BSL 的关联来检测 PiAVR2，突出了这些效应器靶点对疾病和抗病性的核心作用。
Critical to durable disease resistance is understanding evolutionary processes governing pathogen recognition. We determined how Phytophthora infestans effector PiAVR2 is recognised by evolutionarily distinct resistance proteins R2 and Rpi-mcq1. We employed yeast-2-hybrid, co-immunoprecipitation, virus-induced gene silencing, transient overexpression, and phosphatase activity assays to investigate contributions of BSL phosphatases to R2- and Rpi-mcq1-mediated hypersensitive response (HR). Silencing PiAVR2 target BSL1 compromises R2 HR. Rpi-mcq1 HR is compromised only when BSL2 and BSL3 are silenced. BSL1 overexpression increases R2 HR and compromises Rpi-mcq1. However, BSL2 or BSL3 overexpression enhance Rpi-mcq1 and compromise R2 HR. Okadaic acid, which inhibits BSL phosphatase activity, suppresses both recognition events. Moreover, expression of a BSL1 phosphatase-dead (PD) mutant suppresses R2 HR, whereas BSL2-PD and BSL3-PD mutants suppresses Rpi-mcq1 HR. R2 interacts with BSL1 in the presence of PiAVR2, but not with BSL2 and BSL3, whereas no interactions were detected between Rpi-mcq1 and BSLs. Thus, BSL1 activity and association with R2 determine recognition of PiAVR2 by R2, whereas BSL2 and BSL3 mediate Rpi-mcq1 perception of PiAVR2. R2 and Rpi-mcq1 utilise distinct mechanisms to detect PiAVR2 based on association with different BSLs, highlighting central roles of these effector targets for both disease and disease resistance.