丁香假单胞菌HopN1结合植物VAP12和Rho-GTPase,提示在膜相关过程中起作用。

Contact (Thousand Oaks (Ventura County, Calif.)) Pub Date : 2025-09-04 eCollection Date: 2025-01-01 DOI:10.1177/25152564251376890
Charlotte Brinkmann, Jennifer Bortlik, Frederik Börnke
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引用次数: 0

摘要

许多革兰氏阴性细菌病原体部署III型效应蛋白(T3Es)来操纵宿主细胞过程并抑制免疫反应。越来越多的证据表明,某些T3Es模拟真核生物FFAT(酸性通道中的两种苯丙氨酸)基序,能够与囊泡相关膜蛋白(VAMP)相关蛋白(VAPs)相互作用。这些相互作用可能有助于病原体瞄准和利用宿主膜接触点。然而,FFAT拟态在不同细菌病原体中的意义和分布仍然知之甚少,这对于揭示其在致病策略中的作用至关重要。在这项研究中,我们分析了模式植物病原菌丁香假单胞菌pv的T3E库。番茄(Pst) DC3000来识别潜在的FFAT基序。我们的初步数据显示,HopN1,一个属于YopT/AvrPphB半胱氨酸蛋白酶家族的Pst T3E,包含至少一个功能性FFAT基序。酵母双杂交和植物共免疫沉淀实验证实,HopN1与植物VAP蛋白相互作用。这种相互作用表明VAP结合可能促进其定位到特定的膜室。此外,HopN1被证明与植物RHO-GTPase相互作用,暗示其功能与哺乳动物中的YopT相似。我们的研究结果表明,HopN1与VAP12和植物RHO-GTPase相互作用,表明在膜相关过程中具有潜在作用。然而,HopN1是否积极利用VAP蛋白进行亚细胞定位仍有待确定。虽然FFAT基序模仿可能有助于植物致病菌的效应靶向,但需要进一步的研究来确定其在HopN1毒力中的功能意义。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Pseudomonas syringae HopN1 Binds Plant VAP12 and a Rho-GTPase, Suggesting a Role in Membrane-Associated Processes.

Many Gram-negative bacterial pathogens deploy type III effector proteins (T3Es) to manipulate host cellular processes and suppress immune responses. Increasing evidence suggests that certain T3Es mimic eukaryotic FFAT (two phenylalanines in an acidic tract) motifs, enabling interaction with vesicle-associated membrane protein (VAMP)-associated proteins (VAPs). These interactions likely help pathogens target and exploit host membrane contact sites. However, the significance and distribution of FFAT mimicry across different bacterial pathogens remain poorly understood, which is crucial to uncovering its role in pathogenic strategies. In this study, we analyzed the T3E repertoire of the model plant pathogenic bacterium Pseudomonas syringae pv. tomato (Pst) DC3000 to identify potential FFAT motifs. Our preliminary data reveal that HopN1, a Pst T3E belonging to the YopT/AvrPphB family of cysteine proteases, contains at least one functional FFAT motif. Yeast two-hybrid and in planta co-immunoprecipitation assays confirmed that HopN1 interacts with plant VAP proteins. This interaction suggests that VAP binding may facilitate its localization to specific membrane compartments. Furthermore, HopN1 was shown to interact with a plant RHO-GTPase, hinting at a functional parallel to YopT in mammals. Our findings demonstrate that HopN1 interacts with VAP12 and a plant RHO-GTPase, suggesting a potential role in membrane-associated processes. However, whether HopN1 actively exploits VAP proteins for subcellular localization remains to be determined. While FFAT motif mimicry may contribute to effector targeting in plant-pathogenic bacteria, further studies are required to establish its functional significance in HopN1 virulence.

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