The Barley Powdery Mildew Candidate Secreted Effector Protein CSEP0105 Inhibits the Chaperone Activity of a Small Heat Shock Protein
The Barley Powdery Mildew Candidate Secreted Effector Protein CSEP0105 Inhibits the Chaperone Activity of a Small Heat Shock Protein
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DOI：
10.1104/pp.15.00278
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发表时间：
2015-05-01
期刊：
影响因子：
7.4
通讯作者：
Thordal-Christensen, Hans
中科院分区：
文献类型：
--
作者：
Ahmed, Ali Abdurehim;Pedersen, Carsten;Thordal-Christensen, Hans
病原体分泌效应蛋白以与其宿主建立成功的相互作用。在这里，我们描述了两个大麦（大麦）白粉病候选分泌效应蛋白，CSEP 0105和CSEP 0162，这有助于病原体的成功，似乎需要在吸器形成过程中或之后。使用宿主诱导的基因沉默来沉默任一CSEP显著降低真菌吸器形成率。有趣的是，在酵母双杂交试验中，这两种CSEP与大麦小热休克蛋白Hsp16.9和Hsp17.5相互作用。已知小的热休克蛋白通过其分子伴侣活性稳定几种细胞内蛋白，包括防御相关的信号传导组分。CSEP 0105和CSEP 0162定位于大麦表皮细胞的细胞质和细胞核，而Hsp 16.9和Hsp 17.5定位于细胞质。有趣的是，只有那些特定的CSEP改变了定位，并成为限制在细胞质中时，与Hsp16.9和Hsp17.5共表达，确认CSEP-小热休克蛋白相互作用。正如预测的那样，热休克蛋白16.9显示分子伴侣活性，因为它可以防止在热应激过程中的大肠杆菌蛋白质的聚集。值得注意的是，CSEP 0105破坏了这一活动。这些数据表明，CSEP 0105通过干扰大麦小分子热激蛋白的分子伴侣活性来促进毒力，该蛋白对于防御和应激反应至关重要。
Pathogens secrete effector proteins to establish a successful interaction with their host. Here, we describe two barley (Hordeum vulgare) powdery mildew candidate secreted effector proteins, CSEP0105 and CSEP0162, which contribute to pathogen success and appear to be required during or after haustorial formation. Silencing of either CSEP using host-induced gene silencing significantly reduced the fungal haustorial formation rate. Interestingly, both CSEPs interact with the barley small heat shock proteins, Hsp16.9 and Hsp17.5, in a yeast two-hybrid assay. Small heat shock proteins are known to stabilize several intracellular proteins, including defense-related signaling components, through their chaperone activity. CSEP0105 and CSEP0162 localized to the cytosol and the nucleus of barley epidermal cells, whereas Hsp16.9 and Hsp17.5 are cytosolic. Intriguingly, only those specific CSEPs changed localization and became restricted to the cytosol when coexpressed with Hsp16.9 and Hsp17.5, confirming the CSEP-small heat shock protein interaction. As predicted, Hsp16.9 showed chaperone activity, as it could prevent the aggregation of Escherichia coli proteins during thermal stress. Remarkably, CSEP0105 compromised this activity. These data suggest that CSEP0105 promotes virulence by interfering with the chaperone activity of a barley small heat shock protein essential for defense and stress responses.