Valsa mali Pathogenic Effector VmPxE1 Contributes to Full Virulence and Interacts With the Host Peroxidase MdAPX1 as a Potential Target.
Valsa mali Pathogenic Effector VmPxE1 Contributes to Full Virulence and Interacts With the Host Peroxidase MdAPX1 as a Potential Target.
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Valsa mali 致病效应子 VmPxE1 有助于完全毒力并与作为潜在靶标的宿主过氧化物酶 MdAPX1 相互作用
DOI：
10.3389/fmicb.2018.00821
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发表时间：
2018
影响因子：
5.2
通讯作者：
Huang L
中科院分区：
文献类型：
--
作者：
Zhang M;Feng H;Zhao Y;Song L;Gao C;Xu X;Huang L
苹果腐烂病是由苹果腐烂病（Valsa mali，V. mali）引起的一种毁灭性病害。效应蛋白对于真菌的致病性是重要的。我们研究了一个候选效应VmPxE 1分离的基因组信息的基础上，苹果。利用酵母转化酶分泌测定系统，证实vmPxE 1含有具有分泌功能的信号肽。VmPxE 1可以抑制BCL-2相关X蛋白（BAX）诱导的本氏烟草细胞死亡，效率高达92%。在感染的早期阶段，VmPxE 1的表达上调，VmPxE 1的缺失导致苹果枝条和叶片上的毒力显着降低。通过酵母双杂交筛选、双分子荧光互补和体内免疫共沉淀等方法，证实了vmPxE 1可以靶向苹果抗坏血酸过氧化物酶（MdAPX 1）。序列系统发育分析表明，MdAPX 1是一种抗坏血酸过氧化物酶，属于植物超家族血红素依赖性过氧化物酶的一个亚组。突变体中MdAPX 1的异位表达显著增强了对H2 O2的抗性，而VmPxE 1的存在似乎干扰了MdAPX 1的功能。本研究结果为进一步了解vmPxE 1作为苹果腐烂病菌的候选效应子在苹果腐烂病中的作用提供了依据。
The Valsa canker, caused by Valsa mali (V. mali), is a destructive disease of apple in Eastern Asia. Effector proteins are important for fungal pathogenicity. We studied a candidate effector VmPxE1 isolated based on the genome information of V. mali. By using the yeast invertase secretion assay system, VmPxE1 was shown to contain a signal peptide with secretory functions. VmPxE1 can suppress BCL-2-associated X protein (BAX)-induced cell death with a high efficacy of 92% in Nicotiana benthamiana. The expression of VmPxE1 was upregulated during the early infection stage and deletion of VmPxE1 led to significant reductions in virulence on both apple twigs and leaves. VmPxE1 was also shown to target an apple ascorbate peroxidase (MdAPX1) by the yeast two-hybrid screening, bimolecular fluorescence complementation and in vivo co-immunoprecipitation. Sequence phylogenetic analysis suggested that MdAPX1 was an ascorbate peroxidase belonging to a subgroup of heme-dependent peroxidases of the plant superfamily. The ectopic expression of MdAPX1 in the mutant of VmPxE1 significantly enhanced resistance to H2O2, while the presence of VmPxE1 seems to disturb MdAPX1 function. The present results provide insights into the functions of VmPxE1 as a candidate effector of V. mali in causing apple canker.