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LtEPG1, a Secretory Endopolygalacturonase Protein, Regulates the Virulence of Lasiodiplodia theobromae in Vitis vinifera and Is Recognized as a Microbe-Associated Molecular Patterns

文献类型： 外文期刊

作者： Chethana, K. W. Thilini 1 ; Peng, Junbo 1 ; Li, Xinghong 1 ; Xing, Qikai 1 ; Liu, Mei 1 ; Zhang, Wei 1 ; Hyde, Kevin D 1 ;

作者机构： 1.Beijing Acad Agr & Forestry Sci, Inst Plant & Environm Protect, Beijing Key Lab Environm Friendly Management Frui, Beijing 100097, Peoples R China

2.Mae Fah Luang Univ, Ctr Excellence Fungal Res, Chiang Rai 57100, Thailand

3.China Agr Univ, Coll Plant Protect, Beijing 100097, Peoples R China

4.Mae Fah Luang Univ, Sch Sci, Chiang Rai 57100, Thailand

关键词： cell death; elicitor activity; endopolygalacturonase activity; genetics and resistance; glycoside hydrolase family; Lasiodiplodia theobromae; mycology

期刊名称：PHYTOPATHOLOGY （ 影响因子：4.025； 五年影响因子：4.394 ）

ISSN： 0031-949X

年卷期： 2020 年 110 卷 10 期

页码：

收录情况： SCI

摘要： The Lasiodiplodia theobromae genome encodes numerous glycoside hydrolases involved in organic matter degradation and conducive to pathogen infection, whereas their molecular mechanisms are still largely unknown. Here, we identified the glycoside hydrolase family 28 endopolygalacturonase LtEPG1 in L. theobromae and characterized its function in detail. LtEPG1 acts as a virulence factor during L. theobromae infection. Overexpression and silencing of LtEPG1 in L. theobromae led to significantly increased and decreased lesion areas, respectively. Further, the high transcript level of LtEPG1 during the infection process supported its virulence function. Polygalacturonase activity of LtEPG1 was substantiated by detecting its ability to degrade pectin. Furthermore, LtEPG1 functioned as microbe-associated molecular patterns during the infection process. Both transient expression of LtEPG1 in planta and infiltration of purified LtEPG1 triggered cell death in Nicotiana benthamiana. Site-directed mutation of LtEPG1 indicated that the enzymatic activity of LtEPG1 is independent from its elicitor activity. A protein kinase, KINb1, was shown to interact in the yeast two-hybrid system with LtEPG1. This interaction was further confirmed in vitro using a pull-down assay. Our data indicate that LtEPG1 functions as a polygalacturonase and also serves as an elicitor with two independent mechanisms. Moreover, LtEPG1 may be able to manipulate host immune responses by regulating the KINb1-mediated signal pathway and consequently promote its own successful infection and symptom development.

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