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Whole-Genome Metalloproteases in the Wheat Sharp Eyespot Pathogen Rhizoctonia cerealis and a Role in Fungal Virulence

文献类型： 外文期刊

作者： Guo, Feilong 1 ; Pan, Lijun 1 ; Liu, Hongwei 1 ; Lv, Liangjie 2 ; Chen, Xiyong 2 ; Liu, Yuping 2 ; Li, Hui 2 ; Ye, Wenwu 3 ; Zhang, Zengyan 1 ;

作者机构： 1.Chinese Acad Agr Sci, Natl Key Facil Crop Gene Resources & Genet Improv, Key Lab Biol & Genet Improvement Triticeae Crops, Minist Agr & Rural Affairs Peoples Republ China,I, Beijing 100081, Peoples R China

2.Hebei Acad Agr & Forestry Sci, Inst Cereal & Oil Crops, Shijiazhuang 050035, Hebei, Peoples R China

3.Nanjing Agr Univ, Dept Plant Pathol, Key Lab Plant Immun, Nanjing 210095, Peoples R China

关键词： cell death; metalloproteases; Rhizoctonia cerealis; virulence; wheat (Triticum aestivum L; )

期刊名称：INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES （ 影响因子：6.208； 五年影响因子：6.628 ）

ISSN：

年卷期： 2022 年 23 卷 18 期

页码：

收录情况： SCI

摘要： Rhizoctonia cerealis is the causal agent of sharp eyespot, a devastating disease of cereal crops including wheat. Several metalloproteases have been implicated in pathogenic virulence, but little is known about whole-genome metalloproteases in R. cerealis. In this study, a total of 116 metalloproteases-encoding genes were identified and characterized from the R. cerealis Rc207 genome. The gene expression profiles and phylogenetic relationship of 11 MEP36/fungalysin metalloproteases were examined during the fungal infection to wheat, and function of an upregulated secretory MEP36 named RcFL1 was validated. Of 11 MEP36 family metalloproteases, ten, except RcFL5, were predicted to be secreted proteins and nine encoding genes, but not RcFL5 and RcFL2, were expressed during the R. cerealis infection process. Phylogenetic analysis suggested that MEP36 metalloproteases in R. cerealis were closely related to those of Rhizoctonia solani but were remote to those of Bipolaris sorokiniana, Fusarium graminearum, F. pseudograminearum, and Pyricularia oryzae. Expression of RcFL1 was significantly upregulated during the infection process and induced plant cell death in wheat to promote the virulence of the pathogen. The MEP36 domain was necessary for the activities of RcFL1. Furthermore, RcFL1 could repress the expression of wheat genes coding for the chitin elicitor receptor kinase TaCERK1 and chitinases. These results suggest that this MEP36 metalloprotease RcFL1 may function as a virulence factor of R. cerealis through inhibiting host chitin-triggered immunity and chitinases. This study provides insights on pathogenic mechanisms of R. cerealis. RcFL1 likely is an important gene resource for improving resistance of wheat to R. cerealis through host-induced gene silencing strategy.

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