A glycoside hydrolase 12 protein from Cytospora chrysosperma triggers plant immunity but is not essential to virulence

Phytopathogens secrete numerous effectors that facilitate their infection and colonization processes. However, the pathogenic mechanism of effectors in Cytospora chrysosperma , the causal agent of canker disease in many woody plants, remains poorly understood. In this study, we identified five glyco...

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Published in:Phytopathology research 2023-07, Vol.5 (1), p.1-15, Article 32
Main Authors: Xu, Zhiye, Luo, Zheng, Xiong, Dianguang, Gao, Meng, Tian, Chengming
Format: Article
Language:English
Subjects:
Apoptosis
Carbohydrates
Cell death
Cell walls
Cellulase
Colonization
Cytospora chrysosperma
Effectors
Elicitor
Enzymes
Fungi
Gene expression
Genes
Genomes
Glycosidases
Glycoside hydrolase
Glycoside hydrolase 12
Glycosides
Hydrogen peroxide
Infections
Jasmonic acid
Kinases
Leucine
Localization
Microorganisms
Pathogenesis
Pathogenicity
Pathogens
Peptides
Plant immunity
Proteins
Salicylic acid
Virulence
Woody plants
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Summary:Phytopathogens secrete numerous effectors that facilitate their infection and colonization processes. However, the pathogenic mechanism of effectors in Cytospora chrysosperma , the causal agent of canker disease in many woody plants, remains poorly understood. In this study, we identified five glycoside hydrolase family 12 (GH12) effector genes in C. chrysosperma genome, all of which were significantly upregulated during the infection stages. Among them, CcEG1 , which contains an additional carbohydrate-binding module family 1 domain (CBM1) at the C-terminal, was selected for further analysis. Transient expression studies showed that CcEG1 was localized to the apoplastic region of Nicotiana benthamiana and acted as an elicitor to induce cell death, and activate the expression of genes involved in salicylic acid (SA), jasmonic acid (JA), and ethylene (ET) signaling pathways. Furthermore, the GH12 domain (position 43–249) was sufficient for cell death-inducing activity, rather than the CBM1 domain. Additionally, the leucine-rich repeat (LRR) receptor-like kinases NbBAK1 and NbSOBIR1 were required for defense responses triggered by CcEG1. Intriguingly, deletion of CcEG1 did not affect fungal pathogenicity, growth, response to hydrogen peroxide and cell wall integrity agents, but affected cellulase utilization. In conclusion, our results suggest that CcEG1 induces coreceptors NbBAK1 - and NbSOBIR1 - dependent plant immunity, increasing our understanding about fungal pathogenesis during the interaction between C. chrysosperma and its host.
ISSN:2524-4167
2096-5362
2524-4167
DOI:10.1186/s42483-023-00187-9