文献类型： 外文期刊
作者： Chen, Changlong 1 ; Buscaill, Pierre 2 ; Sanguankiattichai, Nattapong 2 ; Huang, Jie 2 ; Kaschani, Farnusch 3 ; Kaiser, Markus 3 ; van der Hoorn, Renier A. L. 2 ;
作者机构： 1.Beijing Acad Agr & Forestry Sci, Inst Biotechnol, Beijing 100097, Peoples R China
2.Univ Oxford, Dept Biol, Plant Chemet Lab, Oxford, England
3.Univ Duisburg Essen, Fac Biol, ZMB Chem Biol, Dept Chem Biol, Essen, Germany
期刊名称：NATURE PLANTS （ 影响因子：13.6； 五年影响因子：17.0 ）
ISSN： 2055-026X
年卷期： 2024 年 10 卷 11 期
页码：
收录情况： SCI
摘要： Recognizing pathogen-associated molecular patterns on the cell surface is crucial for plant immunity. The proteinaceous nature of many of these patterns suggests that secreted proteases play important roles in their formation and stability. Here we demonstrate that the apoplastic subtilase SBT5.2a inactivates the immunogenicity of cold-shock proteins (CSPs) of the bacterial plant pathogen Pseudomonas syringae by cleaving within the immunogenic csp22 epitope. Consequently, mutant plants lacking SBT5.2a activity retain higher levels of csp22, leading to enhanced immune responses and reduced pathogen growth. SBT5.2 sensitivity is influenced by sequence variation surrounding the cleavage site and probably extends to CSPs from other bacterial species. These findings suggest that variations in csp22 stability among bacterial pathogens are a crucial factor in plant-bacteria interactions and that pathogens exploit plant proteases to avoid pattern recognition. Secreted plant subtilase SBT5.2 inactivates immunogenic csp22 epitopes in cold-shock proteins of Pseudomonas syringae, suggesting that pathogens exploit plant proteases to evade detection.
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