Changlong Chen, Pierre Buscaill, Nattapong Sanguankiattichai, Jie Huang, Farnusch Kaschani, Markus Kaiser, Renier A. L. van der Hoorn
{"title":"细胞外植物枯草酶抑制冷冲击肽诱导剂水平","authors":"Changlong Chen, Pierre Buscaill, Nattapong Sanguankiattichai, Jie Huang, Farnusch Kaschani, Markus Kaiser, Renier A. L. van der Hoorn","doi":"10.1038/s41477-024-01815-8","DOIUrl":null,"url":null,"abstract":"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.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"10 11","pages":"1749-1760"},"PeriodicalIF":15.8000,"publicationDate":"2024-10-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.com/articles/s41477-024-01815-8.pdf","citationCount":"0","resultStr":"{\"title\":\"Extracellular plant subtilases dampen cold-shock peptide elicitor levels\",\"authors\":\"Changlong Chen, Pierre Buscaill, Nattapong Sanguankiattichai, Jie Huang, Farnusch Kaschani, Markus Kaiser, Renier A. L. van der Hoorn\",\"doi\":\"10.1038/s41477-024-01815-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"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.\",\"PeriodicalId\":18904,\"journal\":{\"name\":\"Nature Plants\",\"volume\":\"10 11\",\"pages\":\"1749-1760\"},\"PeriodicalIF\":15.8000,\"publicationDate\":\"2024-10-11\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.nature.com/articles/s41477-024-01815-8.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature Plants\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.nature.com/articles/s41477-024-01815-8\",\"RegionNum\":1,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"PLANT SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature Plants","FirstCategoryId":"99","ListUrlMain":"https://www.nature.com/articles/s41477-024-01815-8","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"PLANT SCIENCES","Score":null,"Total":0}
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.
期刊介绍:
Nature Plants is an online-only, monthly journal publishing the best research on plants — from their evolution, development, metabolism and environmental interactions to their societal significance.