Colletotrichum fructicola is a hemibiotrophic fungal plant pathogen that transitions from biotrophic growth on livinghost tissue to necrotrophic tissue destruction. During the hemibiotrophic phase, numerous proteins a...Colletotrichum fructicola is a hemibiotrophic fungal plant pathogen that transitions from biotrophic growth on livinghost tissue to necrotrophic tissue destruction. During the hemibiotrophic phase, numerous proteins are secretedinto the apoplast, mediating host‒pathogen interactions. In this study, we employed apoplastic proteomics and RNAseqto analyse the proteins secreted during the interaction between C. fructicola and pear. A secreted xylanase,CfXyn11A, was identified as a dual-function effector. In the nonhost Nicotiana benthamiana, it triggered immuneresponses, including reactive oxygen species production and programmed cell death. However, CfXyn11A evadesdetection in the host pear, enabling its role in cell wall degradation and nutrient acquisition. Genetic and biochemicalassays confirmed that the immune-triggering function of CfXyn11A relies on its apoplastic localization and is independentof enzymatic activity. Additionally, we identified an aspartic protease-like protein, PbXIP1, in the pear apoplast,which binds CfXyn11A to suppress its enzymatic activity and virulence. This study highlights the role of apoplasticproteomics in elucidating the molecular mechanisms underlying plant immunity and pathogen virulenceand emphasizes the contrasting outcomes of CfXyn11A in different host contexts. The findings provide new insightsinto the interplay between extracellular effectors and plant defense proteins during fungal infection.展开更多
基金supported by Major Scientific and Technological Project of Xinjiang(2024A02006)National Natural Science Foundation of China(32430094)+2 种基金Jiangsu Agricultural Science and Technology Innovation Fund(CX(24)1024)the Priority Academic Program Development of Jiangsu Higher Education Institutions,the Earmarked Fund for Agriculture Research System of China(CARS-28)supported by the High-performance Computing Platform of the Bioinformatics Center,Nanjing Agricultural University.
文摘Colletotrichum fructicola is a hemibiotrophic fungal plant pathogen that transitions from biotrophic growth on livinghost tissue to necrotrophic tissue destruction. During the hemibiotrophic phase, numerous proteins are secretedinto the apoplast, mediating host‒pathogen interactions. In this study, we employed apoplastic proteomics and RNAseqto analyse the proteins secreted during the interaction between C. fructicola and pear. A secreted xylanase,CfXyn11A, was identified as a dual-function effector. In the nonhost Nicotiana benthamiana, it triggered immuneresponses, including reactive oxygen species production and programmed cell death. However, CfXyn11A evadesdetection in the host pear, enabling its role in cell wall degradation and nutrient acquisition. Genetic and biochemicalassays confirmed that the immune-triggering function of CfXyn11A relies on its apoplastic localization and is independentof enzymatic activity. Additionally, we identified an aspartic protease-like protein, PbXIP1, in the pear apoplast,which binds CfXyn11A to suppress its enzymatic activity and virulence. This study highlights the role of apoplasticproteomics in elucidating the molecular mechanisms underlying plant immunity and pathogen virulenceand emphasizes the contrasting outcomes of CfXyn11A in different host contexts. The findings provide new insightsinto the interplay between extracellular effectors and plant defense proteins during fungal infection.
