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<p>Plants employ various defense mechanisms to protect themselves against pathogenic threats, including the production of antifungal proteins (AFPs). This study focused on characterizing a novel AFP from <i>Arabidopsis thaliana</i>. An AFP was isolated from Arabidopsis leaves, and MALDI-TOF/MS analysis confirmed its amino acid sequence similarity with a hypothetical protein in GenBank (accession number NP_180725), designated as AtHSS1 (<i>Arabidopsis thaliana</i> hypothetical stress-sensitive protein 1). The gene expression of AtHSS1 was induced by pathogen-related signaling molecules salicylic acid (SA) and jasmonic acid (JA), indicating its involvement in plant defense responses. To elucidate its function, the AtHSS1 gene was cloned from Arabidopsis cDNA, heterologously expressed in <i>Escherichia coli</i>, and purified using Ni-NTA affinity and gel filtration chromatography. The purified protein exhibited strong inhibitory activity against various pathogenic fungi. Confocal microscopy revealed that AtHSS1 localizes on the fungal cell surface, and its antifungal activity was associated with extracellular reactive oxygen species (ROS) production, leading to fungal membrane damage. These results suggest that AtHSS1 functions as a stress-responsive, non-toxic antifungal protein with potential application in plant protection.</p>

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Extracellular ROS-dependent antifungal action of AtHSS1, a plant defense protein from Arabidopsis thaliana

  • 期刊论文

  • 发表日期：

    2025年7月24日

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  • Seong-Cheol Park,
  • Jung Ro Lee

摘要

Plants employ various defense mechanisms to protect themselves against pathogenic threats, including the production of antifungal proteins (AFPs). This study focused on characterizing a novel AFP from Arabidopsis thaliana. An AFP was isolated from Arabidopsis leaves, and MALDI-TOF/MS analysis confirmed its amino acid sequence similarity with a hypothetical protein in GenBank (accession number NP_180725), designated as AtHSS1 (Arabidopsis thaliana hypothetical stress-sensitive protein 1). The gene expression of AtHSS1 was induced by pathogen-related signaling molecules salicylic acid (SA) and jasmonic acid (JA), indicating its involvement in plant defense responses. To elucidate its function, the AtHSS1 gene was cloned from Arabidopsis cDNA, heterologously expressed in Escherichia coli, and purified using Ni-NTA affinity and gel filtration chromatography. The purified protein exhibited strong inhibitory activity against various pathogenic fungi. Confocal microscopy revealed that AtHSS1 localizes on the fungal cell surface, and its antifungal activity was associated with extracellular reactive oxygen species (ROS) production, leading to fungal membrane damage. These results suggest that AtHSS1 functions as a stress-responsive, non-toxic antifungal protein with potential application in plant protection.