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Article Abstract
Heat-stable antifungal factor (HSAF) isolated from is considered a potential biocontrol agent. However, the target of HSAF in phytopathogenic fungi remains unclear. In this study, we investigated the target of HSAF in that causes fatal pear Valsa canker. Thirty-one HSAF-binding proteins were captured and identified by surface plasmon resonance (SPR) and high-performance liquid chromatography-mass spectrometry (LC-MS/MS), and 11 deletion mutants were obtained. Among these mutants, only Δ showed decreased sensitivity to HSAF. Additionally, Δ exhibited significantly reduced virulence in . Molecular docking and SPR results revealed that HSAF bound to threonine 569 and glycine 570 of VpVeb1, which are crucial for AAA ATPase activity. Another study showed that HSAF could decrease the ATPase activity of VpVeb1, leading to the reduced virulence of . Taken together, this study first identified the potential target of HSAF in fungi. These findings will help us better understand the model of action of HSAF to fungi.
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Article Synopsis
- Heat-stable antifungal factor (HSAF) is being studied as a biocontrol agent against phytopathogenic fungi, specifically targeting the fungus causing fatal pear Valsa canker.
- Researchers identified 31 proteins that bind to HSAF and created 11 deletion mutants, finding that one mutant showed decreased sensitivity and reduced virulence in the fungus.
- The study revealed that HSAF binds to specific amino acids in a protein (VpVeb1) crucial for its ATPase activity, which correlates with the reduced ability of the fungus to cause disease.
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