The role of Npt1 in regulating antifungal protein activity in filamentous fungi

Summary

Researchers discovered how antifungal proteins work against a dangerous fungus (Aspergillus flavus) that damages crops and produces toxins. They found that these proteins break down the fungal cell wall and then interact with an internal fungal protein called Ntp1. By understanding exactly which part of Ntp1 the antifungal proteins bind to, scientists can now develop better treatments to protect food crops from fungal diseases.

Background

Pathogenic filamentous fungi threaten global food security and human health. Current antifungal agents face limitations due to resistance and toxicity. Antifungal proteins (AFPs) are secreted proteins with potent antifungal activity, but their underlying mechanisms remain partially understood.

Objective

This study investigates the molecular and cellular effects of two AFPs (PgAFP and AfAFP) on Aspergillus flavus to elucidate their antifungal mechanisms. The research focuses on identifying intracellular targets and determining how Ntp1, a fungal-exclusive protein, mediates AFP activity.

Results

AFPs reduced chitin content in fungal cell walls and accumulated in the cytoplasm. Mass spectrometry identified 38 potential cellular targets, including Ntp1, a fungal-exclusive protein. Amino acids 417-588 of Ntp1 are critical for AFP binding and regulate growth, sporulation, sclerotia formation, toxin synthesis, and pathogenicity.

Conclusion

AFPs exert antifungal activity through cell wall disruption and interaction with the intracellular effector protein Ntp1. The 417-588 region of Ntp1 is essential for mediating AFP effects on A. flavus. These findings provide a foundation for developing novel antifungal therapeutics targeting Ntp1.
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