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Mechanism of action of AMP-jsa9, a LI-F-type antimicrobial peptide produced by Paenibacillus polymyxa JSa-9, against Fusarium moniliforme

Han, Jinzhi, Wang, Fang, Gao, Peng, Ma, Zhi, Zhao, Shengming, Lu, Zhaoxin, Lv, Fengxia, Bie, Xiaomei
Fungal genetics and biology 2017 v.104 pp. 45-55
Fusarium verticillioides, Gram-positive bacteria, NAD (coenzyme), NADP (coenzyme), Paenibacillus polymyxa, adenosine triphosphate, antimicrobial peptides, biosynthesis, cell walls, chitin, confocal laser scanning microscopy, cytoskeleton, cytotoxicity, ergosterol, feed industry, feeds, fumonisin B1, fungi, hemolysis, mechanism of action, plasma membrane, potassium, protein synthesis, proteomics, scanning electron microscopy, transmission electron microscopy
LI-F type peptides (AMP-jsa9) are a group of cyclic lipodepsipeptides that exhibit broad antimicrobial spectrum against Gram-positive bacteria and filamentous fungi. We sought to assess the toxicity of AMP-jsa9 and the mechanism of AMP-jsa9 action against Fusarium moniliforme. AMP-jsa9 exhibited weak hemolytic activity and weak cytotoxicity at antimicrobial concentrations (32μg/ml). Confocal laser microscopy, SEM, and TEM indicated that AMP-jsa9 primarily targets the cell wall, plasma membrane, and cytoskeleton, increases membranepermeability, and enhances cytoplasm leakage (e.g., K⁺, protein). Quantitative proteomic analysis using isobaric tags for relative and absolute quantitation (iTRAQ) detected a total of 162 differentially expressed proteins (59 up-regulated and 103 down-regulated) following treatment of F. moniliforme with AMP-jsa9. AMP-jsa9 treatment also led to reductions in chitin, ergosterol, NADH, NADPH, and ATP levels. Moreover, fumonisin B1 expression and biosynthesis was suppressed in AMP-jsa9-treated F. moniliforme. Our results provide a theoretical basis for the application of AMP-jsa9 as a natural and effective antifungal agent in the agricultural, food, and animal feed industries.