Antifungal mechanism of sodium dehydroacetate against Geotrichum citri-aurantii

World J Microbiol Biotechnol. 2018 Jan 19;34(2):29. doi: 10.1007/s11274-018-2413-z.

Abstract

This study investigated the potential anti-fungal mechanisms of sodium dehydroacetate (SD) against Geotrichum citri-aurantii. The results showed that the cell wall integrity of G. citri-aurantii was not affected, whereas the membrane permeability of G. citri-aurantii mycelia was visibly altered by SD. Dramatic morphological changes of the mycelia, such as loss of cytoplasm, plasmolysis, and dissolution of intracellular substances, were observed by scanning electron microscopy and transmission electron microscopy analyses, indicating that the mycelium is severely damaged by the SD treatment. Furthermore, SD apparently induced a decrease in the intracellular ATP content before 30 min of exposure. An increase in the activity of the Na+/K+-ATPase was also observed, indicating that Na+ ions might enter the cell and thus disturb the energy supply. Taken together, this study's findings suggest that the anti-fungal activity of SD against G. citri-aurantii can be attributed to the disruption of cell membrane permeability and energy metabolism.

Keywords: Adenosine triphosphate (ATP); Geotrichum citri-aurantii; Membrane permeability; Na+/K+-ATPase; Sodium dehydroacetate.

MeSH terms

  • Adenine Nucleotides / metabolism
  • Adenosine Triphosphatases / drug effects
  • Antifungal Agents / pharmacology*
  • Cell Membrane / drug effects
  • Cell Wall / drug effects
  • Citrus / microbiology
  • Cytoplasm / drug effects
  • Geotrichum / cytology*
  • Geotrichum / drug effects*
  • Microscopy, Electron, Scanning
  • Microscopy, Electron, Transmission
  • Mycelium / cytology
  • Mycelium / drug effects
  • Permeability / drug effects
  • Plant Diseases / microbiology
  • Potassium / metabolism
  • Pyrones / pharmacology*
  • Sodium / metabolism

Substances

  • Adenine Nucleotides
  • Antifungal Agents
  • Pyrones
  • dehydroacetic acid
  • Sodium
  • Adenosine Triphosphatases
  • Potassium