Inhibition of secretion of staphylococcal alpha toxin by cerulenin

J Med Microbiol. 1984 Oct;18(2):205-16. doi: 10.1099/00222615-18-2-205.


Secretion of alpha toxin by Staphylococcus aureus strain Wood 46 was preferentially inhibited by cerulenin, an antibiotic that stops fatty-acid synthesis by inhibiting beta-keto acyl acyl carrier-protein synthetase. At the concentrations used, cerulenin had a negligible effect on cell growth and total protein synthesis, but reduced lipid synthesis by 50%. Extracellular and membrane-associated alpha toxin was absent in cultures treated with cerulenin, but toxin formation was resumed after either removal of the antibiotic or addition of exogenous fatty acids. The apparent absence of toxin precursor in membranes of inhibited cells favours inhibition at an earlier stage in toxin synthesis.

MeSH terms

  • Antifungal Agents / pharmacology*
  • Bacterial Proteins / analysis
  • Bacterial Proteins / biosynthesis
  • Bacterial Toxins / biosynthesis*
  • Cerulenin / pharmacology*
  • Hemolysin Proteins*
  • Lipids / biosynthesis
  • Membrane Proteins / analysis
  • Oleic Acid
  • Oleic Acids / pharmacology
  • Staphylococcus aureus / analysis
  • Staphylococcus aureus / drug effects
  • Staphylococcus aureus / metabolism*
  • Stearates / pharmacology


  • Antifungal Agents
  • Bacterial Proteins
  • Bacterial Toxins
  • Hemolysin Proteins
  • Lipids
  • Membrane Proteins
  • Oleic Acids
  • Stearates
  • staphylococcal alpha-toxin
  • Cerulenin
  • Oleic Acid