Sesquiterpene farnesol as a competitive inhibitor of lipase activity of Staphylococcus aureus.

Staphylococcus aureus lipase (SAL) is known to possess broad substrate specificity for triacylglycerides. We found that a sub-minimum inhibitory concentration of farnesol (1000 mg L(-1)) inhibits this lipase activity on a Mueller-Hinton agar containing 1% Tween substrates. A quantitative lipase assay using p-nitrophenyl palmitate (pNPP) revealed that the inhibitory action of farnesol appears to be the result of the inhibition of lipase activity rather than of its secretion into the culture medium.

Sesquiterpene farnesol inhibits recycling of the C55 lipid carrier of the murein monomer precursor contributing to increased susceptibility to beta-lactams in methicillin-resistant Staphylococcus aureus.

Background And Objectives: The sesquiterpene farnesol, a natural plant metabolite, is known to intensify the effect of antimicrobial agents. However, the mode of action of its antimicrobial synergism has remained poorly understood. In this study, we investigated farnesol's synergistic effects on commonly used antimicrobials, beta-lactams in particular, to explore its potential inhibitory effect on cell wall synthesis.