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The lipophilic fungal pathogen Malassezia spp. must acquire long-chain fatty acids (LCFAs) from outside the cell. To clarify the mechanism of LCFA acquisition, we investigated fatty acid uptake by this fungus and identified the long-chain acyl-CoA synthetase (ACS) gene FAA1 in three Malassezia spp.: M . globosa , M. pachydermatis , and M. sympodialis. These FAA1 genes could compensate for the double mutation of FAA1 and FAA4 in Saccharomyces cerevisiae , suggesting that Malassezia Faa1 protein recognizes exogenous LCFAs. Mg Faa1p and Mp Faa1p utilized a medium-chain fatty acid, lauric acid (C12:0). Interestingly, the ACS inhibitor, triacsin C, affected the activity of the Malassezia Faa1 proteins but not that of S. cerevisiae . Triacsin C also reduced the growth of M. globosa , M. pachydermatis , and M. sympodialis . These results suggest that triacsin C and its derivatives are potential compounds for the development of new anti- Malassezia drugs.

Long-Chain Acyl-CoA Synthetase is Associated with the Growth of Malassezia spp.