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Updated: Jan 19, 2026

Infecting Mice with Malassezia spp. to Study the Fungus-Host Interaction
Published on: November 6, 2019
Long-Chain Acyl-CoA Synthetase is Associated with the Growth of Malassezia spp
1, Kengo Tejima2, Xinyue Chen3
1School of Life Science and Technology, Tokyo Institute of Technology, J3-7, 4259 Nagatsuta, Midori-ku, Yokohama, Kanagawa 226-8501, Japan. tenagy@yahoo.com.
Abstract:
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. MgFaa1p and MpFaa1p 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.
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