Long-Chain Acyl-CoA Synthetase is Associated with the Growth of <i>Malassezia</i> spp.

The lipophilic fungal pathogen <i>Malassezia</i> 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 <i>FA...

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Bibliographic Details
Main Authors: Tenagy, Kengo Tejima, Xinyue Chen, Shun Iwatani, Susumu Kajiwara
Format: Article
Language:English
Published: MDPI AG 2019-09-01
Series:Journal of Fungi
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Online Access:https://www.mdpi.com/2309-608X/5/4/88
Description
Summary:The lipophilic fungal pathogen <i>Malassezia</i> 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 <i>FAA1</i> in three <i>Malassezia</i> spp.: <i>M</i>. <i>globosa</i>, <i>M. pachydermatis</i>, and <i>M. sympodialis.</i> These <i>FAA1</i> genes could compensate for the double mutation of <i>FAA1</i> and <i>FAA4</i> in <i>Saccharomyces cerevisiae</i>, suggesting that <i>Malassezia</i> Faa1 protein recognizes exogenous LCFAs. <i>Mg</i>Faa1p and <i>Mp</i>Faa1p utilized a medium-chain fatty acid, lauric acid (C12:0). Interestingly, the ACS inhibitor, triacsin C, affected the activity of the <i>Malassezia</i> Faa1 proteins but not that of <i>S. cerevisiae</i>. Triacsin C also reduced the growth of <i>M. globosa</i>, <i>M. pachydermatis</i>, and <i>M. sympodialis</i>. These results suggest that triacsin C and its derivatives are potential compounds for the development of new anti-<i>Malassezia</i> drugs.
ISSN:2309-608X