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Article Abstract
In this study, we have specifically blocked a key step of sphingolipid (SL) biosynthesis in by disruption of the orthologs of ScIpt1 and ScSkn1. Based on their close homology with counterparts, the proteins are predicted to catalyze the addition of a phosphorylinositol group onto mannosyl inositolphosphoryl ceramide (MIPC) to form mannosyl diinositolphosphoryl ceramide (M(IP)C), which accounts for the majority of complex SL structures in membranes. High throughput lipidome analysis confirmed the accumulation of MIPC structures in and cells, albeit to lesser extent in the latter. Noticeably, cells showed an increased susceptibility to azoles; however, cells showed no significant changes in the drug susceptibility profiles. Interestingly, the azole susceptible phenotype of cells seems to be independent of the ergosterol content. cells displayed altered lipid homeostasis, increased membrane fluidity as well as high diffusion of radiolabeled fluconazole (H-FLC), which could together influence the azole susceptibility of . Furthermore, in vivo experiments also confirmed compromised virulence of the strain. Contrarily, specific functions of CgSkn1 remain unclear.
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| http://dx.doi.org/10.3390/jof8070651 | DOI Listing |
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