Abstract
Phosphatidylcholine (PC) is an abundant phospholipid in eukaryotic membranes. Our understanding of PC biosynthesis and acyl chain remodeling in Saccharomyces cerevisiae has been expanded with the identification of a glycerophosphosphocholine acyltransferase (GPCAT), Gpc1. Gpc1 acylates glycerophosphocholine (GPC), a product of complete deacylation of PC, to form lysophosphotidylcholine (LysoPC). LysoPC can subsequently be converted to PC by Ale1. This PC deacylation reacylation pathway (PC‐DRP) defines a novel route for PC biosynthesis and provides a potential mechanism to alter the acyl chain composition of a PC molecule. Changes in acyl chain composition can, in turn, affect physical properties of a membrane, such as fluidity, width, thickness and shape. Gpc1 displays no homology to known acyltransferases and defines a new gene family with members in plants, animals and fungi. The pathogenic fungus Candida albicans displays robust transport of GPC into the cell. We have previously shown that the inability of C. albicans to transport GPC results in decreased virulence in a mouse model of disseminated candidiasis, implying this metabolite plays a role during pathogenicity. We have created a C. albicans diploid knockout of Gpc1 homolog (orf19.998) using a transient CRISPR Cas‐9 system. Preliminary lipid analyses indicate that Gpc1 impacts PC biosynthesis in vivo. The physiological roles of CaGpc1 are being examined through growth and expression studies. Conditions to be examined include those associated with the human host and virulence, including elevated temperature, serum exposure, and hyphae inducing conditions.Support or Funding InformationNIH R15 GM104876
Published Version
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