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J. Bacteriol. doi:10.1128/JB.01683-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Genes required for glycolipid synthesis and lipoteichoic acid anchoring in Staphylococcus aureus

Department of Microbiology, University of Chicago, Chicago, Illinois 60637

^* To whom correspondence should be addressed. Email: oschnee{at}bsd.uchicago.edu.

	Abstract

Staphylococcus aureus lipoteichoic acid (LTA) is composed of a linear 1,3-linked polyglycerolphosphate chain and tethered to the bacterial membrane by a glycolipid [diglucosyl-diacylglycerol (Glc₂-DAG)]. Glc₂-DAG is synthesized in the bacterial cytoplasm by YpfP, a processive enzyme that transfers glucose to diacylglycerol (DAG), using UDP-glucose as its substrate. Here we present evidence that the S. aureus -phosphoglucomutase (PgcA) and UTP: -glucose 1-phosphate uridyltransferase (GtaB) homologs are required for the synthesis of Glc₂-DAG. LtaA (lipoteichoic acid protein A), a predicted membrane permease whose structural gene is located in an operon with ypfP, is not involved in Glc₂-DAG synthesis but required for synthesis of glycolipid anchored LTA. Our data suggest a model whereby LtaA facilitates the transport of Glc₂-DAG from the inner (cytoplasmic) to the outer leaflet of the plasma membrane, delivering Glc₂-DAG as substrate for LTA synthesis, thereby generating glycolipid anchored LTA. Glycolipid anchoring of LTA appears to play an important role during infection, as S. aureus variants lacking ltaA display defects in the pathogenesis of animal infections.

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