Open AccessGenes Required for Glycolipid Synthesis and Lipoteichoic Acid Anchoring in Staphylococcus aureus
Author(s) -
Angelika Gründling,
Olaf Schneewind
Publication year - 2007
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.01683-06
Subject(s) - lipoteichoic acid , diacylglycerol kinase , glycolipid , biology , biochemistry , operon , teichoic acid , bacterial outer membrane , staphylococcus aureus , microbiology and biotechnology , bacteria , peptidoglycan , enzyme , gene , escherichia coli , protein kinase c , genetics
Staphylococcus aureus lipoteichoic acid (LTA) is composed of a linear 1,3-linked polyglycerolphosphate chain and is 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 theS. aureus α-phosphoglucomutase (PgcA) and UTP:α-glucose 1-phosphate uridyltransferase (GtaB) homologs are required for the synthesis of Glc2 -DAG. LtaA (l ipot eichoica cid proteinA ), a predicted membrane permease whose structural gene is located in an operon withypfP , is not involved in Glc2 -DAG synthesis but is required for synthesis of glycolipid-anchored LTA. Our data suggest a model in which LtaA facilitates the transport of Glc2 -DAG from the inner (cytoplasmic) leaflet to the outer leaflet of the plasma membrane, delivering Glc2 -DAG as a substrate for LTA synthesis, thereby generating glycolipid-anchored LTA. Glycolipid anchoring of LTA appears to play an important role during infection, asS. aureus variants lackingltaA display defects in the pathogenesis of animal infections.