Abstract
Lipoteichoic acid (LTA) is an important cell wall component of Gram-positive bacteria. In Staphylococcus aureus it consists of a polyglycerolphosphate-chain that is retained within the membrane via a glycolipid. Using an immunofluorescence approach, we show here that the LTA polymer is not surface exposed in S. aureus, as it can only be detected after digestion of the peptidoglycan layer. S. aureus mutants lacking LTA are enlarged and show aberrant positioning of septa, suggesting a link between LTA synthesis and the cell division process. Using a bacterial two-hybrid approach, we show that the three key LTA synthesis proteins, YpfP and LtaA, involved in glycolipid production, and LtaS, required for LTA backbone synthesis, interact with one another. All three proteins also interacted with numerous cell division and peptidoglycan synthesis proteins, suggesting the formation of a multi-enzyme complex and providing further evidence for the co-ordination of these processes. When assessed by fluorescence microscopy, YpfP and LtaA fluorescent protein fusions localized to the membrane while the LtaS enzyme accumulated at the cell division site. These data support a model whereby LTA backbone synthesis proceeds in S. aureus at the division site in co-ordination with cell division, while glycolipid synthesis takes place throughout the membrane.
Highlights
A polyglycerolphosphate (PGP)-type of Lipoteichoic acid (LTA) is found in a variety of Gram-positive bacteria and its synthesis and function has been studied most extensively in S. aureus (Fischer, 1990; Rahman et al, 2009; Reichmann and Gründling, 2011)
We show here that the LTA polymer is not surface exposed in S. aureus, as it can only be detected after digestion of the peptidoglycan layer
Using a bacterial two-hybrid approach, we show that the three key LTA synthesis proteins, YpfP and LtaA, involved in glycolipid production, and LtaS, required for LTA backbone synthesis, interact with one another
Summary
A polyglycerolphosphate (PGP)-type of LTA is found in a variety of Gram-positive bacteria and its synthesis and function has been studied most extensively in S. aureus (Fischer, 1990; Rahman et al, 2009; Reichmann and Gründling, 2011). In this organism, the PGP backbone chain is decorated with D-alanine esters and linked to the outside of the membrane through a diglucosyldiacylglycerol (Glc2-DAG) glycolipid anchor (Duckworth et al, 1975; Fischer and Rosel, 1980; Kiriukhin et al, 2001; Gründling and Schneewind, 2007a). The three key enzymes YpfP, LtaA and LtaS are responsible for the synthesis of the core LTA structure in S. aureus
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