title: Differential localization of LTA synthesis proteins and their interaction with the cell division machinery in Staphylococcus aureus.
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.
authors.affiliation: Section of Microbiology and MRC Centre for Molecular Bacteriology and Infection, Imperial College London, London, SW7 2AZ, UK.
authors.forename: Nathalie T
authors.initials: NT
authors.lastname: Reichmann
authors.forename: Carolina
authors.initials: C
authors.lastname: Piçarra Cassona
authors.forename: João M
authors.initials: JM
authors.lastname: Monteiro
authors.forename: Amy L
authors.initials: AL
authors.lastname: Bottomley
authors.forename: Rebecca M
authors.initials: RM
authors.lastname: Corrigan
authors.forename: Simon J
authors.initials: SJ
authors.lastname: Foster
authors.forename: Mariana G
authors.initials: MG
authors.lastname: Pinho
authors.forename: Angelika
authors.initials: A
authors.lastname: Gründling
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000378:metabolism*; D002455:Cell Division; D002462:Cell Membrane / Q000737:chemistry; D017930:Genes, Reporter; D006017:Glycolipids / Q000096:biosynthesis; D008070:Lipopolysaccharides / Q000096:biosynthesis*; D008164:Luminescent Proteins / Q000032:analysis / Q000235:genetics; D008856:Microscopy, Fluorescence; D009097:Multienzyme Complexes / Q000378:metabolism; D025941:Protein Interaction Mapping; D011993:Recombinant Fusion Proteins / Q000032:analysis / Q000235:genetics; D013211:Staphylococcus aureus / Q000201:enzymology* / Q000502:physiology*; D013682:Teichoic Acids / Q000096:biosynthesis*; D020798:Two-Hybrid System Techniques
chemical_list: D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D006017:Glycolipids; D008070:Lipopolysaccharides; D008164:Luminescent Proteins; D009097:Multienzyme Complexes; D011993:Recombinant Fusion Proteins; D013682:Teichoic Acids; C009900:lipoteichoic acid