title: A Staphylococcus aureus ypfP mutant with strongly reduced lipoteichoic acid (LTA) content: LTA governs bacterial surface properties and autolysin activity.
abstract: Many Gram-positive bacteria produce lipoteichoic acid (LTA) polymers whose physiological roles have remained a matter of debate because of the lack of LTA-deficient mutants. The ypfP gene responsible for biosynthesis of a glycolipid found in LTA was deleted in Staphylococcus aureus SA113, causing 87% reduction of the LTA content. Mass spectrometry and nuclear magnetic resonance spectroscopy revealed that the mutant LTA contained a diacylglycerol anchor instead of the glycolipid, whereas the remaining part was similar to the wild-type polymer except that it was shorter. The LTA mutant strain revealed no major changes in patterns of cell wall proteins or autolytic enzymes compared with the parental strain indicating that LTA may be less important in S. aureus protein attachment than previously thought. However, the autolytic activity of the mutant was strongly reduced demonstrating a role of LTA in controlling autolysin activity. Moreover, the hydrophobicity of the LTA mutant was altered and its ability to form biofilms on plastic was completely abrogated indicating a profound impact of LTA on physicochemical properties of bacterial surfaces. We propose to consider LTA and its biosynthetic enzymes as targets for new antibiofilm strategies.
authors.affiliation: Cellular and Molecular Microbiology Division, University of Tübingen, Department of Medical Microbiology and Hygiene, 72076 Tübingen, Germany.
authors.forename: Iris
authors.initials: I
authors.lastname: Fedtke
authors.forename: Diana
authors.initials: D
authors.lastname: Mader
authors.forename: Thomas
authors.initials: T
authors.lastname: Kohler
authors.forename: Hermann
authors.initials: H
authors.lastname: Moll
authors.forename: Graeme
authors.initials: G
authors.lastname: Nicholson
authors.forename: Raja
authors.initials: R
authors.lastname: Biswas
authors.forename: Katja
authors.initials: K
authors.lastname: Henseler
authors.forename: Friedrich
authors.initials: F
authors.lastname: Götz
authors.forename: Ulrich
authors.initials: U
authors.lastname: Zähringer
authors.forename: Andreas
authors.initials: A
authors.lastname: Peschel
mesh_terms: D000222:Adaptation, Physiological / Q000187:drug effects; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology; D018441:Biofilms / Q000187:drug effects; D002473:Cell Wall / Q000737:chemistry / Q000187:drug effects; D004187:Disaccharides / Q000378:metabolism; D017353:Gene Deletion; D005798:Genes, Bacterial; D005964:Glucosyltransferases / Q000235:genetics; D006017:Glycolipids / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D008070:Lipopolysaccharides / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D050296:Microbial Viability / Q000187:drug effects; D009154:Mutation / Q000235:genetics*; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism*; D012965:Sodium Chloride / Q000494:pharmacology; D013211:Staphylococcus aureus / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics* / Q000502:physiology; D013499:Surface Properties; D013682:Teichoic Acids / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D023181:Antimicrobial Cationic Peptides; D004187:Disaccharides; D006017:Glycolipids; D008070:Lipopolysaccharides; D013682:Teichoic Acids; D012965:Sodium Chloride; C009900:lipoteichoic acid; D005964:Glucosyltransferases; C100873:diglucosyldiacylglycerol synthase; D009238:N-Acetylmuramoyl-L-alanine Amidase