A Staphylococcus aureus ypfP mutant with strongly reduced lipoteichoic acid (LTA) content: LTA governs bacterial surface properties and autolysin activity
| Autor: | Andreas Peschel, Graeme J. Nicholson, Iris Fedtke, Thomas P. Kohler, Diana Mader, Ulrich Zähringer, Friedrich Götz, Katja Henseler, Raja Biswas, Hermann Moll |
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| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
Lipopolysaccharides
Staphylococcus aureus Magnetic Resonance Spectroscopy Surface Properties Mutant Biology Sodium Chloride Disaccharides Microbiology Cell wall chemistry.chemical_compound Glycolipid Cell Wall N-acetylmuramoyl-L-alanine amidase Molecular Biology Research Articles Diacylglycerol kinase Teichoic acid Microbial Viability Autolysin N-Acetylmuramoyl-L-alanine Amidase respiratory system Adaptation Physiological carbohydrates (lipids) Teichoic Acids stomatognathic diseases chemistry Biochemistry Genes Bacterial Glucosyltransferases Biofilms Mutation lipids (amino acids peptides and proteins) Lipoteichoic acid Glycolipids Hydrophobic and Hydrophilic Interactions Gene Deletion Antimicrobial Cationic Peptides |
| Zdroj: | Molecular Microbiology |
| ISSN: | 1365-2958 0950-382X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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