Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O‐acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus

@article{Bera2005WhyAP,
  title={Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O‐acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus},
  author={Agnieszka Bera and Silvia Herbert and Andreas Jakob and Waldemar Vollmer and Friedrich G{\"o}tz},
  journal={Molecular Microbiology},
  year={2005},
  volume={55}
}
Staphylococcus species belong to one of the few bacterial genera that are completely lysozyme resistant, which greatly contributes to their persistence and success in colonizing the skin and mucosal areas of humans and animals. In an attempt to discover the cause of lysozyme resistance, we identified a gene, oatA, in Staphylococcus aureus. The corresponding oatA deletion mutant had an increased sensitivity to lysozyme. HPLC and electrospray ionization tandem mass spectrometry analyses of the… 
Molecular Basis of Resistance to Muramidase and Cationic Antimicrobial Peptide Activity of Lysozyme in Staphylococci
TLDR
It is shown that a Staphylococcus aureus double mutant defective in O-acetyltransferase A (OatA), and the glycopeptide resistance-associated two-component system, GraRS, is much more sensitive to lysozyme than S. aUREus with the oatA mutation alone.
The Lysozyme-Induced Peptidoglycan N-Acetylglucosamine Deacetylase PgdA (EF1843) Is Required for Enterococcus faecalis Virulence
TLDR
Results reveal that peptidoglycan deacetylation is a component of the arsenal that enables E. faecalis to thrive inside mammalian hosts, as both a commensal and a pathogen.
The Presence of Peptidoglycan O-Acetyltransferase in Various Staphylococcal Species Correlates with Lysozyme Resistance and Pathogenicity
ABSTRACT Human-pathogenic bacteria that are able to cause persistent infections must have developed mechanisms to resist the immune defense system. Lysozyme, a cell wall-lytic enzyme, is one of the
Enterococcus faecalis Constitutes an Unusual Bacterial Model in Lysozyme Resistance
TLDR
While EF_0783 is currently involved in the lyso enzyme resistance of E. faecalis, peptidoglycan O acetylation and de-N-acetylation are not the main mechanisms conferring high levels of lysozyme resistance to E. Faecalis.
Understanding the Structure-Function Relationship of Lysozyme Resistance in Staphylococcus aureus by Peptidoglycan O-Acetylation Using Molecular Docking, Dynamics, and Lysis Assay
TLDR
The results indicated for the first time that the active site cleft of lysozyme binding with O-acetylated peptidoglycan in S. aureus was sterically hindered and the structural stability was higher for the lyso enzyme in complex with normal peptidlycercan.
Lysozyme resistance in C. difficile is dependent on two peptidoglycan deacetylases
TLDR
It is concluded that peptidoglycan deacetylation is the major mechanism of lysozyme resistance in C. difficile and CRISPR-Cas9 mediated mutagenesis andCRISPRi knockdown are used to compare other lyso enzyme resistance mechanisms.
Characterization of Listeria monocytogenes Peptidoglycan N-Deacetylase and O-Acetylase Mutations and the Role of Lysozyme Resistance During Infection
TLDR
Notably, the addition of extracellular lysozyme to LysM-minus macrophages restored cytokine induction, host-cell death and L. monocytogenes growth inhibition, suggesting that extacellular ly sozyme can access the macrophage cytosol and act on intracellular, lyso enzyme-sensitive, bacteria.
In vitro characterization of the antivirulence target of Gram-positive pathogens, peptidoglycan O-acetyltransferase A (OatA)
TLDR
This study on the structure-function relationship of OatA provides a molecular and mechanistic understanding of this bacterial resistance mechanism opening the prospect for novel chemotherapeutic exploration to enhance innate immunity protection against Gram-positive pathogens.
Helicobacter pylori Peptidoglycan Modifications Confer Lysozyme Resistance and Contribute to Survival in the Host
TLDR
Two Helicobacter pylori PG modification enzymes (PgdA and PatA) confer a clear protective advantage to a Gram-negative bacterium, protecting the bacterium from lytic enzyme degradation, albeit via different PG modification activities.
Resistance to Mucosal Lysozyme Compensates for the Fitness Deficit of Peptidoglycan Modifications by Streptococcus pneumoniae
TLDR
It is shown that the antimicrobial effect of human lysozyme is due to its muramidase activity and that both peptidoglycan modifications are required for full resistance by pneumococci, and that individual peptidlycercan modifications diminish fitness during colonization.
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References

SHOWING 1-10 OF 45 REFERENCES
The pgdA Gene Encodes for a PeptidoglycanN-Acetylglucosamine Deacetylase in Streptococcus pneumoniae *
TLDR
The pgdA gene may contribute to pneumococcal virulence by providing protection against host lysozyme, which is known to accumulate in high concentrations at infection sites.
Inactivation of the dlt Operon inStaphylococcus aureus Confers Sensitivity to Defensins, Protegrins, and Other Antimicrobial Peptides*
TLDR
A role of thed-alanine-esterified teichoic acids which occur in many pathogenic bacteria in the protection against human and animal defense systems is proposed.
Alanylation of teichoic acids protects Staphylococcus aureus against Toll-like receptor 2-dependent host defense in a mouse tissue cage infection model.
TLDR
It is indicated that alanylated teichoic acids contribute to virulence of S. aureus, and TLR2 mediates host defense, which partly targets alanylation of cell envelope te Jerichoic acids.
Detailed Structural Analysis of the Peptidoglycan of the Human Pathogen Neisseria meningitidis*
TLDR
Comparison of the muropeptide composition of penicillin-susceptible and peniillin-intermediate clinical strains of meningococci showed a positive correlation between the minimum inhibitory concentration (MIC) ofPenicillin G and the amount of murpeptides carrying an intact pentapeptide chain in the peptidoglycan, suggesting reduced susceptibility to penicillins G in N. meningitidis.
O-acetylated peptidoglycan: its occurrence, pathobiological significance, and biosynthesis.
TLDR
The influence of O-acetylation of peptidoglycan on its resistance to degradation both in vitro and in vivo is addressed, the clinical importance of the modification, and the currently held views on the pathway for its biosynthesis are addressed.
Modification of peptidoglycan structure by penicillin action in cell walls of Proteus mirabilis.
Composition of cell wall peptidoglycan was studied in the gram-negative bacterium Proteus mirabilis and in different wall-defective growth forms of this organism which survive and multiply in the
...
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