ArticleAntimicrobial agents and chemotherapy2012
The posttranslocational chaperone lipoprotein PrsA is involved in both glycopeptide and oxacillin resistance in Staphylococcus aureus.
Article in Antimicrobial agents and chemotherapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 67 citations in OpenAlex.
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- Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A.BMC microbiology · 2024Article
- Flanking N- and C-terminal domains of PrsA inVirulence · 2023Article
- Molecular Determinants of β-Lactam Resistance in Methicillin-ResistantAntibiotics (Basel, Switzerland) · 2023Review
- Enhanced Cell Wall and Cell Membrane Activity Promotes Heat Adaptation ofInternational journal of molecular sciences · 2023Article
- Impact of Bicarbonate on PBP2a Production, Maturation, and Functionality in Methicillin-ResistantAntimicrobial agents and chemotherapy · 2023Article
- Characterization of antigen adjuvant interactions in polyacrylate adjuvanted vaccines.Biochemistry and biophysics reports · 2023Article
- Listeria monocytogenes two component system PieRS regulates secretion chaperones PrsA1 and PrsA2 and enhances bacterial translocation across the intestine.Molecular microbiology · 2022Article
- The Phosphatase Bph and Peptidyl-Prolyl Isomerase PrsA Are Required for Gelatinase Expression and Activity in Enterococcus faecalis.Journal of bacteriology · 2022Article
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- Antimicrobial resistance determinants are associated withMicrobial genomics · 2021Article
- Dalbavancin exposure in vitro selects for dalbavancin-non-susceptible and vancomycin-intermediate strains of methicillin-resistant Staphylococcus aureus.Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases · 2021Article
- Staphylococcus aureus Releases Proinflammatory Membrane Vesicles To Resist Antimicrobial Fatty Acids.mSphere · 2020Article
- Identification and optimization of PrsA in Bacillus subtilis for improved yield of amylase.Microbial cell factories · 2019Article
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- Dalbavancin Alone and in Combination with Ceftaroline against Four Different Phenotypes ofAntimicrobial agents and chemotherapy · 2019Article
- VraSR and Virulence Trait Modulation during Daptomycin Resistance in Methicillin-ResistantmSphere · 2019Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding in detail the factors which permit Staphylococcus aureus to counteract cell wall-active antibiotics is a prerequisite to elaborating effective strategies to prolong the usefulness of these drugs and define new targets for pharmacological intervention. Methicillin-resistant S. aureus (MRSA) strains are major pathogens of hospital-acquired and community-acquired infections and are most often treated with glycopeptides (vancomycin and teicoplanin) because of their resistance to most penicillins and a limited arsenal of clinically proven alternatives. In this study, we examined PrsA, a lipid-anchored protein of the parvulin PPIase family (peptidyl-prolyl cis/trans isomerase) found ubiquitously in all Gram-positive species, in which it assists posttranslocational folding at the outer surface of the cytoplasmic membrane. We show by both genetic and biochemical assays that prsA is directly regulated by the VraRS two-component sentinel system of cell wall stress. Disruption of prsA is tolerated by S. aureus, and its loss results in no detectable overt macroscopic changes in cell wall architecture or growth rate under nonstressed growth conditions. Disruption of prsA leads, however, to notable alterations in the sensitivity to glycopeptides and dramatically decreases the resistance of COL (MRSA) to oxacillin. Quantitative transcriptional analysis reveals that prsA and vraR are coordinately upregulated in a panel of stable laboratory and clinical glycopeptide-intermediate S. aureus (GISA) strains compared to their susceptible parents. Collectively, our results point to a role for prsA as a facultative facilitator of protein secretion or extracellular folding and provide a framework for understanding why prsA is a key element of the VraRS-mediated cell wall stress response.
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