ArticleAntimicrobial agents and chemotherapy2015
The Staphylococcus aureus Chaperone PrsA Is a New Auxiliary Factor of Oxacillin Resistance Affecting Penicillin-Binding Protein 2A.
Article in Antimicrobial agents and chemotherapy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.
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Who cites it
47 citing papers in PubMed, 1 synthesis or guideline pooled it, 75 citations in OpenAlex.
- Adjuvant β-Lactam Therapy Combined with Vancomycin or Daptomycin for Methicillin-Resistant Staphylococcus aureus Bacteremia: a Systematic Review and Meta-analysis.Antimicrobial agents and chemotherapy · 2020Pooled it
- Mutation of lipoprotein processing pathway geneAntimicrobial agents and chemotherapy · 2026Article
- Methicillin-resistantiScience · 2026Review
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- Bicarbonate Within: A Hidden Modulator of Antibiotic Susceptibility.Antibiotics (Basel, Switzerland) · 2025Review
- Emerging Antimicrobial Strategies Against Heterogeneous and Vancomycin-IntermediateInternational journal of general medicine · 2025Review
- Article
- Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A.BMC microbiology · 2024Article
- Enhancing the antimicrobial activity of silver nanoparticles against ESKAPE bacteria and emerging fungal pathogens by using tea extracts.Nanoscale advances · 2023Article
- A Review on Five and Six-Membered Heterocyclic Compounds Targeting the Penicillin-Binding Protein 2 (PBP2A) of Methicillin-ResistantMolecules (Basel, Switzerland) · 2023Review
- Molecular Determinants of β-Lactam Resistance in Methicillin-ResistantAntibiotics (Basel, Switzerland) · 2023Review
- Pan-Genome-Wide Association Study of Serotype 19A Pneumococci Identifies Disease-Associated Genes.Microbiology spectrum · 2023Article
- Metabolic reprogramming and altered cell envelope characteristics in a pentose phosphate pathway mutant increases MRSA resistance to β-lactam antibiotics.PLoS pathogens · 2023Article
- Novel antimicrobial strategies to treat multi-drug resistant Staphylococcus aureus infections.Microbial biotechnology · 2023Review
- Impact of Bicarbonate on PBP2a Production, Maturation, and Functionality in Methicillin-ResistantAntimicrobial agents and chemotherapy · 2023Article
- Metabolic reprogramming and flux to cell envelope precursors in a pentose phosphate pathway mutant increases MRSA resistance to β-lactam antibiotics.bioRxiv : the preprint server for biology · 2023Article
- Antibacterial sensitizers from natural plants: A powerful weapon against methicillin-resistantFrontiers in pharmacology · 2023Review
- Important Roles and Potential Uses of Natural and Synthetic Antimicrobial Peptides (AMPs) in Oral Diseases: Cavity, Periodontal Disease, and Thrush.Journal of functional biomaterials · 2022Review
- The Phosphatase Bph and Peptidyl-Prolyl Isomerase PrsA Are Required for Gelatinase Expression and Activity in Enterococcus faecalis.Journal of bacteriology · 2022Article
- Targeting the Achilles' Heel of Multidrug-ResistantInternational journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Expression of the methicillin-resistant S. aureus (MRSA) phenotype results from the expression of the extra penicillin-binding protein 2A (PBP2A), which is encoded by mecA and acquired horizontally on part of the SCCmec cassette. PBP2A can catalyze dd-transpeptidation of peptidoglycan (PG) because of its low affinity for β-lactam antibiotics and can functionally cooperate with the PBP2 transglycosylase in the biosynthesis of PG. Here, we focus upon the role of the membrane-bound PrsA foldase protein as a regulator of β-lactam resistance expression. Deletion of prsA altered oxacillin resistance in three different SCCmec backgrounds and, more importantly, caused a decrease in PBP2A membrane amounts without affecting mecA mRNA levels. The N- and C-terminal domains of PrsA were found to be critical features for PBP2A protein membrane levels and oxacillin resistance. We propose that PrsA has a role in posttranscriptional maturation of PBP2A, possibly in the export and/or folding of newly synthesized PBP2A. This additional level of control in the expression of the mecA-dependent MRSA phenotype constitutes an opportunity to expand the strategies to design anti-infective agents.
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