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The Staphylococcus aureus Chaperone PrsA Is a New Auxiliary Factor of Oxacillin Resistance Affecting Penicillin-Binding Protein 2A.

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Jousselin Ambre, Manzano Caroline, Biette Alexandra, Reed Patricia, Pinho Mariana G, Rosato Adriana E, Kelley William L, Renzoni Adriana,
Project Identification of molecular markers to detect emergence of low-level glycopeptide resistance in Staphylococcus aureus
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Original article (peer-reviewed)

Journal Antimicrobial agents and chemotherapy
Volume (Issue) 60(3)
Page(s) 1656 - 66
Title of proceedings Antimicrobial agents and chemotherapy
DOI 10.1128/aac.02333-15

Open Access

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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