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The Staphylococcus aureus Chaperone PrsA Is a New Auxiliary Factor of Oxacillin Resistance Affecting

Ambre Jousselin1, Caroline Manzano2, Alexandra Biette2

  • 1Infectious Diseases Service, University Hospital and Medical School of Geneva, Geneva, Switzerland Laboratory of Bacterial Cell Biology, Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.

Antimicrobial Agents and Chemotherapy
|December 30, 2015
PubMed

Insights

The PrsA protein regulates methicillin-resistant Staphylococcus aureus (MRSA) by controlling the amount of PBP2A protein, a key factor in beta-lactam antibiotic resistance. This finding offers new strategies for developing anti-infective agents.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Methicillin-resistant Staphylococcus aureus (MRSA) resistance is mediated by PBP2A, encoded by mecA.
  • PBP2A has low affinity for beta-lactam antibiotics and is crucial for peptidoglycan biosynthesis.
  • The SCCmec cassette facilitates horizontal gene transfer of mecA.

Purpose of the Study:

  • Investigate the role of the membrane-bound PrsA protein in regulating beta-lactam resistance expression in MRSA.
  • Determine how PrsA affects PBP2A levels and oxacillin resistance.

Main Methods:

  • Deletion of the prsA gene in MRSA strains.
  • Quantification of PBP2A membrane levels.
  • Measurement of mecA mRNA levels.
  • Analysis of N- and C-terminal domains of PrsA.

Main Results:

  • Deletion of prsA altered oxacillin resistance across different SCCmec backgrounds.
  • prsa deletion decreased PBP2A membrane protein levels without affecting mecA mRNA.
  • Specific domains of PrsA were critical for PBP2A membrane levels and resistance.

Conclusions:

  • PrsA acts as a regulator of beta-lactam resistance by influencing PBP2A levels post-transcriptionally.
  • PrsA may be involved in the maturation, export, or folding of PBP2A.
  • Targeting PrsA offers a novel strategy for developing anti-MRSA agents.

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