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Updated: Jul 10, 2026

Biosensor for Detection of Antibiotic Resistant Staphylococcus Bacteria
Published on: May 8, 2013
Penicillin-binding proteins and cell wall composition in beta-lactam-sensitive and -resistant strains of
Yanjiao Zhou1, Aude Antignac, Shang Wei Wu
1Laboratory of Microbiology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Abstract:
A close homologue of the acquired Staphylococcus aureus mecA gene is present as a native gene in Staphylococcus sciuri. We determined the patterns of penicillin-binding proteins (PBPs) and the peptidoglycan compositions of several S. sciuri strains to explore the functions of this mecA homologue, named pbpD, in its native S. sciuri environment. The protein product of pbpD was identified as PBP4 with a molecular mass of 84 kDa, one of the six PBPs present in representatives of each of three subspecies of S. sciuri examined. PBP4 had a low affinity for nafcillin, reacted with a monoclonal antibody raised against S. aureus PBP2A, and was greatly overproduced in oxacillin-resistant clinical isolate S. sciuri SS37 and to a lesser extent in resistant laboratory mutant K1M200. An additional PBP inducible by oxacillin and corresponding to S. aureus PBP2A was identified in another oxacillin-resistant clinical isolate, S. sciuri K3, which harbors an S. aureus copy of mecA. Oxacillin resistance depended on the overtranscribed S. sciuri pbpD gene in strains SS37 and K1M200, while the resistance of strain K3 depended on the S. aureus copy of mecA. Our data provide evidence that both S. aureus mecA and S. sciuri pbpD can function as resistance determinants in either an S. aureus or an S. sciuri background and that the protein products of these genes, S. aureus PBP2A and S. sciuri PBP4, can participate in the biosynthesis of peptidoglycan, the muropeptide composition of which depends on the bacterium "hosting" the resistance gene.
Insights
A native Staphylococcus sciuri gene, pbpD, functions similarly to the acquired Staphylococcus aureus mecA gene. Both genes confer oxacillin resistance by altering peptidoglycan biosynthesis in their respective bacterial hosts.
Area of Science:
- Microbiology
- Molecular Biology
- Genetics
Background:
- The Staphylococcus aureus mecA gene confers methicillin resistance by encoding a penicillin-binding protein (PBP2A) with low affinity for beta-lactam antibiotics.
- A homologous gene, pbpD, exists naturally in Staphylococcus sciuri, suggesting potential roles in antibiotic resistance or cell wall synthesis.
Purpose of the Study:
- To investigate the function of the S. sciuri pbpD gene, a homologue of S. aureus mecA, within its native S. sciuri environment.
- To characterize the penicillin-binding protein (PBP) patterns and peptidoglycan composition in S. sciuri strains with varying resistance profiles.
Main Methods:
- Penicillin-binding protein (PBP) profiling using techniques like SDS-PAGE and Western blotting with specific antibodies.
- Analysis of peptidoglycan muropeptide composition.
- Genetic analysis of oxacillin-resistant S. sciuri isolates (SS37, K1M200, K3) and laboratory mutants.
Main Results:
- The S. sciuri pbpD gene product, identified as PBP4, is a 84 kDa protein with low nafcillin affinity and cross-reacts with anti-S. aureus PBP2A antibodies.
- PBP4 was overproduced in oxacillin-resistant S. sciuri strains SS37 and K1M200, with resistance attributed to the overtranscribed pbpD gene.
- An S. aureus mecA gene conferred oxacillin resistance in S. sciuri strain K3, demonstrating functional conservation across species.
Conclusions:
- Both S. aureus mecA and S. sciuri pbpD can act as determinants of oxacillin resistance in both S. aureus and S. sciuri.
- The protein products, S. aureus PBP2A and S. sciuri PBP4, are involved in peptidoglycan biosynthesis.
- The specific muropeptide composition of the peptidoglycan is influenced by the bacterial host carrying the resistance gene.
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