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Biosensor for Detection of Antibiotic Resistant Staphylococcus Bacteria
Published on: May 8, 2013
An electronmicroscope study of glycopeptide antibiotic-resistant strains of Staphylococcus epidermidis
1Department of Microbiology, University Hospital, Queen's Medical Centre, Nottingham.
Abstract:
Ultra-thin section transmission electronmicroscopy revealed that two of three glycopeptide-resistant strains of Staphylococcus epidermidis had abnormally thick cell walls, a finding consistent with the view that the reduction in susceptibility may result from the overproduction of glycopeptide binding sites within the cell-wall peptidoglycan. The third resistant strain had a slightly thickened cell wall with an irregular, roughened outline; this strain also underwent autolysis on prolonged incubation on blood agar and the resistance may be associated with abnormal cell-wall synthesis. Sub-MIC concentrations of vancomycin and teicoplanin caused surface damage to a proportion of cocci able to grow in the presence of antibiotic. Exposure to teicoplanin was additionally associated with the formation of filamentous forms and variable amounts of extracellular material. Transmission electronmicroscopy showed that both antibiotics exerted effects within the bacterial cytoplasm of the resistant strains that were not seen in an NCTC control strain: intracellular lamellae and structures resembling mesosomes were observed in the former. These effects were more noticeable in cocci exposed to vancomycin. Bacteria exposed to teicoplanin often showed abnormal septation and, in some preparations, a double-layered cell wall.
Insights
Glycopeptide-resistant Staphylococcus epidermidis strains exhibit thickened cell walls, potentially due to increased binding sites. Antibiotic exposure caused cytoplasmic changes and cell surface alterations in these resistant bacteria.
Area of Science:
- Microbiology
- Cell Biology
- Infectious Diseases
Background:
- Staphylococcus epidermidis is a common cause of nosocomial infections.
- Glycopeptide antibiotics like vancomycin are crucial for treating resistant bacterial infections.
- Understanding the mechanisms of glycopeptide resistance in S. epidermidis is essential for effective treatment.
Purpose of the Study:
- To investigate the ultrastructural changes in glycopeptide-resistant Staphylococcus epidermidis strains.
- To elucidate the effects of sub-inhibitory concentrations of vancomycin and teicoplanin on resistant S. epidermidis.
Main Methods:
- Ultra-thin section transmission electron microscopy was used to examine bacterial cell wall and cytoplasmic structures.
- Resistant and control strains of Staphylococcus epidermidis were cultured and exposed to sub-minimum inhibitory concentrations (sub-MIC) of vancomycin and teicoplanin.
Main Results:
- Two resistant strains showed abnormally thick cell walls, suggesting increased glycopeptide binding sites.
- A third resistant strain exhibited a thickened, irregular cell wall and autolysis, indicating abnormal cell wall synthesis.
- Sub-MIC vancomycin and teicoplanin induced cytoplasmic changes, including intracellular lamellae and mesosome-like structures, in resistant strains.
- Teicoplanin exposure also led to filamentous forms, extracellular material, abnormal septation, and a double-layered cell wall in some resistant bacteria.
Conclusions:
- Glycopeptide resistance in Staphylococcus epidermidis may be associated with altered cell wall synthesis and structure.
- Vancomycin and teicoplanin can induce distinct ultrastructural changes within the cytoplasm and cell envelope of resistant S. epidermidis.
- These findings provide insights into the morphological adaptations and cellular responses contributing to glycopeptide resistance in this opportunistic pathogen.
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