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Related Experiment Videos

Inducible, transferable resistance to vancomycin in Enterococcus faecalis A256.

D M Shlaes1, A Bouvet, C Devine

  • 1Département de Microbiologie Médicale, Faculté de Médecine, Université Pierre et Marie Curie, Paris, France.

Antimicrobial Agents and Chemotherapy
|February 1, 1989
PubMed
Summary

A strain of Enterococcus faecalis developed resistance to glycopeptides, including vancomycin. This resistance is linked to a specific 39-kDa protein and is transferable between bacteria.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Pharmacology

Background:

  • Enterococcus faecalis is a common cause of urinary tract infections.
  • Glycopeptides, such as vancomycin, are critical antibiotics for treating infections caused by Gram-positive bacteria.
  • Emergence of antibiotic resistance in E. faecalis poses a significant public health threat.

Purpose of the Study:

  • To investigate the mechanism of glycopeptide resistance in a clinical isolate of Enterococcus faecalis (A256).
  • To determine the role of specific proteins in mediating this resistance.
  • To assess the transferability of glycopeptide resistance.

Main Methods:

  • Isolation and susceptibility testing of Enterococcus faecalis A256 to various glycopeptides.
  • Growth rate analysis before and after exposure to sub-inhibitory concentrations (sub-MICs) of glycopeptides.

Related Experiment Videos

  • Measurement of peptidoglycan synthesis inhibition.
  • Analysis of protein synthesis, specifically a 39-kilodalton (kDa) protein.
  • Bacterial conjugation experiments to assess resistance transfer.

    • Main Results:

    • Enterococcus faecalis A256 exhibited high-level resistance to vancomycin and other glycopeptides.
    • Exposure to sub-MICs of vancomycin induced self-resistance and cross-resistance to other glycopeptides.
    • A 39-kDa protein in the cytoplasmic membrane was found to be upregulated upon glycopeptide exposure.
    • Vancomycin resistance was transferable to susceptible E. faecalis strains via conjugation.
    • The 39-kDa protein was also inducible in transconjugants.

    Conclusions:

    • The glycopeptide resistance in E. faecalis A256 is mediated by the inducible synthesis of a 39-kDa cytoplasmic membrane protein.
    • This protein likely hinders glycopeptide access to their peptidoglycan targets.
    • The resistance mechanism is transferable, suggesting a potential for rapid dissemination in clinical settings.