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Related Experiment Videos

VanD-type glycopeptide-resistant Enterococcus faecium BM4339

B Perichon1, P Reynolds, P Courvalin

  • 1Unité des Agents Antibactériens, Institut Pasteur, Paris, France. brunoper@pasteur.fr

Antimicrobial Agents and Chemotherapy
|September 26, 1997
PubMed
Summary
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Enterococcus faecium BM4339 exhibits vancomycin and teicoplanin resistance due to a novel mechanism. This glycopeptide resistance phenotype, designated VanD, involves the synthesis of peptidoglycan precursors terminating in D-lactate.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Enterococcus faecium is a significant cause of nosocomial infections.
  • Glycopeptide antibiotics, such as vancomycin, are crucial for treating infections caused by Gram-positive bacteria.
  • Emergence of vancomycin-resistant enterococci (VRE) poses a serious threat to public health.

Purpose of the Study:

  • To investigate the mechanism of vancomycin and teicoplanin resistance in Enterococcus faecium BM4339.
  • To characterize the genetic basis of this novel glycopeptide resistance phenotype.

Main Methods:

  • Phenotypic characterization of antibiotic resistance.
  • Gene amplification using specific primers (V1 and V2).
  • DNA sequencing and amino acid sequence analysis of amplified gene products.

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Main Results:

  • Enterococcus faecium BM4339 demonstrated constitutive resistance to vancomycin (MIC, 64 µg/ml) and teicoplanin (MIC, 4 µg/ml).
  • Sequencing revealed a gene encoding a protein with 69% identity to VanA/VanB and 43% identity to VanC.
  • The bacterium synthesized peptidoglycan precursors terminating in D-lactate, indicating a distinct resistance mechanism.

Conclusions:

  • A new type of glycopeptide resistance, designated VanD, was identified in Enterococcus faecium BM4339.
  • This resistance is associated with the synthesis of D-lactate-terminating peptidoglycan precursors.
  • The VanD phenotype represents a novel mechanism of glycopeptide resistance in enterococci.