Characterization of a divergent vanD-type resistance element from the first glycopeptide-resistant strain of Enterococcus faecium isolated in Brazil

Antimicrob Agents Chemother. 2000 Dec;44(12):3444-6. doi: 10.1128/AAC.44.12.3444-3446.2000.

Abstract

Enterococcus faecium 10/96A from Brazil was resistant to vancomycin (MIC, 256 microg/ml) but gave no amplification products with primers specific for known van genotypes. A 2,368-bp fragment of a van cluster contained one open reading frame encoding a peptide with 83% amino acid identity to VanH(D), and a second encoding a D-alanine-D-lactate ligase with 83 to 85% identity to VanD. The divergent glycopeptide resistance phenotype was designated VanD4.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins / genetics*
  • Brazil
  • Drug Resistance, Microbial / genetics
  • Enterococcus faecium / drug effects
  • Enterococcus faecium / genetics*
  • Genetic Variation
  • Genotype
  • Glycopeptides
  • Humans
  • Molecular Sequence Data
  • Peptide Synthases*
  • Sequence Homology, Amino Acid

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Glycopeptides
  • Peptide Synthases
  • VanD protein, Enterococcus faecium

Associated data

  • GENBANK/AF277571