Penicillin-binding protein 5 sequence alterations in clinical isolates of Enterococcus faecium with different levels of beta-lactam resistance

J Infect Dis. 1998 Jul;178(1):159-63. doi: 10.1086/515605.

Abstract

The low-affinity penicillin-binding protein (PBP) 5 is the main beta-lactam target and is responsible for resistance to this class of antibiotics in Enterococcus faecium. The PBP 5 variants of 15 clinical isolates (including 8 resistant to vancomycin) with different levels of beta-lactam resistance were analyzed. Most of the highly beta-lactam-resistant isolates produced small quantities of PBP 5 of low affinity. This was associated with particular amino acid substitutions: an Ala or Ile for Thr-499, a Glu for Val-629, and a Pro for Ser-667. A change of Met-485 to Thr or Ala (adjacent to the conserved SDN box) was observed in isolates with MICs of ampicillin of 64 or 128 microg/mL, respectively. In the 2 most resistant isolates, with MICs of ampicillin of 256 microg/mL, an additional Ser was present just after Ser-466. Thus, particular point mutations in PBP 5 and combinations thereof may lead to high-level beta-lactam resistance in E. faecium.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Ampicillin / pharmacology
  • Bacterial Proteins*
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism
  • Drug Resistance, Microbial
  • Enterococcus faecium / drug effects*
  • Enterococcus faecium / genetics*
  • Enterococcus faecium / isolation & purification
  • Genetic Variation
  • Gram-Positive Bacterial Infections / microbiology
  • Hexosyltransferases*
  • Humans
  • Imipenem / pharmacology
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Muramoylpentapeptide Carboxypeptidase / chemistry
  • Muramoylpentapeptide Carboxypeptidase / genetics*
  • Muramoylpentapeptide Carboxypeptidase / metabolism
  • Penicillin G / metabolism
  • Penicillin G / pharmacology
  • Penicillin Resistance / genetics
  • Penicillin-Binding Proteins
  • Peptidyl Transferases*
  • Piperacillin / pharmacology
  • Sequence Homology, Amino Acid
  • Vancomycin / pharmacology
  • beta-Lactam Resistance / genetics*

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Penicillin-Binding Proteins
  • Vancomycin
  • Imipenem
  • Ampicillin
  • Peptidyl Transferases
  • Hexosyltransferases
  • Muramoylpentapeptide Carboxypeptidase
  • Penicillin G
  • Piperacillin