Interaction of ceftobiprole with the low-affinity PBP 5 of Enterococcus faecium

Antimicrob Agents Chemother. 2010 Feb;54(2):953-5. doi: 10.1128/AAC.00983-09. Epub 2009 Nov 16.

Abstract

Ceftobiprole is a new cephalosporin that exhibits a high level of affinity for methicillin-resistant Staphylococcus aureus PBP 2a. It was reported that ceftobiprole did not interact with a mutated form of the low-affinity protein Enterococcus faecium PBP 5 (PBP 5fm) that, when overexpressed, confers a beta-lactam resistance phenotype to the bacterium. Our results show that ceftobiprole binds to unmutated PBP 5fm to form a stable acyl-enzyme and that ceftobiprole is able to efficiently kill a penicillin-resistant Enterococcus faecium strain that produces this protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / metabolism*
  • Anti-Bacterial Agents / pharmacology*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Cephalosporins / metabolism*
  • Cephalosporins / pharmacology*
  • Enterococcus faecium / drug effects*
  • Enterococcus faecium / genetics
  • Enterococcus faecium / metabolism*
  • Microbial Sensitivity Tests
  • Penicillin G / pharmacology
  • Protein Binding / genetics

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Cephalosporins
  • ceftobiprole
  • Penicillin G