Role of penicillin-binding proteins in the initiation of the AmpC beta-lactamase expression in Enterobacter cloacae

Antimicrob Agents Chemother. 2000 Jan;44(1):169-72. doi: 10.1128/AAC.44.1.169-172.2000.

Abstract

Penicillin-binding proteins (PBPs) are involved in the regulation of beta-lactamase expression by determining the level of anhydromuramylpeptides in the periplasmatic space. It was hypothesized that one or more PBPs act as a sensor in the beta-lactamase induction pathway. We have performed induction studies with Escherichia coli mutants lacking one to four PBPs with DD-carboxypeptidase activity. Therefore, we conclude that a strong beta-lactamase inducer must inhibit all DD-carboxypeptidases as well as the essential PBPs 1a, 1b, and/or 2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Carboxypeptidases / antagonists & inhibitors
  • Carboxypeptidases / physiology
  • Carrier Proteins / physiology*
  • Enterobacter cloacae / drug effects
  • Enterobacter cloacae / enzymology*
  • Enzyme Induction
  • Hexosyltransferases*
  • Microbial Sensitivity Tests
  • Muramoylpentapeptide Carboxypeptidase / physiology*
  • Penicillin-Binding Proteins
  • Peptidyl Transferases*
  • beta-Lactamases / biosynthesis*

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Penicillin-Binding Proteins
  • Peptidyl Transferases
  • Hexosyltransferases
  • Carboxypeptidases
  • Muramoylpentapeptide Carboxypeptidase
  • AmpC beta-lactamases
  • beta-Lactamases