Interaction of non-lytic beta-lactams with penicillin-binding proteins in Streptococcus pneumoniae

J Gen Microbiol. 1987 Mar;133(3):755-60. doi: 10.1099/00221287-133-3-755.


The monobactam aztreonam and the cephalosporin ceftazidime, beta-lactam antibiotics that possess the same side chain R1, showed unusual effects on exponentially growing pneumococci compared to other beta-lactams. Both antibiotics did not induce lysis even at concentrations up to 2 mg ml-1, values well above the respective MICs. However, morphological alterations and growth inhibition of the cells were observed at much lower concentrations. Binding to penicillin-binding proteins (PBPs) in vitro could be monitored directly by using anti-aztreonam antiserum and the Western blot technique. Both antibiotics showed high affinity for PBP 3, but had an extremely low affinity for PBP 2b. It is suggested that the failure to bind to PBP 2b is responsible for the failure to induce lysis in pneumococci.

MeSH terms

  • Acyltransferases / metabolism*
  • Anti-Bacterial Agents / pharmacology*
  • Aztreonam / pharmacology
  • Bacterial Proteins*
  • Carrier Proteins*
  • Ceftazidime / pharmacology
  • Hexosyltransferases / metabolism*
  • Multienzyme Complexes / metabolism*
  • Muramoylpentapeptide Carboxypeptidase*
  • Penicillin-Binding Proteins
  • Peptidyl Transferases / metabolism*
  • Streptococcus pneumoniae / drug effects*
  • Streptococcus pneumoniae / growth & development


  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Carrier Proteins
  • Multienzyme Complexes
  • Penicillin-Binding Proteins
  • Ceftazidime
  • Acyltransferases
  • Peptidyl Transferases
  • Hexosyltransferases
  • Muramoylpentapeptide Carboxypeptidase
  • Aztreonam