Ampicillin resistance in Haemophilus influenzae: identification of resistance mechanisms

J Antimicrob Chemother. 1987 Nov;20(5):645-56. doi: 10.1093/jac/20.5.645.

Abstract

The incidence and mechanisms of ampicillin resistance (MIC greater than 1 mg/l) were investigated in 105 clinical isolates of Haemophilus influenzae collected in Edinburgh during 1983/4. Fifteen (14.3%) ampicillin-resistant strains were identified and these were non-serotypable and comprised six biotypes. Isoelectric focusing and beta-lactamase-inhibition studies demonstrated that production of the TEM-1 beta-lactamase was the principal mechanism of resistance in nine (60%) strains. Radiolabelling revealed that one beta-lactamase-positive strain also had an unusual penicillin-binding protein (PBP) profit. No beta-lactamase activity was detected in the other six (40%) ampicillin-resistant strains. Two beta-lactamase-negative ampicillin-resistant strains had atypical PBP profiles. SDS-PAGE analysis showed that four beta-lactamase-negative ampicillin-resistant strains, including one with altered PBPs, exhibited outer membrane protein profiles which differed from those of sensitive strains of the same biotype. The ampicillin-resistance mechanism of the remaining strain could not be determined. Thus, several resistance mechanisms, either acting individually or in combination, are implicated in ampicillin resistance in H. influenzae.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ampicillin / pharmacology*
  • Ampicillin Resistance*
  • Bacterial Outer Membrane Proteins / biosynthesis
  • Bacterial Proteins*
  • Carrier Proteins / biosynthesis
  • Cephalosporins / pharmacology
  • Haemophilus influenzae / drug effects*
  • Haemophilus influenzae / enzymology
  • Hexosyltransferases*
  • Isoelectric Focusing
  • Microbial Sensitivity Tests
  • Muramoylpentapeptide Carboxypeptidase / biosynthesis
  • Penicillin-Binding Proteins
  • Peptidyl Transferases*
  • beta-Lactamases / metabolism

Substances

  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Carrier Proteins
  • Cephalosporins
  • Penicillin-Binding Proteins
  • Ampicillin
  • Peptidyl Transferases
  • Hexosyltransferases
  • Muramoylpentapeptide Carboxypeptidase
  • beta-Lactamases
  • nitrocefin