Penicillin-binding proteins of Pseudomonas aeruginosa. Comparison of two strains differing in their resistance to β-lactam antibiotics
- 1 February 1981
- journal article
- research article
- Published by Oxford University Press (OUP) in Journal of Antimicrobial Chemotherapy
- Vol. 7 (2) , 127-136
- https://doi.org/10.1093/jac/7.2.127
Abstract
The contributions of inducible β-lactamase, penicillin-binding protein (PBP) affinity and envelope permeability to the resistance phenotype of two strains of Pseudomonas aeruginosa. which differ markedly in their sensitivities to β-lactam antibiotics, have been investigated. The isolation of β-lactamase non-inducible mutants of the two Ps. aeruginosa strains indicated that the enzyme provided protection against antibiotics sensitive to it. Furthermore, one of the strains, but not the other, still possessed significant resistance levels in the absence of its inducible β-lactamase. Comparison of the affinities of selected β-lactam antibiotics for the PBPs of the two non-inducible mutants with their antibacterial activities indicated that the two Ps. aeruginosa strains owed their differences in non-β-lactamase-mediated resistance primarily to differences in their ability to exclude the compounds by their respective permeability barriers rather than to variations in PBP target affinity or to the stability of PBP-inhibitor complexes.Keywords
This publication has 13 references indexed in Scilit:
- Mutational evidence for identity of penicillin-binding protein 5 in Escherichia coli with the major D-alanine carboxypeptidase IA activityJournal of Bacteriology, 1979
- Modified Peptidoglycan Transpeptidase Activity in a Carbenicillin-Resistant Mutant of Pseudomonas aeruginosa 18sAntimicrobial Agents and Chemotherapy, 1978
- On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins.Proceedings of the National Academy of Sciences, 1978
- Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis in vitro.Proceedings of the National Academy of Sciences, 1977
- Simultaneous deletion of D-alanine carboxypeptidase IB-C and penicillin-binding component IV in a mutant of Escherichia coli K12.Proceedings of the National Academy of Sciences, 1977
- Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity.Proceedings of the National Academy of Sciences, 1977
- Temperature-Sensitive Cell Division Mutants of Escherichia coli with Thermolabile Penicillin-Binding ProteinsJournal of Bacteriology, 1977
- Properties of the Penicillin‐Binding Proteins of Escherichia coli K12European Journal of Biochemistry, 1977
- Cephalosporinase and penicillinase activities of a β-lactamase from Pseudomonas pyocyaneaBiochemical Journal, 1965
- Micro-iodometric assay for penicillinaseBiochemical Journal, 1962