Open AccessInhibition of Escherichia coli K-12 by β-Lactam Antibiotics With Poor Antibacterial Activity: Interaction of Permeability And Intrinsic Activity Against Penicillin-Binding Proteins
Author(s) -
Nigel A. C. Curtis,
C.G. Brown,
Mike Boxall,
Michael G. Boulton
Publication year - 1979
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.15.3.332
Subject(s) - cloxacillin , cephaloridine , escherichia coli , penicillin , microbiology and biotechnology , mutant , penicillin binding proteins , benzylpenicillin , antibiotics , chemistry , biology , biochemistry , cephalosporin , gene
The effect of methicillin, cloxacillin, 1078/1/1, penicillin G, and cephaloridine upon the penicillin-binding proteins of a permeability mutant of Escherichia coli K-12 and its isogenic wild type have been investigated. Comparison of the 50% inhibition values for the antibiotics against the penicillin-binding proteins of the two strains with the minimal inhibitory concentrations for the same compounds indicates that methicillin, cloxacillin, 1078/1/1, and to a lesser extent penicillin G, owe their poor antibacterial activity to exclusion from the bacterial cell, whereas cephaloridine is not excluded and is equally active against both the mutant and its wild type. The results further suggest that the lesion in the permeability mutant E. coli DC2 allows free access of all the compounds tested to the inner membrane target proteins.