Open AccessAffinities of penicillins and cephalosporins for the penicillin-binding proteins of Escherichia coli K-12 and their antibacterial activity
Author(s) -
Nigel A. C. Curtis,
David C. Orr,
Gayle Ross,
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.16.5.533
Subject(s) - penicillin binding proteins , cephalosporin , escherichia coli , penicillin , affinities , mutant , microbiology and biotechnology , chemistry , antibacterial activity , binding affinities , antibacterial agent , antibiotics , enterobacteriaceae , bacteria , biology , biochemistry , receptor , genetics , gene
The affinities of a range of penicillins and cephalosporins for ther penicillin-binding proteins of Escherichia coli K-12 have been studied, and the results were compared with the antibacterial activity of the compounds against E. coli K-12 and an isogenic permeability mutant. Different penicillins and cephalosporins exhibited different affinities for the "essential" penicillin-binding proteins of E. coli K-12, in a manner which directly correlated with their observed effects upon bacterial morphology. Furthermore, the affinities of the compounds for their "primary" lethal penicillin-binding protein targets showed close agreement with their antibacterial activities against the permeability mutant.