SCE-963, a New Potent Cephalosporin with High Affinity for Penicillin-Binding Proteins 1 and 3 of Escherichia coli
Open Access
- 1 January 1979
- journal article
- research article
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 15 (1) , 20-27
- https://doi.org/10.1128/aac.15.1.20
Abstract
A few biochemical activities of SCE-963, a new cephalosporin with potent antibacterial activities against gram-negative bacteria, were compared with those of several currently available cephalosporins against strains of Escherichia coli K-12. The minimum inhibitory concentrations of SCE-963, cefazolin, cephaloridine, cephalothin, and cephalexin were 0.2, 1.56, 3.13, 12.5, and 25 μg/ml, respectively. Affinities of these cephalosporins for the penicillin-binding protein (PBP) 1B of E. coli correlated well with their antibacterial activities; among tested cephalosporins, SCE-963 showed the highest affinity for PBP 1B. SCE-963 inhibited cross-linking of peptidoglycan in a cell-free system the most strongly suggesting that this inhibition results from its high affinity for PBP 1B. SCE-963 also showed the highest affinity for PBP 3; it caused filamentation of cells over a wide range of relatively lower concentrations. Thus its superior antibacterial activity is believed to be manifested through its high affinity for the PBPs.This publication has 18 references indexed in Scilit:
- 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
- Identification of the binding protein which may be the target of penicillin action in Bacillus megateriumNature, 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
- Function of the Outer Membrane of Escherichia coli as a Permeability Barrier to Beta-Lactam AntibioticsAntimicrobial Agents and Chemotherapy, 1977
- Mutants of Escherichia coli which lack a component of penicillin‐binding protein 1 are viableFEBS Letters, 1977
- Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity.Proceedings of the National Academy of Sciences, 1977
- A method for measuring the outer membrane-permeability of .BETA.-lactam antibiotics in gram-negative bacteria.The Journal of Antibiotics, 1977
- Properties of the Penicillin‐Binding Proteins of Escherichia coli K12European Journal of Biochemistry, 1977
- Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.Proceedings of the National Academy of Sciences, 1975
- Isolation and characterization of a temperature-sensitive amber suppressor mutant of Escherichia coli K12Molecular Genetics and Genomics, 1973