The mode of action of Sch 34343: affinity for the penicillin binding proteins of Escherichia coli K-12 and Bacteroides fragilis

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The competition of the new penem antibiotic, Sch 34343, for the penicillin-binding-proteins (PBPs) of Escherichia coli and Bacteroides fragilis was studied. Sch 34343 caused rounding of cells, and then sphaeroplast formation and lysis in both organisms. The primary target in both organisms was PBP 2, and at higher concentrations PBP 1a and 1b (and 1c in Bact. fragilis). These targets were inhibited at well below therapeutically achievable concentrations. The results indicate that in E. coli and Bact. fragilis, the bactericidal activity of Sch 34343 is related to inhibition of two out of three 'essential' PBPs.


Original languageEnglish
Pages (from-to)5-14
Number of pages10
JournalJournal of Antimicrobial Chemotherapy
Volume15 Suppl C
Publication statusPublished - Jun 1985


  • Anti-Bacterial Agents, Bacterial Proteins, Bacteroides fragilis, Carboxypeptidases, Carrier Proteins, Escherichia coli, Hexosyltransferases, Kinetics, Lactams, Microbial Sensitivity Tests, Muramoylpentapeptide Carboxypeptidase, Penicillin-Binding Proteins, Peptidyl Transferases