Improved sensitivity in assays for binding of novel beta-lactam antibiotics to penicillin-binding proteins of Escherichia coli

Author:

Bush K,Smith S A,Ohringer S,Tanaka S K,Bonner D P

Abstract

Tigemonam and temocillin, but not aztreonam, bound to penicillin-binding proteins (PBPs) 1a and 3 of Escherichia coli with apparent improved affinity when challenged with benzylpenicillin at lowered temperatures. Half times for deacylation of the tigemonam-PBP complexes were shorter than were those of the corresponding aztreonam-PBP complexes. The implications of the routine testing of PBP affinities are discussed.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Reference13 articles.

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2. Bush K. F. Y. Liu and S. A. Smith. 1987. Interactions of monobactams with bacterial enzymes p. 153-164. In G. Pierce (ed.) Developments in industrial microbiology vol. 27. Society for Industrial Microbiology Arlington Va.

3. In vivo evaluation of tigemonam, a novel oral monobactam;Clark J. M.;Antimicrob. Agents Chemother.,1987

4. Penicillin-sensitive enzymes in peptidoglycan biosynthesis;Frere J.;Crit. Rev. Microbiol.,1985

5. Binding of monobactams to penicillin-binding proteins of Escherichia coli and Staphylococcus aureus: relation to antibacterial activity;Georgopapadakou N. H.;Antimicrob. Agents Chemother.,1983

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