Competition of Beta-lactam Antibiotics for the Penicillin-binding Proteins of Neisseria Gonorrhoeae

Overview

Journal Antimicrob Agents Chemother

Publisher American Society for Microbiology

Specialty Pharmacology

Date 1981 Jul 1

PMID 6792979

Citations 16

Authors

T J Dougherty

A E Koller

A Tomasz

Affiliations

Soon will be listed here.

Abstract

The affinities of nine structurally different beta-lactam antibiotics for the three major gonococcal penicillin-binding proteins (PBPs) were determined by using a competition assay with tritium-labeled penicillin and live, growing bacteria. Each determination was carried out in parallel in isogenic pairs of penicillin-susceptible (minimal inhibitory concentration of penicillin, 0.0075 microgram/ml) and intrinsically penicillin-resistant (minimal inhibitory concentration of penicillin, 0.5 microgram/ml) cells. Evidence is presented indicating that (i) PBP 3 may be a dispensable function; (ii) acquisition of resistance is accompanied by change in the beta-lactam antibiotic affinities of PBP 2 but not of PBP 1; (iii) PBP 2 appears to be the most important physiological target in the penicillin-susceptible strain; in the penicillin-resistant strain, PBP 1 seems to assume this role. The relative affinities of various beta-lactam antibiotics for the individual PBPs showed substantial variation with the antibiotic structure.

Citing Articles

Differential contribution of PBP occupancy and efflux on the effectiveness of β-lactams at their target site in clinical isolates of Neisseria gonorrhoeae.

Lopez-Arguello S, Alcoceba E, Ordonez P, Taltavull B, Cabot G, Gomis-Font M PLoS Pathog. 2024; 20(12):e1012783.

PMID: 39739989 PMC: 11729944. DOI: 10.1371/journal.ppat.1012783.

Penicillin-Binding Protein Occupancy Dataset for 18 β-Lactams and 4 β-Lactamase Inhibitors in Neisseria gonorrhoeae.

Lopez-Arguello S, Montaner M, Marmol-Salvador A, Velazquez-Escudero A, Docobo-Perez F, Oliver A Microbiol Spectr. 2023; 11(3):e0069223.

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