Affinity of Doripenem and Comparators to Penicillin-Binding Proteins in Escherichia coli and Pseudomonas aeruginosa
- 1 April 2008
- journal article
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 52 (4), 1510-1512
- https://doi.org/10.1128/aac.01529-07
Abstract
Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli , the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.Keywords
This publication has 12 references indexed in Scilit:
- Comparative in vitro antimicrobial activity of a new carbapenem, doripenem: tentative disc diffusion criteria and quality controlJournal of Antimicrobial Chemotherapy, 2005
- Activities of Doripenem (S-4661) against Drug-Resistant Clinical PathogensAntimicrobial Agents and Chemotherapy, 2004
- In Vitro Antimicrobial Activity of Doripenem, a New CarbapenemAntimicrobial Agents and Chemotherapy, 2004
- Recent developments in carbapenemsExpert Opinion on Investigational Drugs, 2002
- BOCILLIN FL, a Sensitive and Commercially Available Reagent for Detection of Penicillin-Binding ProteinsAntimicrobial Agents and Chemotherapy, 1999
- Potent activity of meropenem against Escherichia coli arising from its simultaneous binding to penicillin-binding proteins 2 and 3Journal of Antimicrobial Chemotherapy, 1995
- Penicillin-binding proteins and bacterial resistance to beta-lactamsAntimicrobial Agents and Chemotherapy, 1993
- Mode of action of ceftazidime: affinity for the penicillin-binding proteins of Escherichia coli K12, Pseudomonas aeruginosa and Staphylococcus aureusJournal of Antimicrobial Chemotherapy, 1983
- Binding of monobactams to penicillin-binding proteins of Escherichia coli and Staphylococcus aureus: relation to antibacterial activityAntimicrobial Agents and Chemotherapy, 1983
- Competition of beta-lactam antibiotics for the penicillin-binding proteins of Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella aerogenes, Proteus rettgeri, and Escherichia coli: comparison with antibacterial activity and effects upon bacterial morphologyAntimicrobial Agents and Chemotherapy, 1979