Binding of Ceftobiprole and Comparators to the Penicillin-Binding Proteins of Escherichia coli , Pseudomonas aeruginosa , Staphylococcus aureus , and Streptococcus pneumoniae
- 1 July 2007
- journal article
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 51 (7), 2621-2624
- https://doi.org/10.1128/aac.00029-07
Abstract
Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus , PBP2x in penicillin-resistant Streptococcus pneumoniae , and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus , Escherichia coli , and Pseudomonas aeruginosa . Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.This publication has 27 references indexed in Scilit:
- Activities of Ceftobiprole and Other β-Lactams against Streptococcus pneumoniae Clinical Isolates from the United States with Defined Substitutions in Penicillin-Binding Proteins PBP 1a, PBP 2b, and PBP 2xAntimicrobial Agents and Chemotherapy, 2006
- Activities of Ceftobiprole, a Novel Broad-Spectrum Cephalosporin, against Haemophilus influenzae and Moraxella catarrhalisAntimicrobial Agents and Chemotherapy, 2006
- Antipneumococcal Activity of Ceftobiprole, a Novel Broad-Spectrum CephalosporinAntimicrobial Agents and Chemotherapy, 2005
- BAL9141, a Novel Extended-Spectrum Cephalosporin Active against Methicillin-Resistant Staphylococcus aureus in Treatment of Experimental EndocarditisAntimicrobial Agents and Chemotherapy, 2002
- In Vitro and In Vivo Properties of Ro 63-9141, a Novel Broad-Spectrum Cephalosporin with Activity against Methicillin-Resistant StaphylococciAntimicrobial Agents and Chemotherapy, 2001
- Synthesis and Structure−Activity Relationship of (Lactamylvinyl)cephalosporins Exhibiting Activity against Staphylococci, Pneumococci, and EnterococciJournal of Medicinal Chemistry, 1996
- Biochemical comparison of imipenem, meropenem and biapenem: permeability, binding to penicillin-binding proteins, and stability to hydrolysis by β-lactamasesJournal of Antimicrobial Chemotherapy, 1995
- Genetics of resistance to third‐generation cephalosporins in clinical isolates of Streptococcus pneumoniaeMolecular Microbiology, 1992
- Interaction of Non-lytic -Lactams with Penicillin-binding Proteins in Streptococcus pneumoniaeMicrobiology, 1987
- Mode of action of ceftazidime: affinity for the penicillin-binding proteins of Escherichia coli K12, Pseudomonas aeruginosa and Staphylococcus aureusJournal of Antimicrobial Chemotherapy, 1983