Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae

Todd A Davies; Malcolm G P Page; Wenchi Shang; Ted Andrew; Malgosia Kania; Karen Bush

doi:10.1128/AAC.00029-07

Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae

Antimicrob Agents Chemother. 2007 Jul;51(7):2621-4. doi: 10.1128/AAC.00029-07. Epub 2007 Apr 30.

Authors

Todd A Davies¹, Malcolm G P Page, Wenchi Shang, Ted Andrew, Malgosia Kania, Karen Bush

Affiliation

¹ Johnson & Johnson Pharmaceutical Research and Development, LLC, Room B225, 1000 Route 202, Raritan, NJ 08869, USA. [email protected]

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / metabolism*
Cephalosporins / metabolism*
Escherichia coli Proteins / metabolism*
Gram-Negative Bacteria / metabolism*
Inhibitory Concentration 50
Microbial Sensitivity Tests
Penicillin-Binding Proteins / metabolism*
Pseudomonas aeruginosa / chemistry
Pseudomonas aeruginosa / metabolism
Staphylococcus aureus / chemistry
Staphylococcus aureus / metabolism
Streptococcus pneumoniae / chemistry
Streptococcus pneumoniae / metabolism

Substances

Bacterial Proteins
Cephalosporins
Escherichia coli Proteins
Penicillin-Binding Proteins
ceftobiprole