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

Article Details

Citation

Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K

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. Epub 2007 Apr 30.

PubMed ID
17470659 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Drugs
Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
CeftobiproleMecAProteinStaphylococcus aureus
Yes
Inhibitor
Details
CeftobiprolePenicillin-binding protein 2BProteinStreptococcus pneumoniae (strain ATCC BAA-255 / R6)
Yes
Inhibitor
Details
CeftobiprolePenicillin-binding protein 2xProteinStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Yes
Inhibitor
Details
CeftobiprolePeptidoglycan synthase FtsIProteinEscherichia coli (strain K12)
Unknown
Not AvailableDetails