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