Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
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.
Davies
Todd A
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Johnson & Johnson Pharmaceutical Research and Development, LLC, Room B225, 1000 Route 202, Raritan, NJ 08869, USA. tdavies@prdus.jnj.com
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D001426:Bacterial Proteins / Q000378:metabolism*; D002511:Cephalosporins / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D006090:Gram-Negative Bacteria / Q000378:metabolism*; D020128:Inhibitory Concentration 50; D008826:Microbial Sensitivity Tests; D046915:Penicillin-Binding Proteins / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000737:chemistry / Q000378:metabolism; D013211:Staphylococcus aureus / Q000737:chemistry / Q000378:metabolism; D013296:Streptococcus pneumoniae / Q000737:chemistry / Q000378:metabolism
D001426:Bacterial Proteins; D002511:Cephalosporins; D029968:Escherichia coli Proteins; D046915:Penicillin-Binding Proteins; C443755:ceftobiprole