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

被引:136
作者
Davies, Todd A.
Page, Malcolm G. P.
Shang, Wenchi
Andrew, Ted
Kania, Malgosia
Bush, Karen
机构
[1] Johnson & Johnson Pharmaceut Res & Dev, LLC, Raritan, NJ 08869 USA
[2] Basilea Pharmaceut AG, CH-4005 Basel, Switzerland
关键词
D O I
10.1128/AAC.00029-07
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
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页码:2621 / 2624
页数:4
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