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

被引：141

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

来源：

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY | 2007年 / 51卷 / 07期

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.

引用

收藏

页码：2621 / 2624

页数：4

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