Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae
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作者:
Davies, Todd A.
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机构:Johnson & Johnson Pharmaceut Res & Dev, LLC, Raritan, NJ 08869 USA
Davies, Todd A.
Page, Malcolm G. P.
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机构:Johnson & Johnson Pharmaceut Res & Dev, LLC, Raritan, NJ 08869 USA
Page, Malcolm G. P.
Shang, Wenchi
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机构:Johnson & Johnson Pharmaceut Res & Dev, LLC, Raritan, NJ 08869 USA
Shang, Wenchi
Andrew, Ted
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机构:Johnson & Johnson Pharmaceut Res & Dev, LLC, Raritan, NJ 08869 USA
Andrew, Ted
Kania, Malgosia
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机构:Johnson & Johnson Pharmaceut Res & Dev, LLC, Raritan, NJ 08869 USA
Kania, Malgosia
Bush, Karen
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机构:Johnson & Johnson Pharmaceut Res & Dev, LLC, Raritan, NJ 08869 USA
Bush, Karen
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[1] Johnson & Johnson Pharmaceut Res & Dev, LLC, Raritan, NJ 08869 USA
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.