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Antimicrobial Agents and Chemotherapy, July 2007, p. 2621-2624, Vol. 51, No. 7
0066-4804/07/$08.00+0 doi:10.1128/AAC.00029-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
Binding of Ceftobiprole and Comparators to the Penicillin-Binding Proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae
Todd A. Davies,1*
Malcolm G. P. Page,2
Wenchi Shang,1
Ted Andrew,1
Malgosia Kania,2 and
Karen Bush1
Johnson & Johnson Pharmaceutical Research and Development, LLC, Raritan, New Jersey,1
Basilea Pharmaceutica AG, Grenzacherstrasse 487, P.O. Box CH-4005, Basel, Switzerland2
Received 10 January 2007/
Returned for modification 15 February 2007/
Accepted 19 April 2007
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.
* Corresponding author. Mailing address: Johnson & Johnson Pharmaceutical Research and Development, LLC, Room B225, 1000 Route 202, Raritan, NJ 08869. Phone: (908) 707-3465. Fax: (908) 707-3501. E-mail: tdavies{at}prdus.jnj.com
Published ahead of print on 30 April 2007.
Antimicrobial Agents and Chemotherapy, July 2007, p. 2621-2624, Vol. 51, No. 7
0066-4804/07/$08.00+0 doi:10.1128/AAC.00029-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
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