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. 2006 Jul;50(7):2530-2.
doi: 10.1128/AAC.00238-06.

Activities of ceftobiprole and other beta-lactams against Streptococcus pneumoniae clinical isolates from the United States with defined substitutions in penicillin-binding proteins PBP 1a, PBP 2b, and PBP 2x

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Activities of ceftobiprole and other beta-lactams against Streptococcus pneumoniae clinical isolates from the United States with defined substitutions in penicillin-binding proteins PBP 1a, PBP 2b, and PBP 2x

Todd A Davies et al. Antimicrob Agents Chemother. 2006 Jul.

Abstract

The activities of ceftobiprole and other beta-lactams were examined with 30 Streptococcus pneumoniae isolates containing multiple pbp1a, pbp2b, and pbp2x mutations. The highest ceftobiprole MIC was 1 microg/ml, while the comparator MICs were 16 to 64 microg/ml. Fifty percent inhibitory concentrations for penicillin-binding protein 2x were 0.5 microg/ml (ceftobiprole) and 4 microg/ml (ceftriaxone) in a penicillin- and ceftriaxone-resistant isolate.

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FIG. 1.
FIG. 1.
Binding of ceftobiprole and ceftriaxone to PBPs 2x, 2a, and 2b from S. pneumoniae isolate 8819 (penicillin resistant, ceftriaxone resistant).

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