Wild-type penicillin-binding protein (PBP) 2b from penicillin-susceptible
Streptococcus pneumoniae had high affinity for ceftobiprole
and penicillin (50% inhibitory concentrations [IC
50s] of

0.15
µg/ml) but not ceftriaxone (IC
50 of >8 µg/ml).
In clinical isolates, ceftobiprole and PBP 2b affinities were
reduced 15- to 30-fold with a Thr-446-Ala substitution and further
still with an additional Ala-619-Gly PBP 2b substitution. Ceftobiprole
remained active (MICs of
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1 µg/ml) against all strains
tested and behaved more like penicillin than ceftriaxone with
respect to PBP 2b binding.
Antimicrobial Agents and Chemotherapy, October 2010, p. 4510-4512, Vol. 54, No. 10
0066-4804/10/$12.00+0 doi:10.1128/AAC.00590-10
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