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Chemotherapy. 1995 May-Jun;41(3):159-64.

Interaction of beta-lactam antibiotics with the penicillin-binding proteins of penicillin-resistant Streptococcus pneumoniae.

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Department of Chemotherapy, Fujisawa Pharmaceutical Co., Osaka, Japan.


The binding of five structurally diverse beta-lactam antibiotics to penicillin-binding proteins (PBPs) of two clinical isolates of Streptococcus pneumoniae resistant to penicillin G was compared with that of a susceptible strain. A common feature of the PBP patterns of the resistant strains was the absence of PBP 1a detected in the susceptible strain. For each beta-lactam antibiotic tested, there appeared to be significant decreases in the affinity for BPB 1b, 2a and 2b of the resistant strains. We attempted to evaluate a quantitative correlation between the antibacterial activity of the drugs for three strains and their affinity for the various PBPs. A close correlation was found between the minimum inhibitory concentrations and the affinity for PBP 2a, but not for any of the other PBPs.

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