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  • Title: Interaction of beta-lactam antibiotics with the penicillin-binding proteins of penicillin-resistant Streptococcus pneumoniae.
    Author: Ikeda F, Yokota Y, Ikemoto A, Teratani N, Shimomura K, Kanno H.
    Journal: Chemotherapy; 1995; 41(3):159-64. PubMed ID: 7656660.
    Abstract:
    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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