Chemotherapy

Microbiology

Interaction of Beta-Lactam Antibiotics with the Penicillin-Binding Proteins of Penicillin-Resistant Streptococcus pneumoniae

Ikeda F.a · Yokota Y.a · Ikemoto A.a · Teratani N.a · Shimomura K.a · Kanno H.b

Author affiliations

aDepartment of Chemotherapy, Pharmacological Research Laboratories, Fujisawa Pharmaceutical Co., Osaka, and bDepartment of Laboratory Medicine, Chiba University Hospital, Chiba, Japan

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Chemotherapy 1995;41:159–164

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Article / Publication Details

First-Page Preview
Abstract of Microbiology

Published online: September 11, 2009
Issue release date: 1995

Number of Print Pages: 6
Number of Figures: 0
Number of Tables: 0

ISSN: 0009-3157 (Print)
eISSN: 1421-9794 (Online)

For additional information: https://www.karger.com/CHE

Abstract

The binding of five structurally diverse β-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 la detected in the susceptible strain. For each β-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.

© 1995 S. Karger AG, Basel




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Article / Publication Details

First-Page Preview
Abstract of Microbiology

Published online: September 11, 2009
Issue release date: 1995

Number of Print Pages: 6
Number of Figures: 0
Number of Tables: 0

ISSN: 0009-3157 (Print)
eISSN: 1421-9794 (Online)

For additional information: https://www.karger.com/CHE


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