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Antimicrobial Agents and Chemotherapy, January 2001, p. 303-305, Vol. 45, No. 1
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.1.303-305.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Affinities of beta -Lactams for Penicillin Binding Proteins of Chlamydia trachomatis and Their Antichlamydial Activities

Christopher Storey and Ian Chopra*

Division of Microbiology and Antimicrobial Research Centre, University of Leeds, Leeds LS2 9JT, United Kingdom

Received 23 May 2000/Returned for modification 20 August 2000/Accepted 1 October 2000

Binding affinities of beta -lactam antibiotics for the three penicillin binding proteins (PBPs) from Chlamydia trachomatis were determined in vitro and compared with their antichlamydial activities. Mecillinam selectively inhibited PBP1, with a 50% inhibitory concentration for PBP1 binding (0.2 µg/ml) similar to the MIC (0.1 µg/ml) and minimum bactericidal concentration (0.25 µg/ml). Although the other beta -lactams inhibited a wider range of PBPs than mecillinam, their antichlamydial activities were inferior to that of mecillinam.

* Corresponding author. Mailing address: Division of Microbiology and Antimicrobial Research Centre, University of Leeds, Leeds LS2 9JT, United Kingdom. Phone: 44 113 233 5604. Fax: 44 113 233 5638. E-mail: i.chopra{at}leeds.ac.uk.

Antimicrobial Agents and Chemotherapy, January 2001, p. 303-305, Vol. 45, No. 1
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.1.303-305.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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