title: Affinities of beta-lactams for penicillin binding proteins of Chlamydia trachomatis and their antichlamydial activities.
abstract: 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 microg/ml) similar to the MIC (0.1 microg/ml) and minimum bactericidal concentration (0.25 microg/ml). Although the other beta-lactams inhibited a wider range of PBPs than mecillinam, their antichlamydial activities were inferior to that of mecillinam.
authors: Division of Microbiology and Antimicrobial Research Centre, University of Leeds, Leeds LS2 9JT, United Kingdom.
authors: C
authors: C
authors: Storey
authors: I
authors: I
authors: Chopra
mesh_terms: D000560:Amdinocillin / Q000494:pharmacology; D000900:Anti-Bacterial Agents / Q000378:metabolism* / Q000494:pharmacology*; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000378:metabolism*; D002692:Chlamydia trachomatis / Q000187:drug effects* / Q000378:metabolism*; D006602:Hexosyltransferases; D008826:Microbial Sensitivity Tests; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism*; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D011485:Protein Binding
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D000560:Amdinocillin