Properties of penicillin-binding proteins in Neisseria gonorrhoeae.
The properties of penicillin-binding proteins (PBPs) of Neisseria gonorrhoeae were studied by comparing PBPs of clinical isolates of different penicillin susceptibility and by putting various beta-lactam antibiotics in competition with radioactive penicillin for PBP binding. Apparent molecular weights of the three major PBPs found were 87,000 (PBP 1), 59,000 (PBP 2), and 44,000 (PBP 3). Relative penicillin resistance was associated with decreased binding to PBP 2 and, to a lesser extent, to PBP 1. Cephaloridine and benzylpenicillin, which produced spheroplasts at minimal inhibitory concentrations, bound to all three PBPs. In contrast, antibiotics which produced a majority of enlarged but apparently intact cells bound only to PBP 2 (mecillinam) or to PBPs 2 and 3 (cephalexin) at their minimal inhibitory concentrations.
D000900:Anti-Bacterial Agents / Q000378:metabolism / Q000494:pharmacology; D001426:Bacterial Proteins / Q000378:metabolism*; D001667:Binding, Competitive; D002352:Carrier Proteins / Q000378:metabolism*; D006602:Hexosyltransferases; D007769:Lactams / Q000378:metabolism; D008826:Microbial Sensitivity Tests; D002267:Muramoylpentapeptide Carboxypeptidase; D009344:Neisseria gonorrhoeae / Q000187:drug effects / Q000378:metabolism*; D010403:Penicillin Resistance; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000378:metabolism; D010458:Peptidyl Transferases
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D002352:Carrier Proteins; D007769:Lactams; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase