Relative penicillin G resistance in Neisseria meningitidis and reduced affinity of penicillin-binding protein 3.
We examined clinical isolates of Neisseria meningitidis relatively resistant to penicillin G (mean MIC, 0.3 micrograms/ml; range, 0.1 to 0.7 micrograms/ml), which were isolated from blood and cerebrospinal fluid for resistance mechanisms, by using susceptible isolates (mean MIC, less than or equal to 0.06 micrograms/ml) for comparison. The resistant strains did not produce detectable beta-lactamase activity, otherwise modify penicillin G, or bind less total penicillin. Penicillin-binding protein (PBP) 3 of the six resistant isolates tested uniformly bound less penicillin G in comparison to the same PBP of four susceptible isolates. Reflecting the reduced binding affinity of PBP 3 of the two resistant strains tested, the amount of 3H-labeled penicillin G required for half-maximal binding was increased in comparison with that of PBP 3 of the two susceptible isolates. We conclude that the mechanism of resistance in these meningococci relatively resistant to penicillin G was decreased affinity of PBP 3.
D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000378:metabolism*; D002855:Chromatography, Thin Layer; D006602:Hexosyltransferases; D006801:Humans; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism*; D009345:Neisseria meningitidis / Q000187:drug effects* / Q000201:enzymology / Q000378:metabolism; D010400:Penicillin G / Q000494:pharmacology*; D010403:Penicillin Resistance; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D001618:beta-Lactamases / Q000378:metabolism
D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D001618:beta-Lactamases; D010400:Penicillin G