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. 1988 May;32(5):706–709. doi: 10.1128/aac.32.5.706

Relative penicillin G resistance in Neisseria meningitidis and reduced affinity of penicillin-binding protein 3.

P M Mendelman 1, J Campos 1, D O Chaffin 1, D A Serfass 1, A L Smith 1, J A Sáez-Nieto 1
PMCID: PMC172256  PMID: 3134848

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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