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. 1978 Apr;13(4):618–623. doi: 10.1128/aac.13.4.618

Contribution of a TEM-1-Like Beta-Lactamase to Penicillin Resistance in Neisseria gonorrhoeae

Sven Bergström 1, Lena Norlander 1, Anders Norqvist 1, Staffan Normark 1
PMCID: PMC352298  PMID: 96728

Abstract

Two β-lactamase-producing strains of Neisseria gonorrhoeae were studied. The substrate profile, molecular weight, and isoelectric point of their β-lactamases were similar to those of the TEM-1 enzyme produced by many gram-negative bacilli. The gonococcal β-lactamase was cell bound during exponential growth and was most likely located in the periplasm. Penicillin hydrolysis was efficient in intact cells, suggesting that the cell-bound β-lactamase was freely accessible to benzylpenicillin. Both β-lactamase-producing strains of N. gonorrhoeae contained an additional multicopy plasmid with a mass of 3.3 megadaltons (Mdal). A spontaneous penicillin-susceptible revertant lacked both β-lactamase activity and the 3.3-Mdal plasmid, providing evidence for plasmid-mediated penicillin resistance. During a shift from GC medium to rich MOPS medium, growth of the penicillin-susceptible revertant in contrast to that of the plasmid-carrying strain was markedly impaired, suggesting a physiological effect due to the presence of the 3.3-Mdal plasmid.

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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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