Contribution of a TEM-1-Like Beta-Lactamase to Penicillin Resistance in Neisseria gonorrhoeae
AUTOR(ES)
Bergström, Sven
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=352298Documentos Relacionados
- Plasmid-Mediated Beta-Lactamase Production in Neisseria gonorrhoeae
- Transfer of Plasmid-Borne Beta-Lactamase in Neisseria gonorrhoeae
- Emergence of clinical isolates of Escherichia coli producing TEM-1 derivatives or an OXA-1 beta-lactamase conferring resistance to beta-lactamase inhibitors.
- Transfer of beta-lactamase plasmids by conjugation in Neisseria gonorrhoeae.
- Transfer of Beta-Lactamase Genes of Neisseria gonorrhoeae by Conjugation
