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. 1986 Nov;30(5):659–663. doi: 10.1128/aac.30.5.659

Modulation of bacteriolysis by cooperative effects of penicillin-binding proteins 1a and 3 in Escherichia coli.

E Tuomanen, K Gilbert, A Tomasz
PMCID: PMC176509  PMID: 3541782

Abstract

Escherichia coli characteristically lyses upon treatment with most beta-lactam antimicrobial agents. In contrast, an investigational aminothiazole cephem, CGP 31523A, produced a new combination of antibacterial effects: it was highly bactericidal without causing cell wall degradation or lysis. Killing was associated with the formation of vacuolated filaments. Because the compound bound to penicillin-binding proteins (PBPs) 1a and 3, we investigated the role of PBP 3 in modulation of lysis caused by inhibition of PBP 1a. A temperature-sensitive mutant with a nonfunctional PBP 3 lysed when treated with CGP 31523A. The combination of a PBP 1 inhibitor (cefsulodin) and a PBP 3 inhibitor (aztreonam) also caused filamentation and death without lysis of wild-type cells over a narrow concentration range. We conclude that cooperative effects between PBPs in E. coli can lead to a dissociation of bacterial killing and lysis.

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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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