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Journal of Bacteriology, April 2003, p. 2169-2177, Vol. 185, No. 7
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.7.2169-2177.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Enterococcus faecalis Plasmid pAD1-Encoded Fst Toxin Affects Membrane Permeability and Alters Cellular Responses to Lantibiotics

Division of Basic Biomedical Sciences, School of Medicine, University of South Dakota, Vermillion, South Dakota 57069,¹ Departments of Laboratory Medicine & Pathology and Surgery, University of Minnesota, Minneapolis, Minnesota 55455-0374,² Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455³

Received 18 September 2002/ Accepted 29 December 2002

Fst is a peptide toxin encoded by the par toxin-antitoxin stability determinant of Enterococcus faecalis plasmid pAD1. Intracellular overproduction of Fst resulted in simultaneous inhibition of all cellular macromolecular synthesis concomitant with cell growth inhibition and compromised the integrity of the cell membrane. Cells did not lyse or noticeably leak intracellular contents but had specific defects in chromosome partitioning and cell division. Extracellular addition of synthetic Fst had no effect on cell growth. Spontaneous Fst-resistant mutants had a phenotype consistent with changes in membrane composition. Interestingly, overproduction of Fst sensitized cells to the lantibiotic nisin, and Fst-resistant mutants were cross-resistant to nisin and the pAD1-encoded cytolysin.

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