Enterococcus faecalis plasmid pAD1-encoded Fst toxin affects membrane permeability and alters cellular responses to lantibiotics

Keith E. Weaver, Dariel M. Weaver, Carol L. Wells, Christopher M. Waters, Marshall E. Gardner, Erik A. Ehli

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2169-2177
Number of pages9
JournalJournal of bacteriology
Volume185
Issue number7
DOIs
StatePublished - Apr 2003

Fingerprint Dive into the research topics of 'Enterococcus faecalis plasmid pAD1-encoded Fst toxin affects membrane permeability and alters cellular responses to lantibiotics'. Together they form a unique fingerprint.

Cite this