Cell-Associated Pheromone Peptide (cCF10) Production and Pheromone Inhibition in Enterococcus faecalis

• DOI: 10.1128/jb.182.17.4926-4933.2000
• Publication Date: 2002-07-27T10:00:58Z
• Authors: B. A. (Leonard) B...; M. H. Antiporta; G. M. Dunny
• Keywords: 0301 basic medicine; Membrane Proteins; Protein Sorting Signals; Pheromones; Culture Media; 03 medical and health sciences; Bacterial Proteins; Cell Wall; Mutagenesis; Enterococcus faecalis; Protein Precursors; Oligopeptides

ABSTRACT

In Enterococcus faecalis , the peptide cCF10 acts as a pheromone, inducing transfer of the conjugative plasmid pCF10 from plasmid-containing donor cells to plasmid-free recipient cells. In these studies, it was found that a substantial amount of cCF10 associates with the envelope of the producing cell. Pheromone activity was detected in both wall and membrane fractions, with the highest activity associated with the wall. Experiments examining the effects of protease inhibitor treatments either prior to or following cell fractionation suggested the presence of a cell envelope-associated pro-cCF10 that can be processed to mature cCF10 by a maturase or protease. A pCF10-encoded membrane protein, PrgY, was shown to prevent self-induction of donor cells by reducing the level of pheromone activity in the cell wall fraction.