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Journal of Bacteriology, September 2000, p. 4926-4933, Vol. 182, No. 17
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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

B. A. (Leonard) Buttaro,dagger M. H. Antiporta, and G. M. Dunny*

Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455

Received 28 December 1999/Accepted 8 June 2000

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.

* Corresponding author. Mailing address: Department of Microbiology, University of Minnesota Medical School, 1420 Delaware St. SE, Minneapolis, MN 55455. Phone: (612) 625-9930. Fax: (612) 626-0623. E-mail: gary-d{at}biosci.cbs.umn.edu.

dagger Present address: Department of Microbiology and Immunology, Temple University School of Medicine, Philadelphia, PA 19140.

Journal of Bacteriology, September 2000, p. 4926-4933, Vol. 182, No. 17
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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