Toxins 2013, 5(5), 895-911; doi:10.3390/toxins5050895

Structure, Function, and Biology of the Enterococcus faecalis Cytolysin

Department of Ophthalmology and Department of Microbiology and Immunobiology, Harvard Medical School, Massachusetts Eye and Ear Infirmary, 243 Charles St., Boston, MA 02114, USA
* Author to whom correspondence should be addressed.
Received: 25 March 2013; in revised form: 22 April 2013 / Accepted: 23 April 2013 / Published: 29 April 2013
(This article belongs to the Special Issue Pore-Forming Toxins)
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Abstract: Enterococcus faecalis is a Gram-positive commensal member of the gut microbiota of a wide range of organisms. With the advent of antibiotic therapy, it has emerged as a multidrug resistant, hospital-acquired pathogen. Highly virulent strains of E. faecalis express a pore-forming exotoxin, called cytolysin, which lyses both bacterial and eukaryotic cells in response to quorum signals. Originally described in the 1930s, the cytolysin is a member of a large class of lanthionine-containing bacteriocins produced by Gram-positive bacteria. While the cytolysin shares some core features with other lantibiotics, it possesses unique characteristics as well. The current understanding of cytolysin biosynthesis, structure/function relationships, and contribution to the biology of E. faecalis are reviewed, and opportunities for using emerging technologies to advance this understanding are discussed.
Keywords: cytolysin; lantibiotic; bacteriocin

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MDPI and ACS Style

Van Tyne, D.; Martin, M.J.; Gilmore, M.S. Structure, Function, and Biology of the Enterococcus faecalis Cytolysin. Toxins 2013, 5, 895-911.

AMA Style

Van Tyne D, Martin MJ, Gilmore MS. Structure, Function, and Biology of the Enterococcus faecalis Cytolysin. Toxins. 2013; 5(5):895-911.

Chicago/Turabian Style

Van Tyne, Daria; Martin, Melissa J.; Gilmore, Michael S. 2013. "Structure, Function, and Biology of the Enterococcus faecalis Cytolysin." Toxins 5, no. 5: 895-911.

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