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

Structure, Function, and Biology of the Enterococcus faecalis Cytolysin

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Received: 25 March 2013 / Revised: 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 cytolysin; lantibiotic; bacteriocin
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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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