@article {1363214,
	title = {Structure, function, and biology of the Enterococcus faecalis cytolysin},
	journal = {Toxins (Basel)},
	volume = {5},
	number = {5},
	year = {2013},
	month = {2013 Apr 29},
	pages = {895-911},
	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 = {Animals, Bacteriocins, Cross Infection, Enterococcus faecalis, Gram-Positive Bacterial Infections, Humans, Molecular Structure},
	issn = {2072-6651},
	doi = {10.3390/toxins5050895},
	author = {Van Tyne, Daria and Martin, Melissa J and Gilmore, Michael S}
}
