Structure, Function, and Biology of the Enterococcus faecalis Cytolysin

• Main Authors: Daria Van Tyne, Melissa J. Martin, Michael S. Gilmore
• Format: Article
• Language: English
• Published: MDPI AG 2013-04-01
• Series: Toxins
• Subjects: cytolysin; lantibiotic; bacteriocin
• Online Access: http://www.mdpi.com/2072-6651/5/5/895

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.