Structure, Function, and Biology of the Enterococcus faecalis Cytolysin
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CitationVan Tyne, Daria, Melissa J. Martin, and Michael S. Gilmore. 2013. “Structure, Function, and Biology of the Enterococcus faecalis Cytolysin.” Toxins 5 (5): 895-911. doi:10.3390/toxins5050895. http://dx.doi.org/10.3390/toxins5050895.
AbstractEnterococcus 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.
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