Structural analysis and proteolytic activation of Enterococcus faecalis cytolysin, a novel lantibiotic

Authors: Booth, Mary C.1; Bogie, Charles P.2; Sahl, Hans-Georg3; Siezen, Roland J.4; Hatter, Kenneth L.1; Gilmore, Michael S.1

Source: Molecular Microbiology, Volume 21, Number 6, October 1996 , pp. 1175-1184(10)

Publisher: Blackwell Publishing

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Abstract:

Clinical isolates of Enterococcus faecalis more commonly produce a cytolysin than do commensal isolates. Epidemiologic evidence and animal-model studies have established a role for the cytolysin in the pathogenesis of enterococcal disease. The cytolysin consists of two structural subunits, CylLL and CylLS, that are activated by a third component, CylA. Genetic and biochemical characterization of CylA indicate that it is a serine protease, and that activation putatively results from cleavage of one or both cytolysin subunits. Genetic evidence also suggests that the cytolysin subunits are related to the rapidly growing class of bacteriocins termed lantibiotics. However, unlike lantibiotics, the cytolysin is lytic for eukaryotic as well as prokaryotic cells, and it consists of two structural subunits. This report describes the purification and characterization of the cytolysin subunits and detection of lanthionine-type post-translational modifications within their structures. Furthermore, the cleavage specificity of the CylA activator is reported and it is shown that proteolytic activation of both subunits is essential for activity.

Document Type: Research article

DOI: 10.1046/j.1365-2958.1996.831449.x

Affiliations: 1: Department of Ophthalmology and Dean A. McGee Eye Institute, Molecular Pathogenesis of Eye Infection Research (MPEIR) Center, 608 S. L. Young Boulevard, Oklahoma City, Oklahoma 73104, USA. 2: Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, PO Box 26901, Oklahoma City, Oklahoma 73190, USA. 3: Institut fur Medizinische Mikrobiologie und Immunologie, Universitat Bonn, D-53105 Bonn, Germany. 4: Department of Biophysical Chemistry, NIZO, PO Box 20, 6710BA Ede, The Netherlands.

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