JB Accepts, published online ahead of print on 8 September 2006

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J. Bacteriol. doi:10.1128/JB.00773-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

C-terminal WxL domain mediates cell-wall binding in Enterococcus faecalis and other Gram-positive bacteria

Sophie Brinster, Sylviane Furlan, and Pascale Serror^*

Unité des Bactéries Lactiques et Pathogènes Opportunistes, INRA, Jouy-en-Josas, France

^* To whom correspondence should be addressed. Email: pascale.serror{at}jouy.inra.fr.

Analysis of the genome sequence of Enterococcus faecalis clinical isolate V583 revealed novel genes encoding surface proteins. Among them, twenty seven proteins, annotated as having unknown functions, possess a putative N-terminal signal peptide and a conserved C-terminal region characterized by a novel conserved domain, named WxL. Proteins having similar characteristics were also detected in other low GC Gram positive bacteria. We hypothesized that the role of the WxL region might be a determinant of bacterial cell location. This was tested by generating protein fusions between the C-terminal regions of two WxL proteins in E. faecalis, and a nuclease reporter protein. We demonstrated that the C-terminal regions of both proteins confer a cell surface localization to the reporter fusions in E. faecalis. This localization was abolished by introducing specific deletions in the domains. Interestingly, exogenously added protein fusions displayed binding to whole cells of various Gram positive bacteria. We further showed that the peptidoglycan is a binding ligand for WxL domain attachment to the cell surface, and that neither proteins nor carbohydrates were necessary for binding. Based on our findings, we propose that WxL region constitutes a novel cell-wall binding domain in E. faecalis and other Gram-positive bacteria.

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