This Article Full Text Full Text (PDF) Other Versions of this Article: JB.00773-06v1 189/4/1244    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Brinster, S. Articles by Serror, P. Search for Related Content PubMed PubMed Citation Articles by Brinster, S. Articles by Serror, P.

 Previous Article  |  Next Article 

Journal of Bacteriology, February 2007, p. 1244-1253, Vol. 189, No. 4
0021-9193/07/$08.00+0     doi:10.1128/JB.00773-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

C-Terminal WxL Domain Mediates Cell Wall Binding in Enterococcus faecalis and Other Gram-Positive Bacteria

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

Received 29 May 2006/ Accepted 30 August 2006

Analysis of the genome sequence of Enterococcus faecalis clinical isolate V583 revealed novel genes encoding surface proteins. Twenty-seven of these 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 designated WxL. Proteins having similar characteristics were also detected in other low-G+C-content gram-positive bacteria. We hypothesized that the WxL region might be a determinant of bacterial cell location. This hypothesis 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 conferred a cell surface localization to the reporter fusions in E. faecalis. This localization was eliminated by introducing specific deletions into the domains. Interestingly, exogenously added protein fusions displayed binding to whole cells of various gram-positive bacteria. We also showed that the peptidoglycan was 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 the WxL region is a novel cell wall binding domain in E. faecalis and other gram-positive bacteria.

Published ahead of print on 8 September 2006.

This article has been cited by other articles:

• Brinster, S., Posteraro, B., Bierne, H., Alberti, A., Makhzami, S., Sanguinetti, M., Serror, P. (2007). Enterococcal Leucine-Rich Repeat-Containing Protein Involved in Virulence and Host Inflammatory Response. Infect. Immun. 75: 4463-4471 [Abstract] [Full Text]  
• Bierne, H., Cossart, P. (2007). Listeria monocytogenes Surface Proteins: from Genome Predictions to Function. Microbiol. Mol. Biol. Rev. 71: 377-397 [Abstract] [Full Text]