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Enterococcal Leucine-Rich Repeat-Containing Protein Involved in Virulence and Host Inflammatory Response

Unité des Bactéries Lactiques et Pathogènes Opportunistes UR13888, INRA, Jouy-en-Josas, France,¹ Institute of Microbiology, Catholic University of Sacred Heart, Roma, Italy,² Unité des Interactions Bactéries-Cellules, Institut Pasteur, INSERM U604, INRA USC2020, Paris, France³

Received 20 February 2007/ Returned for modification 19 April 2007/ Accepted 29 June 2007

Enterococcus faecalis is an important nosocomial pathogen associated with high morbidity and mortality for patients who are immunocompromised or who have severe underlying diseases. The E. faecalis genome encodes numerous surface-exposed proteins that may be involved in virulence. This work describes the characterization of the first internalin-like protein in E. faecalis, ElrA, belonging to the recently identified WxL family of surface proteins. ElrA contains an N-terminal signal peptide for export, a leucine-rich repeat domain that may interact with host cells, and a C-terminal WxL domain that interacts with the peptidoglycan. Disruption of the elrA gene significantly attenuates bacterial virulence in a mouse peritonitis model. The elrA deletion mutant also displays a defect in infection of host macrophages and a decreased interleukin-6 response in vivo. Finally, elrA expression is induced in vivo. Altogether, these results demonstrate a role for ElrA in the E. faecalis infectious process in vivo and suggest that this surface protein may contribute to E. faecalis virulence by stimulating the host inflammatory response.

Published ahead of print on 9 July 2007.

Editor: V. J. DiRita

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