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Staphylococcus intermedius Produces a Functional agr Autoinducing Peptide Containing a Cyclic Lactone

Guangyong Ji,^1* Wuhong Pei,¹ Linsheng Zhang,^1, Rongde Qiu,¹ Jianqun Lin,¹ Yvonne Benito,² Gerard Lina,² and Richard P. Novick^3*

Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Rd., Bethesda, Maryland 20814,¹ Centre National de Référence des Staphylocoques, INSERM E0230, IFR62 Laennec, 7 rue Guillaume Paradin, 69372 Lyon Cedex 08, France,² Molecular Pathogenesis Program, Skirball Institute of Biomolecular Medicine, New York University Medical Center, 540 First Ave., New York, New York 10016³

Received 31 July 2004/ Accepted 19 January 2005

The agr system is a global regulator of accessory functions in staphylococci, including genes encoding exoproteins involved in virulence. The agr locus contains a two-component signal transduction module that is activated by an autoinducing peptide (AIP) encoded within the agr locus and is conserved throughout the genus. The AIP has an unusual partially cyclic structure that is essential for function and that, in all but one case, involves an internal thiolactone bond between a conserved cysteine and the C-terminal carboxyl group. The exceptional case is a strain of Staphylococcus intermedius that has a serine in place of the conserved cysteine. We demonstrate here that the S. intermedius AIP is processed by the S. intermedius AgrB protein to generate a cyclic lactone, that it is an autoinducer as well as a cross-inhibitor, and that all of five other S. intermedius strains examined also produce serine-containing AIPs.

Present address: Division of Pediatric Oncology, The Johns Hopkins University, 1650 Orleans St., Baltimore, MD 21231.

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