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Journal of Bacteriology, November 2005, p. 7434-7443, Vol. 187, No. 21
0021-9193/05/$08.00+0     doi:10.1128/JB.187.21.7434-7443.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

NspS, a Predicted Polyamine Sensor, Mediates Activation of Vibrio cholerae Biofilm Formation by Norspermidine

Ece Karatan, Tammi R. Duncan, and Paula I. Watnick*

Department of Geographic Medicine and Infectious Diseases, 750 Washington St., Box 041, Boston, Massachusetts 02111

Received 7 July 2005/ Accepted 24 August 2005

Vibrio cholerae is both an environmental bacterium and a human intestinal pathogen. The attachment of bacteria to surfaces in biofilms is thought to be an important feature of the survival of this bacterium both in the environment and within the human host. Biofilm formation occurs when cell-surface and cell-cell contacts are formed to make a three-dimensional structure characterized by pillars of bacteria interspersed with water channels. In monosaccharide-rich conditions, the formation of the V. cholerae biofilm requires synthesis of the VPS exopolysaccharide. MbaA (locus VC0703), an integral membrane protein containing a periplasmic domain as well as cytoplasmic GGDEF and EAL domains, has been previously identified as a repressor of V. cholerae biofilm formation. In this work, we have studied the role of the protein NspS (locus VC0704) in V. cholerae biofilm development. This protein is homologous to PotD, a periplasmic spermidine-binding protein of Escherichia coli. We show that the deletion of nspS decreases biofilm development and transcription of exopolysaccharide synthesis genes. Furthermore, we demonstrate that the polyamine norspermidine activates V. cholerae biofilm formation in an MbaA- and NspS-dependent manner. Based on these results, we propose that the interaction of the norspermidine-NspS complex with the periplasmic portion of MbaA diminishes the ability of MbaA to inhibit V. cholerae biofilm formation. Norspermidine has been detected in bacteria, archaea, plants, and bivalves. We suggest that norspermidine serves as an intercellular signaling molecule that mediates the attachment of V. cholerae to the biotic surfaces presented by one or more of these organisms.

* Corresponding author. Mailing address: Tufts-New England Medical Center, Department of Geographic Medicine and Infectious Diseases, 750 Washington St., Box 041, Boston, MA 02111. Phone: (617) 636-2545. Fax: (617) 636-3216. E-mail: pwatnick{at}tufts-nemc.org.

Journal of Bacteriology, November 2005, p. 7434-7443, Vol. 187, No. 21
0021-9193/05/$08.00+0     doi:10.1128/JB.187.21.7434-7443.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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