JB Accepts, published online ahead of print on 2 November 2007

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J. Bacteriol. doi:10.1128/JB.01410-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

A novel role for Enzyme I of the Vibrio cholerae phosphoenol-pyruvate phosphotransferase system in regulation of growth in a biofilm

Laetitia Houot and Paula I. Watnick^*

^* To whom correspondence should be addressed. Email: paula.watnick{at}childrens.harvard.edu.

Glucose is a universal energy source and a potent inducer of surface colonization for many microbial species. Highly efficient sugar assimilation pathways ensure successful competition for this preferred carbon source. One such pathway is the phosphoenol-pyruvate phosphotransferase system, a multi-component sugar transport system that phosphorylates the sugar as it enters the cell. Components required for transport of glucose through the PTS include Enzyme I, Histidine protein, Enzyme IIA^Glc, and Enzyme IIBC^Glc. In Escherichia coli, components of the PTS fulfill many regulatory roles including regulation of nutrient scavenging and catabolism, chemotaxis, glycogen utilization, catabolite repression, and inducer exclusion. We previously observed that genes encoding the components of the V. cholerae PTS were co-regulated with the vps genes, which are required for synthesis of the biofilm matrix exopolysaccharide. In this work, we identify the PTS components required for transport of glucose and investigate the role of each of these components in regulation of biofilm formation. Our results establish a novel role for the phosphorylated form of Enzyme I in specific regulation of biofilm-associated growth. As the PTS is highly conserved among bacteria, the Enzyme I regulatory pathway may be relevant to a number of biofilm-based infections.

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