{"id":102,"date":"2015-11-09T20:17:28","date_gmt":"2015-11-09T20:17:28","guid":{"rendered":"https:\/\/lab.research.sickkids.ca\/howell\/?page_id=102"},"modified":"2018-04-19T09:43:22","modified_gmt":"2018-04-19T14:43:22","slug":"pel","status":"publish","type":"page","link":"https:\/\/lab.research.sickkids.ca\/howell\/molecular-mechanisms\/exopolysaccharides\/pel\/","title":{"rendered":"Pel"},"content":{"rendered":"
\"Model<\/a><\/span><\/div>
<\/div>
<\/div>
<\/div>

Model of Pel\u00a0biosynthetic machinery<\/p>\n<\/div>

<\/div><\/div><\/div>

In addition to mucoid P. aeruginosa <\/em>strains, strains with a wrinkly small colony morphology and increased biofilm forming capacity have been isolated from CF sputum. These strains have increased expression of the Psl and Pel polysaccharides, and suggest that all three exopolysaccharides, alginate, Psl and Pel, play important roles in the colonization and maintenance of CF lung infections. Pel and Psl are the predominant polysaccharides found in biofilm infections in other clinical and all environmental settings, where together or individually they act as adhesins to maintain biofilm structure. Pel is a cationic polymer composed of 1,4 linked N-<\/em>acetylglucosamine and N-<\/em>acetylgalactosamine. Pel has been shown to initiate and maintain cell-to-cell interactions, and provide resistance to aminoglycoside antibiotics.<\/p>\n

At present, our understanding of the molecular processes used by the seven proteins encoded on the pelABCDEFG <\/em>operon to produce Pel is relatively limited. Our studies have shown that PelA is a multi-domain protein with both de-N<\/em>-acetylase and hydrolase activities, and that while Pel polymerization, like alginate, is regulated by c-di-GMP, the inner membrane protein PelD uses a degenerate GGDEF domain rather than a PilZ domain (left).<\/p>\n<\/div>

Current projects<\/h2>\n

Our current projects are focused on:<\/p>\n