When introduced to harsh conditions such as low pH, <i>E. coli </i>can secrete colanic acid, an exopolysaccharide that completely engulfs the organism, establishing a protective barrier between the organism and the acidic environment. This action may contribute to the survival of virulent <i>E. coli</i> in contaminated food products and inside a host organism. Colanic acid is a sugar polymer comprised of many six-sugar repeating units that each consist of: glucose, 2,3-acetylated fucose, fucose, galactose, glucuronic acid, and 4,6- pyruvated galactose. While the structure of the repeating unit and the gene cluster responsible for encoding the colanic acid biosynthesis proteins is known, the specific characterization for the majority of the proteins in this pathway has not been elucidated. The goal of this research is to functionally characterize the enzymes responsible for colanic acid repeating unit biosynthesis. All colanic acid biosynthesis genes have been cloned and the corresponding proteins have been expressed and purified. An HPLC assay has been developed to monitor glycosyltransferase activity on a fluorescent isoprenoid anchor.

Characterization of the colanic acid biosynthesis pathway with a novel isoprenoid analog

249th National Meeting (2015)

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