Recombinant H. pylori Fucosyltransferase Protein, CF

Lewis X (Le^X), a fucosylated trisaccharide glycan epitope (Gal beta1,4 [Fuc alpha1,3]GlcNAc beta) also known as CD15, and sialylated Lewis X (sLe^X) are distributed throughout eukaryotes and are determinants of many functional glycoconjugates that play central roles in numerous physiological and pathological processes (1, 2). Le^x-bearing glycans are also found in the infectious bacterium Helicobacter pylori to mask the bacterium from the host immune surveillance (3). H. pylori is the pathogen that causes peptic ulcers that can further lead to stomach cancer and gastritis. H. pylori fucosyltransferase is responsible for generating the Le^X glycans, therefore is potentially a drug target for curing peptic ulcers, gastritis and stomach cancer. In molecular terms, H. pylori fucosyltransferase is an  alpha1,3 fucosyltransferase that shares function with human FUT4, FUT5, FUT6, and FUT9 (4). Remarkably, H. pylori fucosyltransferase can transfer IgG antibody to the glycocalyx on the surfaces of live cells when the antibody is conjugated to the enzyme's natural donor substrate GDP-Fucose (5). The activity of this enzyme has been measured with a phosphatase coupled method (6).