InterPro domain: IPR017177

Helicobacter pylori is a prevalent bacterial, gastroduodenal pathogen of humans that can express Lewis (Le) and related antigens in the O-chains of its surface lipopolysaccharide. The alpha1,3-fucosyltransferase VI (FUT VI) protein is a key enzyme for synthesis of sialyl Lewis X and Lewis X in epithelial cells [ 1 ]. Despite striking functional similarity, there is low sequence homology between the bacterial and mammalian alpha(1,3/4)- and alpha(1,2)-fucosyltransferases. Le antigen expression and fucosylation have multiple biological effects on pathogenesis and disease outcome of H. pylori [ 2 ]. The sialyl-Lewis X (SLe(x)) determinant is important in leukocyte extravasation, metastasis and bacterial adhesion [ 3 ]. Changes in enzyme activity and the expression levels of alpha(1,6)fucosyltransferase [alpha(1,6)FT] occur in certain types of malignant transformations. Alpha(1,6)FT activity is higher in tumour tissue than in healthy tissue. Increased alpha(1,6)FT expression is also found in tumour tissues as compared to healthy and transitional tissues, inflammatory lesions and adenomas [ 4 ].

This group represents an alpha-(1,3)-fucosyltransferase/alpha-(1,4)-fucosyltransferase found in plants.

1. Transcriptional regulation of the fucosyltransferase VI gene in hepatocellular carcinoma cells. Glycoconj. J. 25, 225-35
2. Relevance of fucosylation and Lewis antigen expression in the bacterial gastroduodenal pathogen Helicobacter pylori. Carbohydr. Res. 343, 1952-65
3. Core saccharide dependence of sialyl Lewis X biosynthesis. Glycoconj. J. 123, 641-6
4. Expression and enzyme activity of alpha(1,6)fucosyltransferase in human colorectal cancer. Int. J. Cancer