Molecular cloning and characterization of a caenorhabditis elegans al,3 fucosyltransferase gene

The helminthic parasite, Schistosoma mansoni, synthesizes fucosylated glycans bearing Lewis X (GalI,4[FucI,3]GlcNAc-R) and fucosylated LacDiNAc (GalNAc/31,4[Fucc1,3]GlcNAc-R) determinants. We have focused our attention on the enzymes responsible for the synthesis of these structures. An 1,3 fucosyltransferase ((M,3 FT) in schistosomes has been identified and characterized. The schistosome 1,3 FT exhibits properties similar to the (1,3 FT in human myeloid cells, termed fucosyltransferase IV (FTIV). In light of the possible involvement of fucosylated glycans in host/parasite interactions, we have extended our studies to other helminths, both parasitic and nonparasitic. We previously identified an c1,3 FT in extracts of the parasitic nematode,Haemonchus contortus, which infect sheep. Like the schistosome enzyme, the H. contortus 1,3 FT displays enzymatic properties closely resembling those of human FTIV. In the present study, we report the identification, molecular cloning, and characterization of an al,3 FT from the non-parasitic helminth Caenorhabditis elegans. The enzyme is homologous to the al,3 FTs found in H. contortus and S. mansoni. The discovery of al,3 fucosylation in C. elegans opens the possibility of using this well-studied nematode as a model system to study the role of fucosylated glycans in the development and/or survival of helminths.