Molecular cloning of a putative alpha3-fucosyltransferase from Schistosoma mansoni.

Alpha 3-fucosylation of protein or lipid substrates is an important component of the host/parasite interactions during schistosomiasis. In this process, alpha3-fucosyltransferases (alpha3-FucTs) are considered as key enzymes ensuring both parasite survival and adaptation in their (in)vertebrate hosts. In this paper, we report the molecular cloning of a putative alpha3-FucT from Schistosoma mansoni that we termed SmFucTA. The full-length SmFucTA encodes a typical transmembrane type II protein with a short cytoplasmic domain, a transmembrane segment and a long C-terminal catalytic domain. In this region, the GDP-fucose binding site is well conserved whereas the putative acceptor site displays sequence divergence compared to the corresponding region from vertebrate and invertebrate alpha3-FucTs. Southern blot analysis suggested that SmFucTA is present as several copies or has highly related counterparts in the S. mansoni genome. Northern blot revealed a single SmFucTA transcript at 2 kb in adult worms. Affinity purified antibodies directed against recombinant SmFucTA identified a 50 kDa native protein that localizes to the subtegumental and parenchymal regions of adult worms.