Molecular cloning of a putative alpha 3-fucosyltransferase from Schistosoma mansoni

Alpha 3-fucosylation of protein or lipid substrates is an important compone nt of the host/parasite interactions during schistosomiasis. In this proces s, alpha 3-fucosyltransferases (alpha 3-FucTs) are considered as key enzyme s ensuring both parasite survival and :adaptation in their (in)vertebrate h osts. In this paper, we report the molecular cloning of a putative alpha 3- FucT from Schistosoma, mansoni that we termed SmFucTA. The full-length SmFu cTA encodes a typical transmembrane type 11 protein with a short cytoplasmi c domain, a transmembrane segment and a long C-terminal catalytic domain. I n this region, the GDP-fucose binding site is well conserved whereas the pu tative acceptor site displays sequence divergence compared to the correspon ding region from vertebrate and invertebrate alpha 3-FucTs. Southern blot a nalysis suggested that SmFucTA is present as several copies or has highly r elated counterparts in the S. mansoni genome. Northern blot revealed a sing le SmFucTA transcript at 2 kb in adult worms. Affinity purified antibodies directed against recombinant SmFucTA identified a 50 kDa native protein tha t localizes to the subtegumental and parenchymal regions of adult worms. (C ) 2000 Elsevier Science B,V. All rights reserved.