Trottein, F ; Mollicone, R ; Fontaine, J ; de Mendonca, R ; Piller, F ; Pierce, R ; Oriol, R ; Capron, M
Molecular and Biochemical Parasitology 107 (2) 279-287
publié le , mis à jour le
Alpha 3-fucosylation of protein or lipid substrates is an important component of the host/parasite interactions during schistosomiasis. In this process, alpha 3-fucosyltransferases (alpha 3-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 alpha 3-FucT from Schistosoma, mansoni that we termed SmFucTA. The full-length SmFucTA encodes a typical transmembrane type 11 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 alpha 3-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. (C) 2000 Elsevier Science B,V. All rights reserved.