Schistosoma mansoni contains a galactosyltransferase activity distinct from that typically found in mammalian cells

Abstract

It has been reported previously that some complex-type Asn-linked oligosaccharides contained in glycoproteins synthesized by Schistosoma mansoni adult males contain terminal galactosyl residues [17]. We report here that extracts from S. mansoni adult male and female worms contain a β1,4-galactosyltransferase activity that transfers galactose from the donor substrate UDP-galactose to the acceptor substrate N-acetylglucosamine in a β1,4-linkage position to form the disaccharide Galβ1,4GlcNAc. In this respect the schistosome-derived activity is similar to that commonly found in mammalian tissues. The kinetic properties, however, of the common β1,4-galactosyltransferase activity in mammalian tissues are dramatically altered in the presence of the modifier protein α-lactalbumin, whereas the β1,4-galactosyltransferase activities in adult male and female schistosomes are not altered by this modifier. Overall, our results demonstrate that adult schistosomes contain a β1,4-galactosyltransferase activity and that it is unlike that commonly found in mammalian tissues.