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

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. We report here that extracts from S. mansoni adult male and female worms contain a beta 1,4-galactosyltransferase activity that transfers galactose from the donor substrate UDP-galactose to the acceptor substrate N-acetylglucosamine in a beta 1,4-linkage position to form the disaccharide Gal beta 1,4GlcNAc. In this respect the schistosome-derived activity is similar to that commonly found in mammalian tissues. The kinetic properties, however, of the common beta 1,4-galactosyltransferase activity in mammalian tissues are dramatically altered in the presence of the modifier protein alpha-lactalbumin, whereas the beta 1,4-galactosyltransferase activities in adult male and female schistosomes are not altered by this modifier. Overall, our results demonstrate that adult schistosomes contain a beta 1,4-galactosyltransferase activity and that it is unlike that commonly found in mammalian tissues.