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.
Rivera-Marrero
C A
CA
Department of Zoology, University of Georgia, Athens 30602.
Cummings
R D
RD
D000117:Acetylglucosamine / Q000378:metabolism; D000818:Animals; D002850:Chromatography, Gel; D002854:Chromatography, Paper; D005260:Female; D005690:Galactose / Q000378:metabolism; D005700:Galactosyltransferases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D007768:Lactalbumin / Q000494:pharmacology; D008297:Male; D012550:Schistosoma mansoni / Q000201:enzymology*
D007768:Lactalbumin; D005700:Galactosyltransferases; C067546:N-acetylglucosamine 4-beta-galactosyltransferase; D000117:Acetylglucosamine; D005690:Galactose