Mannosyl transferase activity in homogenates of adult Schistosoma mansoni.

Homogenates of adult Schistosoma mansoni contain enzymes which are capable of transferring [14C]mannose from GDP[U-14C]mannose to a lipid acceptor which migrates as a single peak on a silica gel thin-layer plate. This lipid may belong to the class of polyprenol monophosphates which are intermediate elements in the glycosylation of nascent proteins. The schistosome mannosyl transferase activity is associated with membranous particles and is dependent on the presence of Mn2+. However, other divalent metals such as Mg2+ or Ca2+ can, in decreasing order of efficiency, replace Mn2+. When UDP[U-14C]glucose was incubated with the homogenates in the same conditions, relatively little label was transferred to the lipid acceptor. Live worms incubated in a medium containing GDP[U-14C]mannose seem to incorporate the label preferentially on the tegument and on adjacent subtegumental structures. By adding foetal calf serum to the medium, incorporation of the label can be stimulated.