Atypical post-translational modification and targeting of a Schistosoma mansoni surface receptor, a member of the transforming growth factor beta receptor family of cell surface receptors.

The surface membrane of the intravascular parasite Schistosoma mansoni is composed of not one but two closely apposed lipid bilayers which overlie a syncytial cellular layer, known as the tegument or neodermis. To gain insights into how membrane proteins are transported to and displayed on this unusual surface structure, we have investigated the post-translational modification and targeting of SmRK-1, a receptor and type I membrane protein expressed on the parasite surface, using heterologous expression systems. While SmRK-1 enters the secretory pathway in these systems, our data indicate that the SmRK-1 N-terminal signal peptide is either not cleaved by signal peptidase or is only eleven amino acids long or less. Retention of the signal peptide is accompanied by N-linked glycosylation of an asparagine residue within the predicted signal peptide. The SmRK-1 signal peptide is not capable of directing another cytoplasmic protein to the secretory pathway, suggesting that the signal for insertion of the SmRK-1 extracellular domain into the endoplasmic reticulum resides elsewhere in the protein. Further, SmRK-1 is inefficiently transported to the cell surface in mammalian cells, suggesting that the schistosome neodermis possesses specialized systems for receptor targeting and localization.