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Caenorhabditis elegans  is a widely accepted model system for parasitic nematodes, drug screening and developmental studies. Similar to parasitic worms,  C. elegans  expresses glycosphingolipids and glycoproteins carrying, in part, phosphorylcholine ( P Cho) substitutions, which might play important roles in nematode development, fertility and, at least in the case of parasites, survival within the host. With the exception of a major secretory/excretory product from  Acanthocheilonema viteae  (ES-62), no protein carrying this epitope has been studied in detail yet. Here we report on the identification, characterization and localization of the aspartyl protease ASP-6 of  C. elegans , which is excreted by the nematode in a  P Cho-substituted form. Within the worm, most prominent expression of the protein is observed in the intestine, while muscle and epithelial cells express  asp-6  to a lesser extent. In animals harboring an ASP-6::GFP fusion protein, diffuse fluorescence throughout the body cavity of adult worms indicates that the chimeric protein is secreted.

biological chemistry

First identification of a phosphorylcholine-substituted protein from  Caenorhabditis elegans : isolation and characterization of the aspartyl protease ASP-6