First identification of a phosphorylcholine-substituted protein from Caenorhabditis elegans: isolation and characterization of the aspartyl protease ASP-6.
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 (PCho) 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 PCho-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.
Lochnit
Günter
G
Institute of Biochemistry, Faculty of Medicine, Justus-Liebig-University, Friedrichstrasse 24, D-35392 Giessen, Germany.
Grabitzki
Julia
J
Henkel
Björn
B
Tavernarakis
Nektarios
N
Geyer
Rudolf
R
D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D017173:Caenorhabditis elegans / Q000201:enzymology* / Q000235:genetics; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010767:Phosphorylcholine / Q000378:metabolism*
D010767:Phosphorylcholine; D016282:Aspartic Acid Endopeptidases