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Gene inactivation confirms the identity of enzymes involved in nematode phosphorylcholine-N-glycan synthesis

Houston, Katrina M. and Sutharsan, Ratneswary and Steiger, C.N. and Schachter, Harry and Harnett, W. (2008) Gene inactivation confirms the identity of enzymes involved in nematode phosphorylcholine-N-glycan synthesis. Molecular and Biochemical Parasitology, 157 (1). pp. 88-91. ISSN 0166-6851

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Abstract

An unusual feature of nematodes is the covalent attachment of immunomodulatory phosphorylcholine (PC) moieties to N-type glycans. Our previous work on the filarial nematode glycoprotein ES-62 has enabled us to predict the identity of enzymes necessary for PC-N-glycan biosynthesis. Here, we addressed these predictions using gene knockout technology applied to C. elegans and present two pieces of confirmatory data. Employing a triple null mutant worm lacking all three genes that encode active UDP-N-acetyl-d-glucosamine: α-3-d-mannoside β1, 2-N-acetylglucosaminyltransferase I (GnT I) we have confirmed our earlier prediction that a crucial step in the generation of the substrate for PC transfer is addition of terminal GlcNAc to the α1-3-linked mannose residue of the glycan by GnT I. Second, by silencing genes responsible for expressing enzymes of the Kennedy pathway of phosphatidylcholine biosynthesis by RNA interference (RNAi), we have confirmed our belief for a role for diacylglycerol: choline phosphotransferase (CPT) in PC-N-glycan biosynthesis.

Item type: Article
ID code: 13247
Keywords: C. elegans, gene inactivation, N-glycan, phosphorylcholine, pharmacology, Therapeutics. Pharmacology, Pharmacy and materia medica, Microbiology, Molecular Biology, Parasitology
Subjects: Medicine > Therapeutics. Pharmacology
Medicine > Pharmacy and materia medica
Science > Microbiology
Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
Related URLs:
    Depositing user: Ms Ann Barker-Myles
    Date Deposited: 13 Oct 2009 15:07
    Last modified: 04 Sep 2014 22:09
    URI: http://strathprints.strath.ac.uk/id/eprint/13247

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