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 (https://doi.org/10.1016/j.molbiopara.2007.08.009)
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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.
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Item type: Article ID code: 13247 Dates: DateEventJanuary 2008Published9 August 2007Published OnlineSubjects: Medicine > Therapeutics. Pharmacology
Medicine > Pharmacy and materia medica
Science > MicrobiologyDepartment: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences Depositing user: Ms Ann Barker-Myles Date deposited: 13 Oct 2009 14:07 Last modified: 08 Apr 2024 16:58 URI: https://strathprints.strath.ac.uk/id/eprint/13247