Caenorhabditis elegans glycosylation
Abstract
The model organism, Caenorhabditis elegans, is being much studied at the genetic level; however, its glycosylation is poorly understood. Recent data from this and other laboratories suggest that the carbohydrates covalently-bound to nematode glycoproteins share some basic features with those found in mammals, but have some novel decorations. In particular, the presence of asparagine-linked glycan structures with up to four fucose residues and two O-methyl substitutions is highly intriguing. O-methylated residues have also been found on the nematode's O-linked oligosaccharides. Some of these features are shared, at least in part, by parasitic nematodes and so Caenorhabditis elegans is potentially a useful model for developing novel strategies in the study of these types of oligosaccharides with potential benefits in combatting nematode parasites. In the proposed study, it is intended to complete the analyses of the glycan structures and to initiate a study of their biosynthesis. In particular, the relevant fucosyl- and methyltransferases will be assayed from nematode extracts. Further, purification of these enzymes will be performed and their peptide maps compared to the protein sequences predicted from the complete genomic sequence. The corresponding cDNAs will be cloned and expressed and the enzymatic activity of the recombinant proteins tested. Recombinant enzymes will be used in synthesis of key N- and O-linked structures and these will be conjugated to protein in order to raise antibodies against the putatively immunogenic oligosaccharides. These antibodies could then be used to examine a wide range of extracts from parasitic nematodes. In particular, we will apply our findings to Haemonchus contortus, a parasite of sheep and cattle.
- Caenorhabditis
- glycosylation
- fucosyltransferases
- methylation
Publications
More structures than cells? The N-glycans of Caenorhabditis elegans.
Autoren: Kolarich, D., Fabini, G., Wilson, I.B.H., Altmann, F. Jahr: 2001
Conference & Workshop proceedings, paper, abstract
Molecular basis of anti-horseradish peroxidase staining in Caenorhabditis elegans.
Autoren: Paschinger, K; Rendic, D; Lochnit, G; Jantsch, V; Wilson, IB Jahr: 2004
Journal articles
Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates.
Autoren: Paschinger, K; Staudacher, E; Stemmer, U; Fabini, G; Wilson, IB Jahr: 2005
Journal articles
Definition of immunogenic carbohydrate epitopes.
Autoren: Paschinger, K; Fabini, G; Schuster, D; Rendic, D; Wilson, IB Jahr: 2005
Journal articles
Reconstitution in vitro of the GDP-fucose biosynthetic pathways of Caenorhabditis elegans and Drosophila melanogaster.
Autoren: Rhomberg, S; Fuchsluger, C; Rendic, D; Paschinger, K; Jantsch, V; Kosma, P; Wilson, IB Jahr: 2006
Journal articles
Comparative characterisation of recombinant invertebrate and vertebrate peptide O-Xylosyltransferases.
Autoren: Brunner, A; Kolarich, D; Voglmeir, J; Paschinger, K; Wilson, IB Jahr: 2006
Journal articles
In vitro-Wiederherstellung der GDP-Fukose-Biosynthesewege von Caenorhabditis elegans and Drosophila melanogaster
Autoren: Rhomberg, S. Jahr: 2006
Master / Diploma Thesis
Biosynthesis of truncated N-linked oligosaccharides results from non-orthologous hexosaminidase-mediated mechanisms in nematodes, plants, and insects
Autoren: Gutternigg, M; Kretschmer-Lubich, D; Paschinger, K; Rendic, D; Hader, J; Geier, P; Ranftl, R; Jantsch, V; Lochnit, G; Wilson, IBH Jahr: 2007
Journal articles
Complicated N-linked glycans in simple organisms.
Autoren: Schiller, B; Hykollari, A; Yan, S; Paschinger, K; Wilson, IB; Jahr: 2012
Journal articles
Project staff
Iain B.H. Wilson
Ao.Univ.Prof. Dr.phil. Iain B.H. Wilson
iain.wilson@boku.ac.at
Tel: +43 1 47654-77216, 77217
Project Leader
01.01.2002 - 28.02.2005
Katharina Paschinger
Dipl.-Ing. Dr. Katharina Paschinger
katharina.paschinger@boku.ac.at
Tel: +43 1 47654-77216, 77217
Project Staff
01.01.2002 - 28.02.2005