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Glycobiology Advance Access published online on December 15, 2004
Glycobiology, doi:10.1093/glycob/cwi028
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© Oxford University Press 2004; all rights reserved.
Received July 7, 2004
Revised November 2, 2004
Accepted December 10, 2004

Article

Fucosyltransferase substrate specificity and the order of fucosylation in invertebrates

Katharina Paschinger 1, Erika Staudacher 2, Ute Stemmer 2, Gustáv Fabini 3, and Iain B. H. Wilson 2*

1 Department für Chemie der Universität für Bodenkultur Muthgasse 18, 1190 Wien, Austria
2 Department für Chemie der Universität für Bodenkultur Muthgasse 18, 1190 Wien, Austria
3 Department für Chemie der Universität für Bodenkultur Muthgasse 18, 1190 Wien, Austria; Octapharma Pharmazeutika Produktionsges.m.b.H., A-1100 Wien

* To whom correspondence should be addressed.
Iain B. H. Wilson, E-mail: iain.wilson{at}boku.ac.at


  Abstract

Core {alpha}1,6-fucosylation is a conserved feature of animal N-linked oligosaccharides being present in both invertebrates and vertebrates. In order to prove that the enzymatic basis for this modification is also evolutionarily conserved, cDNAs encoding the catalytic regions of the predicted Caenorhabditis elegans and Drosophila melanogaster homologues of vertebrate {alpha}1,6-fucosyltransferases (EC 2.4.1.68) were engineered for expression in the yeast Pichia pas oris. Recombinant forms of both enzymes were found to display core fucosyltransferase activity as shown by a variety of methods.Unsubstituted non-reducing terminal GlcNAc residues appeared to be an obligatory feature of the substrate for the recombinant Caenorhabditis and Drosophila {alpha}1,6- fucosyltransferases, as well as for native Caenorhabditis and Schis osoma mansoni core {alpha}1,6-fucosyltransferases. On the other hand, these {alpha}1,6-fucosyltransferases could not act on N-glycopeptides already carrying core {alpha}1,3-fucose residues, whereas recombinant Drosophila and native Schistosoma core {alpha}1,3-fucosyltransferases were able to utilise core {alpha}1,6-fucosylated glycans as substrates. Lewis-type fucosylation was observed with native Schistosoma extracts and could take place after core {alpha}1,3- fucosylation, whereas prior Lewis-type fucosylation precluded the action of the Schistosoma core {alpha}1,3-fucosyltransferase. Overall, we conclude that the strict order of fucosylation events, previously determined for fucosyltransferases in crude extracts from insect cell lines (core {alpha}1,6 before core {alpha}1,3), also applies for recombinant Drosophila core {alpha}1,3- and {alpha}1,6-fucosyltransferases as well as for core fucosyltransferases in schistosomal egg extracts.

Keywords: Caenorhabditis, Drosophila, Schistosoma, fucosyltransferase.
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