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Papers In Press, published online ahead of print September 13, 2004
Department für Chemie, Universität für Bodenkultur, Wien A-1190
Corresponding Author: iwilson{at}edv2.boku.ac.at
Cross-reactivity with anti-horseradish peroxidase antiserum is a feature of many glycoproteins from plants and invertebrates; indeed staining with this reagent has been used to track neurons in Drosophila melanogaster and Caenorhabditis elegans. Although in insects the evidence indicates that the cross-reaction is due to the presence of core
J. Biol. Chem, 10.1074/jbc.M408978200
Submitted on August 5, 2004
Revised on September 13, 2004
Accepted on September 13, 2004
Molecular basis of anti-horseradish peroxidase staining in Caenorhabditis elegans
1,3-fucosylated N-glycans, the molecular basis for anti-horseradish peroxidase staining in nematodes has been, to date, unresolved. Using Western blots of wild-type and mutant C. elegans extracts in conjunction with specific inhibitors we show that the cross-reaction is due to core 1,3-fucosylation. Of various mutants examined, one with a deletion of the fut-1 (K08F8.3) gene showed no reaction to anti-horseradish peroxidase; the molecular phenotype was rescued by injection of either the K08F8 cosmid or the fut-1 open reading frame under control of the let-858 promoter. Furthermore, expression of fut-1 cDNA in Pichia and insect cells in conjunction with antibody staining, HPLC and MALDI-TOF MS analyses showed that FUT-1 is a core 1,3-fucosyltransferase with an unusual substrate specificity: it is the only core fucosyltransferase in plants and animals described to date that does not require the prior action of N-acetylglucosaminyltransferase I.
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