A novel α1,2-fucosyltransferase (CE2FT-2) in Caenorhabditis elegans generates H-type 3 glycan structures

Abstract

The α1,2-fucosyltransferase family (α1,2FT) is the largest family of glycosyltransferases in the genome of the free-living nematode Caenorhabditis elegans, and early evidence suggests that each member may have a unique activity. Here we describe a C. elegans gene (designated CE2FT-2) encoding an α1,2FT that has the potential to generate the sequence Fucα1-2Galβ1-3GalNAcα-R, which is the H-type 3 blood group structure. The CE2FT-2 cDNA encodes a putative transmembrane protein that shows ∼42% amino acid identity to a previously cloned C. elegans α1,2FT (termed CE2FT-1), but has a very low identity (∼16-20%) to α1,2FT sequences in humans, rabbits, and mice. A recombinant form of CE2FT-2 expressed in human 293T cells has a high α1,2FT activity toward Galβ1-3GalNAcα-O-pNP, but unexpectedly, the enzyme is inactive toward the acceptor Galβ-O-phenyl. Thus, CE2FT-2 differs from all other α1,2FTs previously described from animals that all utilize Galβ-O-phenyl. CE2FT-2 is expressed at all stages of worm development, but remarkably, promoter analysis of the CE2FT-2 gene using green fluorescent protein reporter constructs indicates that the CE2FT-2 is expressed exclusively in pharyngeal cells of the worm from embryo to an adult stage. Because pharyngeal cells are known to secrete their glycoconjugates to the nematode surface, these results may indicate that products of CE2FT-2 contribute to interactions of the nematode with its environment or are used as ligands for bacterial attachment. These findings, along with those on other α1,2FTs in C. elegans, suggest that each α1,2FT in this organism may have a unique acceptor specificity, expression pattern, and biological function. © 2008 The Author(s).