Molecular cloning and characterization of an 1,3 fucosyltransferase, CEFT-1, from Caenorhabditis elegans

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Abstract
We report on the identification, molecular cloning, and characterization of an α1,3 fucosyltransferase (α1,3FT) expressed by the nematode, Caenorhabditis elegans. Although C.elegans glycoconjugates do not express the Lewis x antigen Galβ1→4[Fucα1→3]GlcNAcβ→R, detergent extracts of adult C.elegans contain an α1,3FT that can fucosylate both nonsialylated and sialylated acceptor glycans to generate the Lex and sialyl Lex antigens, as well as the lacdiNAc-containing acceptor GalNAcβ1→4GlcNAcβ1→R to generate GalNAcβ1→4 [Fucα1→3]GlcNAcβ1→R. A search of the C.elegans genome database revealed the existence of a gene with 20–23% overall identity to all five cloned human α1,3FTs. The putative cDNA for the C.elegans α1,3FT (CEFT-1) was amplified by PCR from a cDNA λZAP library, cloned, and sequenced. COS7 cells transiently transfected with cDNA encoding CEFT-1 express the Lex, but not sLex antigen. The CEFT-1 in the transfected cell extracts can synthesize Lex, but not sialyl Lex, using exogenous acceptors. A second fucosyltransferase activity was detected in extracts of C.elegans that transfers Fuc in α1,2 linkage to Gal specifically on type-1 chains. The discovery of α-fucosyltransferases in C.elegans opens the possibility of using this well-characterized nematode as a model system for studying the role of fucosylated glycans in the development and survival of C.elegans and possibly other helminths.