CGC Bibliography Paper 3181

Molecular cloning and characterization of an alpha1,3 fucosyltransferase, CEFT-1, from Caenorhabditis elegans.

DeBose-Boyd RA, Kwame Nyame A, Cummings RD

Medline:

98342252

Citation:

Glycobiology 8: 905-917 1998

Type:

ARTICLE

Genes:

Abstract:

We report on the identification, molecular cloning, and characterization of an alpha 1,3 fucosyltransferase (alpha 1,3FT) expressed by the nematode, Caenorhabditis elegans. Although C. elegans glycoconjugates do not express the Lewis x antigen Gal beta 1-->4[Fuc alpha 1-->3]GlcNAc beta-->R, detergent extracts of adult C,elegans contain an al,3FT that can fucosylate both nonsialylated and sialylated acceptor glycans to generate the Le(X) and sialyl Le(X) antigens, as well as the lacdiNAc-containing acceptor GalNAc beta 1-->4GlcNAc beta 1-->R to generate GalNAc beta 1-->4 [Fuc alpha 1-->3]GlcNAc beta 1-->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 alpha 1,3FTs. The putative cDNA for the C,elegans alpha 1,3FT (CEFT-1) was amplified by PCR from a cDNA lambda ZAP library, cloned, and sequenced. COS7 cells transiently transfected with cDNA encoding CEFT-1 express the Le(X), but not sLe(X) antigen. The CEFT-1 in the transfected cell extracts can synthesize Le(X), but not sialyl Le(X), using exogenous accepters. A second fucosyltransferase activity was detected in extracts of C,elegans that transfers Fuc in alpha 1,2 linkage to Gal specifically on type-1 chains. The discovery of alpha-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