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Background  Glycosphingolipids (GSL) are integral components of mammalian cell membranes that are involved in cell adhesion and cell signaling processes. GSL are subdivided into structural series, like ganglio-, lacto/neolacto-, globo- and isoglo-series, which are defined by distinct trisaccharide cores. The β1,3 N-acetylglucosaminyltransferase-V (B3gnt5) enzyme catalyzes the formation of the Lc3 structure, which is the core of lactoseries derived GSL.    Results  The biological significance of the glycoconjugates produced by the B3gnt5 enzyme was investigated by inactivating the  B3gnt5  gene in the mouse germline. The disruption of the  B3gnt5  protein-coding region in mouse embryonic stem cells resulted in reduced Lc3-synthase activity, supporting its specific contribution to lactoseries derived GSL synthesis. Breeding of heterozygous mutant mice failed to produce any viable progeny homozygous for the  B3gnt5 -null allele. The genotypic examination of embryos from heterozygous crosses showed that the disruption of the  B3gnt5  gene leads to pre-implantation lethality. This finding was compatible with the expression pattern of the  B3gnt5  gene in the pre-implantation embryo as shown by  in situ  hybridization. The analysis of GSL profiles in embryonic stem cells heterozygous for the  B3gnt5 -null allele confirmed the reduced levels of lactoseries derived GSL levels and of other GSL species.    Conclusion  The disruption of the  B3gnt5  gene in mice affected the expression of lactoseries derived GLS and possibly of protein-bound β3GlcNAc-linked glycans, thereby demonstrating an essential contribution of these glycoconjugates in early embryonic development, and supporting the importance of these glycoconjugates in cell differentiation and adhesion processes.

The Lc3-synthase gene B3gnt5is essential to pre-implantation development of the murine embryo