In vivo activity of recombinant human Lewis fucosyltransferase III in leaves of Nicotiana tabacum L.

Fucosylation in plants occurs in glycoproteins and polysaccharides but the function of fucosylation is largely unknown. We aimed to analyze the effects of over-expression of human fucosyltransferase III (hFucT III) on in vivo N-glycan accumulation in tobacco plant leaves and focused on comparing the amount of Lewis a (Lea)-epitope accumulation in transgenic and in wild-type plants. Fucosyltransferase assays, Western blot and mass spectrometry were used to identify, quantify and analyse Lea N-glycans. We found that constitutive overexpression of hFucT III activity had no effect on Lea complex type N-glycans accumulation. Our results suggest that tobacco recombinant hFucT III acts more as a hydrolase than as a transferase.