Fucosylated glycoconjugates of the human spermatozoon. Comparison of the domains of these glycoconjugates with the alpha-fucosyl binding sites, and with lactosaminic glycoconjugates and beta-D-galactosyl binding site domains.

Fucosylated glycoconjugates play an important role in fertilization as the recognition signal of the zona pellucida. In this work, using "critical" concentrations of either, FITC Lotus tetragonolobus lectin or FITC alpha-L-fucosyl-BSA neoglycoprotein as molecular probes, population densities of fucosylated glycoconjugates and of their "complementary" molecules (carrying fucosyl receptors), were found all over the sperm surface with higher population densities in post acrosomal sheath, neck and midpiece. These results were compared with previously reported data on the population densities of lactosaminic compounds and their "complementary" molecules, obtained on same samples of spermatozoa. Statistical data demonstrate that fucosylated glycoconjugates share the same domains with biantennary N-acetyllactosaminic oligosaccharides carrying outer galactose and bisected N-acetylglucosamine residues. These domains highly differ with those of the lactosaminic glycoproteins carrying tri and tetraantennary N-acetyllactosaminic oligosaccharides. These studies also show that the domains of fucosylated glycoconjugates and their "complementary" molecules (carrying fucosyl receptors) locate in different zones of the spermatozoon than those of the compounds carrying beta-galactosyl receptors. Besides, the results suggest structural differences between fucosylated glycoconjugates of the acrosome, equatorial zone and post acrosomal sheath. This may be relevant to the different biological behavior of these compounds and zones, in fertilization.