Gal-Specific Neolectins: Towards Promising Diagnostic Tools.

In the absence of naturally available galactofuranose-specific lectin, we report herein the bioengineering of GalNeoLect, from the first cloned wild-type galactofuranosidase ( sp. strain JHA19), which recognises and binds a single monosaccharide that is only related to nonmammalian species, usually pathogenic microorganisms. We kinetically characterised the GalNeoLect to confirm attenuation of hydrolytic activity and used competitive inhibition assay, with close structural analogues of Gal, to show that it conserved interaction with its original substrate. We synthetised the bovine serum albumin-based neoglycoprotein (GalNGP), carrying the multivalent Gal units, as a suitable ligand and high-avidity system for the recognition of GalNeoLect which we successfully tested directly with the galactomannan spores of (ATCC 16404). Altogether, our results indicate that GalNeoLect has the necessary versatility and plasticity to be used in both research and diagnostic lectin-based applications.