Category Archives: What’s up in Glycobiology

Latest GLYcoDiag’s publications

1. Last publication about the use of our FimH and DC-SIGN LEctPROFILE kits for the design of new gold mannoside nanoparticles. We thank Dr.Stephane Vincent (from the University of namur) to give us the chance to be associated with this wonderful work.

Wang, T. et al. “Glycofullerene-AuNPs as multivalent ligands of DC-SIGN and bacterial lectin FimH: tuning nanoparticule size and ligand density”. Nanoscale, 2023, 15, 11657-11666. DOI:

2. First publication of the collaborative work (ANR Cyclick) between University of Le Mans (IMMM), University of Nantes (CEISAM) and GLYcoDiag about the synthesis of linear glycopolymers and their evaluations through lectins interactions (ConA, BC2LA, FimH, Langerin and DC-SIGN).

Gonnot, C. et al.ROMP-based Glycopolymers with high Affinity for mannose-binding lectins”. Biomacromolecules, 2023, 14, 3689-3699.

Glycobiological interaction studies – a key for the understanding of exopolysaccharide behavior and biofilm formation.

Recently, the group of Parsek have published a study about the function of the exopolysaccharide (PsI) found in Pseudomonas aeruginosa and its interaction with the bacterial lectin LecB that induce stabilisation of the biofilm. This work justifies the interest of glycobiological interactions studies that enable to answer and explain some stayed unknown mecanisms up to now. The expertise of GLYcoDiag in this field is now well known through the GLYcoPROFILE technology platform which is adapted for bacteria-cells glycobiological interactions studies.

Learn more about GLYcoPROFILE

Passos da Silva, D., Matwichuk, M. L., Townsend, D. O., Reichhardt, C., Lamba, D., Wozniak, D. J., Parsek, M. R., Nat. Comm., 2019, 10, 2183 (DOI : 10,1038/s41467-019-10201-4)

Tulipa gesneriana agglutinin (TXLC-I) a Gal/GalNAc lectin is now available

Tulipa gesneriana agglutinin (TxLC-I) is isolated from tulip bulbs and purified by affinity column chromatography on a Fetuin-Sepharose 4B gel. TxLC-I was originally described as a tetramer of four identical subunits of 28 kDa. Then, after amino acid sequence analyses, this subunit seems to be partialy cleaved into two smaller polypeptides of approximatively 14 kDa each. TxLC-I have a Gal/GalNAc binding domain and show highest affinity to triantennary carbohydrates and diantennary oligosaccharide with Gal residues.
GLYcoDiag lectin TxLC-I v1.2

GLYcoDiag participate to a research collaboration aimed at the study of new lectin ligands

H. Prasch, C. Hojnik, T. K. Lindhorst, B. Didak, L. Landemarre, T. M. Wrodnigg. New lectin ligands: Testing of Amadori rearrangement products with a series of mannoside-specific lectins, Carbohydr. Res., 2019, accepted manuscript (DOI: 10.1016/j.carres.2019.01.010).

C-glycosyl-type compounds derived from an Amadori rearrangement: D-glycero-D-galacto-aldoheptose and the two corresponding multivalent BSA neoglycoproteins, were evaluated as ligands on a series of seven relevant mannose-specific lectins. The evaluation of the IC50-value (concentration corresponding to 50% of inhibition) of the compounds has been evaluated. Multivalency turned out to effectively influence ligand selectivity and lectin binding.

GLYcoDiag participate to a research collaboration aimed at the study of sialidases and multivalent thiosialosides

Brissonnet, Y., Assailly, C. Saumonneau, A., Bouckaert, J., Maillasson, M., Petito, C., Roubinet, B., Didak, B., Landemarre, L., Bridot, C., Blossey, R., Deniaud, D., Yan, X., Bernard, J. Tellier, C., Grandjean, C., Daligault, F., Gouin, S. G., Multivalent thiosialosides and their synergistic interaction with pathogenic sialidases, Chem. Eur. J., accepted article (DOI: 10.1002/chem.201805790)

Sialidases (SA) hydrolyze sialyl residues from glycoconjugates of the eukaryotic cell surface and are virulence factors expressed by pathogenic bacteria, viruses and parasites. The catalytic domain of SA are often flanked with carbohydrate-binding module(s) previously shown to bind sialosides and to enhance enzymatic catalytic efficiency. Here we designed non-hydrolyzable multivalent thiosialosides as probes and inhibitors of V. cholerae, T. cruzi and S. pneumoniae (NanA) sialidases. NanA was truncated from the catalytic and lectinic domains (NanA-L and NanA-C) to probe their respective roles when interacting with sialylated surfaces and the synthetically designed di-, and polymeric thiosialosides. NanA-L domain was shown to fully drive NanA binding, improving affinity for the thiosialylated surface and compounds by more than two orders of magnitude. Importantly, each thiosialoside grafted onto the polymer was also shown to reduce NanA and NanA-C catalytic activity with a 3000-fold higher efficiency compared to the monovalent thiosialoside reference. These results extend the concept of multivalency for designing potent bacterial and parasitic sialidase inhibitors.