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.

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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)

Glycodiag support the 30th Glycobiology meeting (JGM) at Villeneuve d’Ascq from 27th to 29 October 2019. If you want to participate visit the following website.

Event’s WebSite

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

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.

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.