Anne Imberty

TL;DR: The results of a series of experimental and computational endeavors revealing the unusual distortion of histo-blood group antigens by bacterial and fungal lectins show that conformational adaptation of oligosaccharides is of paramount importance in cell recognition and should be considered when designing anti-infective glyco-compounds.

TL;DR: LecA is identified as a bacterial factor, which utilizes a so far unrecognized mechanism for phospho-CrkIIY221 induction by binding to the host glycosphingolipid receptor Gb3, which represents a signalling receptor for the P. aeruginosa lectin LecA to induce CrkII phosphorylation at tyrosine 221.

TL;DR: In this article, the tetrasaccharide adopts a plate-like overall shape with a very shallow depression on one side, which is clearly apparent on comparing the (Φ, Ψ) torsion angles of the two α-(1→6) linkages.

TL;DR: Comparison of theoretical and experimental data indicates that an equilibrium between two families of low-energy conformers most likely reflects the solution behavior of the trisaccharide in solution, and leads to the conclusion that one conformation of blood group A trisACcharide is selected upon binding by D. biflorus lectin.

TL;DR: The different specificities of DiscI and DiscII for oligosaccharides were rationalized from the different structures obtained by either X-ray crystallography or molecular modeling.