Deciphering the recognition features of glycans by human lectins at the molecular level

Abstract

Carbohydrates are one of the most variable and complex molecules of biological systems. They areusually located at the cell membrane, mainly as glycoconjugates, glycoproteins or glycolipids and play an important role in the specific molecular recognitions. Since structure and function are intrinsically correlated, the three-dimensional shape, dynamics and presentation of these molecules is essential for the recognition processes to take place.In this work, we have employed a combination of X-Ray crystallography and Nuclear Magnetic Resonance spectroscopy (NMR) techniques, for obtaining atomic-scale information on the interactions of glycans and glycomimetics, using either intact glycoproteins (the receptor binding domain of the spikegly coprotein of SARS CoV2) or small molecules, with different receptors related to human diseases, with special emphasis on galectins and siglecs (immune response). The presented methodology allows disentangling the fine details of the vital glycan epitopes, providing key information for the developmentof novel therapeutics.