Carbohydrate-Protein Interactions and Glycosylation

Oligosaccharides expressed on the surface of cells and in biological fluids as glycoproteins, glycolipids, proteoglycans, and polysaccharides can be recognised by partner proteins, and these interactions have been shown to mediate fundamental biological events such as the immune response, signal transduction, development, and cancer metastasis.

The specificities of these partner proteins (lectins) for their glycan ligands are dictated by glycan composition, shape and density of expression, and the participation of the aglycone moiety in the recognition motif. As additional secondary binding sites continue to be identified, our understanding of the functionality of sugar-binding proteins increases. This issue focuses on recent advances in understanding how C-type lectins in the immune system function, how novel motifs involving asymmetric glycan branch recognition and protein-protein interactions influence critical biological functions such as signal transduction and bactericidal pore formation, as well as recent studies on novel glycan-binding proteins produced by bacteriophage, analysis of the interactions between heparin/heparan sulphate and their binding proteins, and , recent discoveries about the molecular interactions between chondroitin-dermatan sulphate and other bioactive protein components.