Structural and biological properties of the carbohydrate units of nervous tissue glycoproteins

We have identified structures in nervous tissue glycoproteins that are novel for glycoproteins in general or enriched in nervous tissue or cells of neural origin. These include: (alpha 2-8)-linked polysialic acid units, the linear form of poly-N-acetyllactosamine glycans, the sialylated X antigen determinant NeuAc(alpha 2-3)-Gal(beta 1-4) [Fuc(alpha 1-3)]GlcNAc, a series of Man-O-Ser(Thr)-linked glycans, and the O-glycosidically linked disaccharide unit Gal(alpha 1-3)GalNAc. The polysialic and poly-N-acetyllactosamine glycans are also developmentally regulated. The polysialic acid units in the cell adhesion molecule N-CAM. The poly-N-acetyllactosamine units occur in the adhesion molecule NILE (which is immunologically similar to Ng-CAM and L1) and in some other components revealed by a cell surface-labelling method specific for these glycans. The mannose-linked glycans occur in a chondroitin sulphate proteoglycan involved in neuron-glia interactions. Other biological interactions of the carbohydrates include their serving as bacterial receptors in meningitis, their serving as models for molecular mimicry by the capsules of meningitis-causing bacteria, and the role of some structures as antigens in autoimmune conditions. At the molecular level, two types of mechanisms are suggested for the glycans in molecular interactions: they may function either as mediators of interactions by serving as specific recognition ligands, or as modulators of the interactions determined by polypeptides or other molecules.