Abstract
The L2/HNK-1 carbohydrate epitope has been shown to carry an unusual 3'-sulfoglucuronic acid linked O-glycosidically through a neolactosyl-type backbone to a ceramide residue. Using monoclonal antibodies, the same or a closely related epitope has also been detected N-glycosidically linked to glycoproteins, amongst them several neural cell adhesion molecules. We used synthetic glycolipids carrying sulfated or non-sulfated glucuronic acid attached to ceramide through glycans of different length to show that not only the sulfated glucuronic acid but also the neolactosyl-type backbone is essential for the recognition of the L2/HNK-1 carbohydrate by a monoclonal antibody, its binding to laminin and its role in neural cell migration and outgrowth of processes from neurons and astrocytes.