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(Received for publication, June 6, 1996)
From the Department of Neurobiology, Swiss Federal Institute of
Technology, Hönggerberg, CH-8093 Zürich, Switzerland and
the § Department of Bio-Organic Chemistry, Bijvoet Center
for Biomolecular Research, Utrecht University, P. O. Box 80.075, NL-3508 TB Utrecht, The Netherlands
The HNK-1 carbohydrate epitope, expressed by many
neural recognition molecules, is involved in cell interactions that
control cell type-specific neurite outgrowth and regeneration. It is
also the target for autoimmune IgM antibodies in demyelinating
neuropathies of the peripheral nervous system in humans. Despite its
acknowledged importance in cell interactions, the HNK-1 carbohydrate
structure, when expressed on glycoproteins, is still unknown. Here, we
describe the structure of one of the predominant HNK-1-bearing glycans
of bovine P0. The epitope consists of the sulfated trisaccharide
SO4-3GlcA
Volume 271, Number 38,
Issue of September 20, 1996
pp. 22957-22960
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
1-3Gal1-4GlcNAc, attached to the 
1-6
arm of a diantennary core with a bisecting
N-acetylglucosamine. It is the first example of a terminal
3-sulfated glucuronic acid on an asparagine-linked carbohydrate.
Because the similarity between the glycoprotein-derived structure and
the glycosphingolipids carrying HNK-1 is restricted to the terminal
sulfated trisaccharide, we conclude that this element is sufficient for
HNK-1 immunoreactivity. Knowledge of the HNK-1 structure on proteins is
an important prerequisite for the elucidation of its functional role in
development and disease.
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