Comparison of the N‐Linked Oligosaccharide Structures of the Two Major Human Myelin Glycoproteins MAG and P0: Assessment of the Structures Bearing the Epitope for HNK‐1 and Human Monoclonal Immunoglobulin M Found in Demyelinating Neuropathy

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Abstract
The epitope for HNK‐1 and patient's monoclonal autoantibodies in demyelinating polyneuropathy associated with immunoglobulin M gammopathy is borne by different types of N‐linked Oligosaccharide structures in human PO and myelin‐associated glycoprotein (MAG). Fourteen glycopep‐tide fractions bearing different Oligosaccharide structures were obtained from either MAG or P0 glycopeptides by serial lectin affinity chromatography on concanavalin A‐Sepharose, Phaseolus vulgaris erythrophytohemagglutinin‐agarose, Pisum sativum agglutinin‐agarose, and Phaseolus vulgaris leucophytohemagglutinin‐agarose. As shown by dot‐TLC plate immunostaining, the same MAG and P0 glycopeptide fractions were recognized by HNK‐1 and patient's immunoglobulin M, confirming that these antibodies display similar specificities. The antigenic carbohydrate was present in glycopeptide fractions that either interact with Pisum sativum agglutinin‐agarose or were bound by Aleuria aurantia agglutinin‐digoxigenin, indicating that these structures contained α(l‐6)fucose residues. This study demonstrates that the L2/ HNK‐1 epitope is borne mainly or even exclusively by N‐linked Oligosaccharide structures α(l‐6)fucosylated in the core.

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