Characterization and partial purification of a novel 36 kDa peripheral myelin protein recognized by the sera of patients with neurological disorders.

Sera of some patients with acquired sensory neuropathy, chronic inflammatory demyelinating polyradiculoneuropathy and motor neuron disease have high titres of IgG autoantibodies to a minor human peripheral nerve glycoprotein of approximately 36 kDa. This protein cofractionated with PNS myelin and was also found in bovine and rat nerve but not in CNS myelin or other nonneural human tissues. The N-terminal sequence revealed that this protein is related to the major myelin protein P0. Monoclonal antibodies to P0 and to the carbohydrate epitope HNK-1 did not recognize the 36-kDa protein, and the human anti-36-kDa antibodies did not bind to P0. IgG binding to this protein was not abolished after periodate oxidation or deglycosylation, suggesting that the epitope recognized by the human antibodies is peptidic. Differential glycosylation did not account for the differences in the apparent molecular weight between these two proteins. Overall our results indicate that the 36-kDa protein is a variant of P0.