P0 protein was prepared from bovine spinal root myelin. The purity was shown by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunostaining with affinity purified antisera. P0 in the presence of lysophosphatidylcholine induced paralysis and histological lesions resembling experimental allergic neuritis in Lewis rats. Lysophosphatidylcholine also enhanced the ability of P2 to produce neuritis. The conformation of these proteins may be important in determining their ability to induce experimental allergic neuritis. P0 deserves consideration as an antigen relevant to Guillain-Barré syndrome.