Cross-reactivity of anti-galactocerebroside autoantibodies with a Trypanosoma brucei proteolipidic epitope.

Pathogenic mechanisms of the demyelinating encephalopathy featuring the nervous phase of human African trypanosomiasis (HAT) are largely unknown. They might include autoimmune disorders. A variety of autoantibodies is detected during the disease and we have previously evidenced anti-galactocerebroside (GalC) antibodies in the serum and cerebrospinal fluid (CSF) from patients in the nervous stage (stage II) of HAT. We now show that anti-GalC antibodies recognize an antigen located on the parasite membrane and common to different strains of trypanosomes. By using affinity chromatography with a rabbit anti-GalC antiserum, a 52-kD proteolipid was isolated from the membrane of Trypanosoma brucei (T. b.) brucei AnTat 1.9, AnTat 1. 1E, and T. b. rhodesiense Etat 1.2/R and Etat 1.2/S. Antibodies directed against this antigen were found in the CSF from patients with nervous stage HAT. These CSF also contained anti-GalC antibodies and adsorption with the proteolipid decreased anti-GalC reactivity. Immunization of mice with this antigen induced the production of antibodies which cross-reacted with GalC but no protection from experimental infection with T. b. brucei. These data support the hypothesis that anti-GalC antibodies detected in the CSF from HAT patients might be induced by molecular mimicry with a parasite antigen.