Immune lysis of lipid vesicles containing myelin basic protein or glycolipid antigens by multiple sclerosis and normal sera.

We have compared the reactivity of sera from 34 multiple sclerosis (MS) patients and 32 normal (N) individuals with lipid vesicles containing myelin basic protein (BP) and several glycolipids reconstituted into a membrane environment. The ability of the sera to cause complement-mediated lysis of lipid vesicles containing these antigens was determined by measuring the release of a water-soluble spin label, tempocholine chloride, from the height of its electron spin resonance spectrum. Only 4 MS sera caused lysis of BP-containing vesicles which was comparable to that produced by specific antibody to BP. A number of both MS and N sera caused significant lysis of vesicles containing GM1 ganglioside or digalactosyldiglyceride. A few MS and N sera also caused significant lysis of vesicles containing GM2, GT1 and GD1a gangliosides. However, in no case was there a statistically significant difference between the mean lysis produced by MS and N sera. There was some overlap between the specific MS and N sera reactive to vesicles containing BP, GM1, GM2, and DGDG while a completely different group of MS and N sera were reactive to GT1 and GD1a gangliosides. This suggested that there was either antigenic cross reactivity between the two groups of glycolipids or two different origins of the immune response to the two groups of antigens. It was concluded that antibody-dependent complement fixation by these particular antigens, in the kind of lipid environment used, is not characteristic of or specific to MS.