Autoantibodies to GM1 ganglioside: different reactivity to GM1-liposomes in amyotrophic lateral sclerosis and lower motor neuron disorders

J Neurol Sci. 1991 Aug;104(2):209-14. doi: 10.1016/0022-510x(91)90312-u.


We studied the ability of anti-GM1 ganglioside antibodies to bind to GM1 in a lipid, "membrane-like" environment. Liposomes containing GM1 were synthesized to simulate this environment. We then compared the binding of anti-GM1 a autoantibodies to GM-1-liposomes and to purified GM1. Antibody binding was quantitated using enzyme-linked immunosorbent assay methodology. Our results showed a 250-fold variation in the ability of anti-GM1 antibodies to bind to GM1-liposomes. There was no correlation between GM-1-liposome binding and the carbohydrate specificities of the anti-GM1 antibodies. However, anti-GM1 antibodies from patients with amyotrophic lateral sclerosis (ALS) showed a 4 fold greater binding to GM1-liposomes than antibodies from patients with lower motor neuron (LMN) syndromes. We conclude that a lipid, presumably "membrane-like", environment may greatly influence the degree of anti-GM1 antibody binding to GM1. The low levels of anti-GM1 antibody binding to GM1-liposomes in patients with LMN syndromes may provide a diagnostic means for distinguishing these patients from those with ALS. Anti-GM1 antibodies from patients with ALS may bind especially well to neuronal membranes containing GM1 in vivo.

Publication types

  • Comparative Study

MeSH terms

  • Amyotrophic Lateral Sclerosis / blood
  • Amyotrophic Lateral Sclerosis / immunology*
  • Autoantibodies / analysis*
  • Chromatography, High Pressure Liquid
  • Enzyme-Linked Immunosorbent Assay
  • G(M1) Ganglioside / immunology*
  • Humans
  • Immunoglobulin M / analysis
  • Liposomes
  • Motor Neuron Disease / blood
  • Motor Neuron Disease / immunology*


  • Autoantibodies
  • Immunoglobulin M
  • Liposomes
  • G(M1) Ganglioside