Specificity and Cross-reactivity of anti-galactocerebroside antibodies Academic Article Article uri icon


MeSH Major

  • Antibodies, Anti-Idiotypic
  • Gangliosides
  • Immunoglobulin M
  • Myelin-Associated Glycoprotein


  • Anti-galactocerebroside (GalC) antibodies have been reported to inhibit myelin formation, cause demyelination, and block HIV-I infection of neural cells. We examined the binding of 3 monoclonal and polyclonal anti-GalC antibodies to a panel of purified glycolipids by ELISA and by an immunospot assay on nitrocellulose blots. All 3 antibodies bound strongly to GM1 ganglioside, monogalactosyl diglyceride, and asialo-GM1, and 2 of the antibodies bound to GD1b and psychosine. The anti-GalC antibodies also bound to 3 glycoprotein bands in human neuroblastoma cells on Western blot, and binding to the proteins was abolished by pre-treatment with pronase or with periodate which oxidizes the terminal carbohydrate residues. These results indicate that anti-GalC antibodies cross react with oligosaccharide determinants of other glycolipids and glycoproteins, and that these cross-reactivities may be responsible for some of the biological effects of the anti-GalC antibodies.

publication date

  • January 1995



  • Academic Article


Digital Object Identifier (DOI)

  • 10.3109/08820139509066860

PubMed ID

  • 7542630

Additional Document Info

start page

  • 595

end page

  • 606


  • 24


  • 4