Monoclonal antibody R24 distinguishes between different N-acetyl- and N-glycolylneuraminic acid derivatives of ganglioside GD3 Journal Article


Authors: Tai, T.; Kawashima, I.; Furukawa, K.; Lloyd, K. O.
Article Title: Monoclonal antibody R24 distinguishes between different N-acetyl- and N-glycolylneuraminic acid derivatives of ganglioside GD3
Abstract: Monoclonal antibody (MAb) R24 was previously shown to be directed toward ganglioside GD3 [Pukel, C. S., Lloyd, K. O., Travassos, L. R., Dippold, W. G., Oettgen, H. F., and Old, L. J. (1982) J. Exp. Med. 155, 1133-1147]. The structural specificity of the MAb has now been further characterized based on binding to structurally related glycolipids, including four GD3 derivatives with different N-acetylneuraminic acid (NeuAc) and N-glycolylneuraminic acid (NeuGc) substituents. Three assay systems (enzyme immunostaining on thin-layer chromatography, enzyme-linked immunosorbent assay, and immune adherence inhibition assay) were used. MAb R24 was found to react with (NeuAc-NeuAc-)GD3 and (NeuAc-NeuGc-)GD3 but not with (NeuGc-NeuAc-)GD3 or (NeuGc-NeuGc-)GD3. These results clearly indicate that the outer sialic acid (Sia) moiety of GD3 is crucial and must be a NeuAc residue, while the inner sialic acid is less involved in binding to the MAb and can be either NeuAc or NeuGc. The MAb was also found to cross-react weakly with two gangliosides, GT1a and GQ1b, but none of other gangliosides nor neutral glycolipids tested reacted. These findings suggest that the epitope detected by MAb R24 is the trisaccharide structure NeuAcα2→8Siaα2→3Gal-, which must be in a terminal position. © 1988.
Keywords: immunohistochemistry; animal cell; animal; mice; enzyme linked immunosorbent assay; monoclonal antibody; antibodies, monoclonal; brain; cattle; sialic acids; glycolipids; epitopes; gangliosides; ganglioside; antigen-antibody reactions; sialic acid; chromatography, thin layer; human; n-acetylneuraminic acid; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; leukocyte adherence inhibition test
Journal Title: Archives of Biochemistry and Biophysics
Volume: 260
Issue: 1
ISSN: 0003-9861
Publisher: Elsevier Inc.  
Date Published: 1988-01-01
Start Page: 51
End Page: 55
Language: English
DOI: 10.1016/0003-9861(88)90423-7
PUBMED: 2449128
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 6 August 2020 -- Source: Scopus
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  1. Kenneth O Lloyd
    163 Lloyd