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. 1988 Apr 1;251(1):17–22. doi: 10.1042/bj2510017

Characterization of the binding epitope of a monoclonal antibody to sulphatide.

P Fredman 1, L Mattsson 1, K Andersson 1, P Davidsson 1, I Ishizuka 1, S Jeansson 1, J E Månsson 1, L Svennerholm 1
PMCID: PMC1148958  PMID: 2455508

Abstract

An IgG1 monoclonal antibody, Sulph I, reacting with sulphatide (3'-sulphogalactosylceramide), was produced by immunizing Balb/c mice with that glycolipid coated on Salmonella minnesota bacterial membrane. Radioimmunodetection of the binding of the monoclonal antibody to structurally related glycolipids adsorbed to microtitre plates or chromatographed on thin-layer plates was used to determine its binding epitope. The antibody showed similar binding avidity to three sulphated glycolipids: sulphatide, sulpholactosylceramide and seminolipid. Lysosulphatide did bind the antibody, but, compared with sulphatide, 30 times more antigen was needed for half-maximal binding. Bis(sulphogangliotriosyl)ceramide and bis-sulphogangliotetraosylceramide did not bind the antibody. These results suggest that terminal galactose-3-O-sulphate and part of the hydrophobic region of the glycolipid are recognized by the Sulph I antibody.

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Selected References

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