The panagglutination phenomenon described by Thomsen and Friedenreich(TF) is due to the reaction of naturally occurring TF-antibodies with the carbohydrate groupβ-D-Gal-(1-3)-D-Ga1NAc of desialylated glycophorin A, the major glycoprotein component of the erythrocyte membrane. The specificity of human TF-antibodies reacting with this disaccharide was investigated by hemagglutination inhibition assay and radioimmunoassay using various synthetic oligosaccharides and neoglycoproteins as well as asialoglycophorin A. The results indicate that TF-antibodies represent a heterogeneous mixture of carbohydrate-specific antibodies. The disaccharide β-D-Gal-(l-3)-D-Ga1NAc is the common structure recognized by all TF-antibodies. However, the conjugation mode of the carbohydrate to the carrier protein is important for defining the specificity of different subpopulations of TF-antibodies. The immunological reaction depends on the configuration of the glycosidical linkage as well as on the chemical nature of the aglycon, which is coupled to the disaccharide. These findings suggest that the heterogeneity of natural TFantigens is due to the wide distribution of the carbohydrate structure β-D-Gal-(1-3)-D-Ga1NAc. The characterization of TF- or TF-like antibodies directed to particular natural TF-antigens (e.g. asialoglycophorin A, tumor TF-antigens, glycolipids, bacterial antigens)requires TF-analogues, which contain the additional molecular regions together with the TF-disaccharide. These structures, apart from the TF-hapten, are obviously important for defining the immunodeterminant group of TF-antigens of different origin.

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