Abstract:
:The panagglutination phenomenon described by Thomsen and Friedenreich (TF) is due to the reaction of naturally occurring TF-antibodies with the carbohydrate group beta-D-Gal-(1-3)-D-GalNAc 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 beta-D-Gal-(1-3)-D-GalNAc 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 TF-antigens is due to the wide distribution of the carbohydrate structure beta-D-Gal-(1-3)-D-GalNAc. 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.
journal_name
Vox Sangjournal_title
Vox sanguinisauthors
Höppner W,Fischer K,Poschmann A,Paulsen Hdoi
10.1111/j.1423-0410.1985.tb00179.xsubject
Has Abstractpub_date
1985-01-01 00:00:00pages
246-53issue
4eissn
0042-9007issn
1423-0410journal_volume
48pub_type
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