Anti-Pr cold agglutinins recognize immunodominant α2,3- or α2,6-sialyl groups on glycophorins

Autor: Kewitz, S., Groß, H., Kosa, R., Roelcke, D.
Zdroj: Glycoconjugate Journal; October 1995, Vol. 12 Issue: 5 p714-720, 7p
Abstrakt: Anti-Pr cold agglutinins (CAs) with the subspecificities anti-Pr1h,-Pr1d, -Pr2, -Pr3h, -Pr3d, -PrMand anti-Sa CAs recognize immunodominantN-acetylneuraminic acid (NeuNAc) groups of tetra and/or trisaccharides (O-glycans) of glycophorin. These O-glycans are sialylated in α2,3- and/or α2,6-linkages. Sa and most Pr antigens have been inactivated by α2,3-specific sialidases. Antigenicity was reconstituted on desialylated glycophorin by α2,3-specific Galβ1,3GalNAc-sialyltransferase indicating that α2,3-linked NeuNAc groups are the immunodominant components of Sa and most Pr antigens. Some Pr antigens were resistant to α2,3-specific sialidase and were not reconstituted by α2,3-specific Galβ1,3GalNAc-sialyltransferase, which indicates that α2,6-linked NeuNAc group represents an immunodominant component of some Pr antigens.
Databáze: Supplemental Index