PMID: 8595264Oct 1, 1995Paper

Anti-Pr cold agglutinins recognize immunodominant alpha 2,3- or alpha 2,6-sialyl groups on glycophorins

Glycoconjugate Journal
S KewitzD Roelcke

Abstract

Anti-Pr agglutinins (CAs) with the subspecificities anti-Pr1h, -Pr1d, -Pr2, -Pr3h, -Pr3d, -PrM and anti-Sa CAs recognize immunodominant N-acetylneuraminic acid (NeuN Ac) groups of tetra and/or trisaccharides (O-glycans) of glycophorin. These O-glycans are sialylated in alpha 2,3- and/or alpha 2,6-linkages. Sa and most Pr antigens have been inactivated by alpha 2,3-specific sialidases. Antigenicity was reconstituted on desialylated glycophorin by alpha 2,3-specific Gal beta 1,3GalN Ac-sialyltransferase indicating that alpha 2,3-linked NeuN Ac groups are the immunodominant components of Sa and most Pr antigens. Some Pr antigens were resistant to alpha 2,3-specific sialidase and were not reconstituted by alpha 2,3-specific Gal beta 1,3GalN Ac-sialyltransferase, which indicates that alpha 2,6-linked NeuN Ac group represents an immunodominant component of some Pr antigens.

References

Jun 1, 1992·Annals of Hematology·A L KönigD Roelcke
Apr 1, 1989·Transfusion Medicine Reviews·D Roelcke
Nov 15, 1988·European Journal of Biochemistry·H J Gross, R Brossmer
Nov 2, 1987·European Journal of Biochemistry·H J GrossR Brossmer
Apr 1, 1973·European Journal of Immunology·D Roelcke
Jan 1, 1974·Vox Sanguinis·D RoelckeD J Anstee
May 1, 1984·Transfusion·D Roelcke, H Kreft
Jan 1, 1986·Advances in Space Research : the Official Journal of the Committee on Space Research (COSPAR)·A W Schwartz

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