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

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Abstract

Anti-Pr cold agglutinins (CAs) with the subspecificities anti-Pr1h,-Pr1d, -Pr2, -Pr3h, -Pr3d, -PrM and anti-Sa CAs recognize immunodominantN-acetylneuraminic acid (NeuN Ac) 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 Galβ1,3GalN Ac-sialyltransferase indicating that α2,3-linked NeuN Ac 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 Galβ1,3GalN Ac-sialyltransferase, which indicates that α2,6-linked NeuN Ac group represents an immunodominant component of some Pr antigens.

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Authors and Affiliations

  1. Institute for Immunology, University of Heidelberg, Im Neuenheimer Feld 305, 69120, Heidelberg, Germany

    S. Kewitz, R. Kosa & D. Roelcke

  2. Institute for Biochemistry II, University of Heidelberg, Im Neuenheimer Feld 328, 69120, Heidelberg, Germany

    H. J. Groß

Authors
  1. S. Kewitz
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  2. H. J. Groß
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  3. R. Kosa
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  4. D. Roelcke
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Kewitz, S., Groß, H.J., Kosa, R. et al. Anti-Pr cold agglutinins recognize immunodominant α2,3- or α2,6-sialyl groups on glycophorins. Glycoconjugate J 12, 714–720 (1995). https://doi.org/10.1007/BF00731269

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  • DOI: https://doi.org/10.1007/BF00731269

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