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α2,3‐Specific Desialylation of Human Red Cells: Effect on the Autoantigens of the Pr, Sa and Sia‐I1, ‐b1, ‐Ib1 Series
Author(s) -
Roelcke D.,
Hack H.,
Kreft H.,
Gross H. J.
Publication year - 1998
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1046/j.1423-0410.1998.7420109.x
Subject(s) - antigen , sialic acid , recombinant dna , glycan , epitope , sialidase , glycophorin , chemistry , red cell , microbiology and biotechnology , glycoprotein , biochemistry , neuraminidase , biology , immunology , medicine , enzyme , gene
Background and objectives : Pr 1,2,3, Pr M , Sa and Sia‐11, ‐b1, ‐1b1 are sialic acid (Neu N Ac)‐dependent antigens recognized by human cold agglutinins. Pr and Sa antigens are the O‐glycans of glycophorins containing α2,3Neu N Ac (to galactose) and/or α2,6Neu N Ac (to galactosamine). The antigens of the Sia‐11, ‐b1, ‐1b1 complex are gangliosides that may carry α2,3Neu N Ac (to galactose) and/or α2,8Neu N Ac (to Neu N Ac). We studied the Neu N Ac groups involved in the antigens. Materials and methods : From 74 sera with cold agglutinins against Neu N Ac‐dependent antigens, anti‐T‐free preparations were made and tested against human red cells, treated with an α2,3‐specific recombinant sialidase. Results : Most (51/62) Pr antigens use α2,3Neu N Ac, some (8/62) use α2,6Neu N Ac and a few (3/62) use both sialyl groups as immunodominant components on glycophorins. The immunodominant component of Sa and Sia‐11, ‐b1, ‐1b1 determinants was α2,3Neu N Ac in all cases. Conclusion : The red cell target structures for cold agglutinins against Neu N Ac‐dependent antigens have been identified. We propose a Pr nomenclature to reflect this. The binding of anti‐Pr to gangliosides may be the basis for anti‐Pr‐induced peripheral neuropathy.