α2,3-Specific Desialylation of Human Red Cells: Effect on the Autoantigens of the Pr, Sa and Sia-l1, -b1, -lb1 Series

Background and objectives: Pr1, 2, 3, PrM, Sa and Sia-l1, -b1, -lb1 are sialic acid (NeuNAc)-dependent antigens recognized by human cold agglutinins. Pr and Sa antigens are the O-glycans of glycophorins containing α2,3NeuNAc (to galactose) and/or α2,6NeuNAc (to galactosamine). The antigens of the Sia-l1, -b1, -lb1 complex are gangliosides that may carry α2,3NeuNAc (to galactose) and/or α2,8NeuNAc (to NeuNAc). We studied the NeuNAc groups involved in the antigens. Materials and methods: From 74 sera with cold agglutinins against NeuNAc-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 α2,3NeuNAc, some (8/62) use α2,6NeuNAc and a few (3/62) use both sialyl groups as immunodominant components on glycophorins. The immunodominant component of Sa and Sia-l1, -b1, -lb1 determinants was α2,3NeuNAc in all cases. Conclusion: The red cell target structures for cold agglutinins against NeuNAc-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.

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