A novel series of anti-human glycophorin A (CD235a) antibodies defining five extra- and intracellular epitopes

Glycophorin A (GPA, CD235a) is a major membrane glycoprotein and marker of cells of the erythroid lineage. It is also the target of Plasmodium falciparum and of influenza virus. We describe a novel series of 10 antibodies towards GPA, recognizing four extra- and intracellular peptide epitopes of this molecule (defined by epitope mapping) and one mixed peptide/carbohydrate epitope. All antibodies bind better to the desialylated than to the fully sialylated molecule, including those specific for the intracellular epitope. For some of the antibodies (representing all five epitopes) functional binding constants were determined by Surface Plasmon Resonance. The new panel complements the already known anti-glycophorin antibodies and offers several potential applications for, e.g., differential diagnosis of erythroleukemias, lineage analyses of erythroid cells, isolation of senescent erythrocytes, or a highly sensitive neuraminidase assay.

Research Highlights
► Nine novel antibodies to human glycophorin A defining five epitopes (A–E) are described.
► Binding ratios towards sialylated vs non-sialylated GPA and functional binding constants are given.
► Antibody A63-C/A9 detects a mixed epitope (core-1 on GPA) which is very special and useful for a highly sensitive sialidase assay.