Anti-Human/Mouse/Rat Glycophorin A - Purified (G210-GRP)

Glycophorins are transmembrane proteins of red blood cells (RBC)1 . There are four glycophorin encoding genes (A, B, C, and D), and a fifth pseudogene (E), which has no protein product. Glycophorin A, B, and E are tandemly arranged repeats on chromosome 4 and are prone to rearrangements that lead to rare blood groups. Glycophorin A and B carry MN and Ss blood group antigens. Glycophorin A is a type I glycoprotein carrying sialylated O- and N-glycans, and most of the O-glycans are NeuAcα2-3Galβ1-3(NeuAcα2-6)GaINAc-tetrasaccharide chains linked to serine or threonine residues 2 . The abundance of glycophorin A on the surface of RBCs is thought to create a negatively charged cell surface of complex glycans that allows for RBC circulation without sticking to other cells or blood vessel walls1 . Glycophorin A binds CD170 3 (Siglec 5, which mediates sialic-acid dependent binding to cells4), influenza virus, and EBA-175, the erythrocyte binding antigen of Plasmodium falciparum, the parasite responsible for malaria in Africa 2 . Babesia divergens, which like Plasmodium is a parasite in the Apicomplexa phylum, also uses glycophorins A and B to enter RBCs. Other pathogens that bind to glycophorin A on the surface of RBCs include: some strains of Escherichia coli, reoviruses (a group of viruses that includes rotavirus), encephalomyocarditis virus, and hepatitis A 2 . Glycophorin A also interacts with influenza virus but because influenza virus cannot replicate in anucleated RBCs glycophorin A might be acting as a decoy receptor to divert infection away from other tissues. JC159 was generated using splenic hairy cell leukemia cells as immunogen and reacts with a formalin-fixed, paraffin-embedded resistant epitope, likely between amino acids 27 and 40, on the extracellular domain5.