Recombinant Human GYPA

Background

Glycophorin A (GYPA) is a major sialoglycoprotein found on the membrane of human red blood cells (RBCs) and plays a crucial role in the structure and function of the erythrocyte membrane. As a prominent surface protein, it is highly glycosylated and carries sialic acid residues, which contribute to the overall negative charge on the RBC surface, helping to prevent cell aggregation and maintain blood flow. GYPA is most recognized for its involvement in the MNS blood group system, which includes the MN and Ss antigens; variations in the GYPA gene form the molecular basis for these antigenic determinants. This protein is highly relevant in transfusion medicine due to its immunogenic potential and role in blood group antigenicity. In addition to its structural role, GYPA interacts with various pathogens, particularly Plasmodium falciparum, the causative agent of malaria. This interaction is significant for the pathogen’s adhesion to RBCs during infection. GYPA also functions as a receptor for viruses like influenza, playing a broader role in infectious disease dynamics.