GYPA (Glycophorin A) antibodies are specialized immunoglobulins targeting the glycophorin A protein, a key component of human erythrocyte membranes. Glycophorin A, encoded by the GYPA gene, is critical for maintaining red blood cell structure, presenting MN blood group antigens, and serving as a receptor for pathogens like Plasmodium falciparum and influenza viruses . GYPA antibodies are widely used in transfusion medicine, hematology research, and diagnostic assays to detect or block this protein.
Glycophorin A is a 151-amino acid sialoglycoprotein with:
N-terminal extracellular domain: Heavily glycosylated with O-linked sialic acids, responsible for blood group M/N antigenicity .
Transmembrane domain: Anchors the protein to the erythrocyte membrane .
C-terminal cytoplasmic domain: Interacts with cytoskeletal proteins like ankyrin .
The GYPA gene is located on chromosome 4q31, sharing ~97% homology with GYPB and GYPE genes, which encode related glycophorins . Variants like Miltenberger and Dantu complexes arise from recombination between these genes .
Specificity: Most antibodies target the extracellular N-terminal domain, distinguishing GPA from glycophorin B .
Conjugation: Available in unconjugated (e.g., 6A7M ) or labeled forms (e.g., PE ).
SUMI (MNS50): A low-frequency antigen caused by GYPA p.Thr31Pro, detected via anti-SUMI mAbs .
GP.Mur Homozygotes: Lack normal GPB, leading to anti-U/JENU antibodies detectable via GYPA-negative screening .
A 2023 study used GYPA antibodies to map spatial heterogeneities on reconstituted lipid bilayers. The HIR2 clone revealed GYPA’s height (~12 nm), demonstrating how crowding impacts epitope accessibility. For example, CD45’s C363 epitope (higher) was less affected than I3 (lower), highlighting GPA’s role in modulating receptor interactions .
Monoclonal antibodies 1A9 and 1G7 agglutinate erythrocytes via GPA binding, enabling rapid plasma separation. This method avoids centrifugation, critical for point-of-care diagnostics in low-resource areas .
Hemolytic Anemia: Anti-GPA antibodies aid in diagnosing GPA-related disorders .
Transfusion Compatibility: Polyclonal antibodies detect GPA variants (e.g., Miltenberger) to prevent adverse reactions .
Glycophorin A (GPA) is a significant sialoglycoprotein found on the surface of human red blood cells (erythrocytes). It plays a crucial role in the MNS blood group system, which includes the M and N antigens. The mouse anti-human antibody targeting Glycophorin A is widely used in research and clinical diagnostics to study erythrocyte-related disorders and blood group antigens.
Glycophorin A is a type I transmembrane protein with a molecular weight of approximately 10 kDa . It is composed of 151 amino acids and exists as a homodimer in the cell membrane . The protein is heavily glycosylated, with numerous sialic acid residues contributing to its negative charge. This negative charge is essential for preventing red blood cells from sticking together and to the blood vessel walls.
Glycophorin A carries the antigenic determinants for the MNS blood group system. The M and N antigens are determined by the amino acid sequence at positions 1 and 5 of the protein. Specifically, the M antigen has serine and glycine at these positions, while the N antigen has leucine and glutamic acid .
Glycophorin A is not only important for blood group antigenicity but also plays a role in pathogen interactions. It serves as a receptor for various pathogens, including the malaria parasite Plasmodium falciparum, which binds to Glycophorin A during the invasion of red blood cells . Additionally, some viruses, such as the influenza virus and hepatitis A virus, also utilize Glycophorin A as a binding site .
The mouse anti-human Glycophorin A antibody is a monoclonal antibody that specifically binds to the Glycophorin A protein on human erythrocytes. This antibody can recognize both the M and N types of Glycophorin A, making it a valuable tool for various applications in research and diagnostics .