Identification of an Erythrocyte Component Carrying the Duffy Blood Group Fy ^a Antigen

Abstract

The erythrocyte component carrying the Duffy blood group antigen Fya has been identified as a 35- to 43-kilodalton protein. The protein is degraded by proteases, chymotrypsin, and Pronase, which destroy its antigenicity on intact erythrocytes. Its unusual property of aggregating on being boiled in 5 percent sodium dodecyl sulfate with 5 percent 2-mercaptoethanol distinguishes it from other erythrocyte membrane proteins described to date.

Blocking of the receptor‐mediated invasion of erythrocytes by Plasmodium knowlesi malaria with sulfated polysaccharides and glycosaminoglycans

“…This is of interest since the analogous receptor protein in Plasmodium falciparum requires sialic acid for binding to the erythrocyte membrane [17]. Although the Duffy blood group antigen also carries sialic acids, these are not the binding groups since neuraminidase treatment, while reducing the electrophoretic mobility of the Duffy antigen [7], does not decrease the 135-kDa polypeptide binding. Therefore, different negatively charged groups or erythrocytes are involved in the binding of the P. knowlesi and P. falciparum erythrocyte receptor molecules.…”

“…1, no inhibitor). Since we had determined that this molecule binds to the Duffy antigen in these erythrocytes [4] and that the Duffy antigen was highly glycosylated [7], we examined whether various monosaccharides, polysaccharides and glycoproteins could inhibit the binding of the 135-kDa polypeptide to human Duffy b erythrocytes. These reagents, added to the reaction mix at a final concentration of 1 mg/ml, included glucose, N-acetylglucosamine, mucin (submaxillary), fibrinogen and fucoidan.…”

Close Association of the First and Fourth Extracellular Domains of the Duffy Antigen/Receptor for Chemokines by a Disulfide Bond Is Required for Ligand Binding

“…It is known that on sodium dodecyl sulfate-polyacrylamide gel electrophoresis the DARC protein migrated as a 37-or 42-kDa species under reducing and nonreducing conditions, respectively, suggesting that cysteine residues of DARC may be involved in intrachain disulfide bond formation (29,33). By analogy with the IL-8 receptors (23,34,35), it is assumed that the extracellular cysteines 51 (or 54) and 276 and cysteines 129 and 197 (numbered on the major DARC polypeptide, see above) might be involved in disulfide bonds between the NH 2 -terminal domain and the third extracellular loop and between the first and second extracellular loops, respectively.…”

Postcapillary venule endothelial cells in kidney express a multispecific chemokine receptor that is structurally and functionally identical to the erythroid isoform, which is the Duffy blood group antigen.

“…The Duffy blood group antigen was first identified serologically as the target of alloantibodies that can cause posttransfusion hemolytic reactions (11). It was subsequently identified and characterized as a 35-43-kD membrane glycoprotein (12,13) which is necessary for the invasion of human erythrocytes by the monkey malaria Plasmodium knowlesi (14) and the human malaria, Plasmodium vivax (15,16). Production of an anti-Duffy monoclonal antibody, anti-Fy6, (17) facilitated the purification and the subsequent cloning of the cDNA for the Duffy antigen receptor for chemokines (DARC) (18,19).…”