Monoclonal Antibodies Against Glycophorin A

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Abstract
Two mouse IgM monoclonal antibodies, 177.1 and 179.3, are directed against glycophorin A, the major sialoglycoprotein of human erythrocytes. Both antibodies agglutinate blood group M and N erythrocytes equally well, both before and after treatment with neuraminidase or trypsin, but fail to agglutinate erythrocytes treated with papain. Antibody 179.3 agglutinates MiVII(K.T.) cells, whose glycophorin A probably contains some alterations in amino acid sequence between residues 46-56, but antibody 177.1 does not agglutinate these cells. Neither antibody agglutinates En(a-)G.W. cells, which lack glycophorin A completely. The hemagglutinating activity of antibody 177.1 is inhibited by purified glycophorin A and its chymotryptic glycopeptides CH1 (amino acid residues 1-64) and CH3 (amino acid residues 35-64), whereas the hemagglutinating activity of 179.3 is inhibited weakly by glycophorin A but not by chymotryptic peptides. These antibodies both are classified as anti-En(a-)FS but apparently bind different epitopes.