title: Identification of the major human sialoglycoprotein from red cells, glycophorin AM, as the receptor for Escherichia coli IH 11165 and characterization of the receptor site.
abstract: The pyelonephritogenic Escherichia coli strain 1 H 11165 specifically agglutinates human erythrocytes carrying the M blood group antigen. The polymorphic forms of this antigen, M and N, are located in the NH2-terminal region of the major human red-cell sialoglycoprotein, glycophorin A. Radioactively labeled glycophorin A from M cells specifically bound to the bacteria. Purified glycophorin AM, but not glycophorin AN, efficiently inhibited for binding. Mild periodate treatment oxidized the NH2-terminal serine in glycophorin AM and this resulted in loss of binding to the bacteria. High concentrations of serine and alkali-labile oligosaccharides derived from glycophorin AM inhibited the binding, whereas the synthetic M-specific NH2-terminal pentapeptide Ser-Ser-Thr-Thr-Gly did not. Neuraminidase treatment of glycophorin AM did not destroy the binding. The most efficient inhibition of binding was observed with the N-terminal glyco-octapeptide obtained from glycophorin AM by CNBr cleavage. This peptide contains both the essential serine residue and the alkali-labile oligosaccharides, which both are recognized by the bacterium.
mesh_terms: D000595:Amino Acid Sequence; D004910:Erythrocyte Membrane / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism / Q000382:microbiology*; D004926:Escherichia coli / Q000378:metabolism*; D006021:Glycophorins / Q000138:chemical synthesis / Q000378:metabolism*; D006801:Humans; D008951:MNSs Blood-Group System; D019158:N-Acetylneuraminic Acid; D011946:Receptors, Antigen / Q000378:metabolism*; D012794:Sialic Acids / Q000097:blood; D012795:Sialoglycoproteins / Q000378:metabolism*; D012995:Solubility
chemical_list: D006021:Glycophorins; D008951:MNSs Blood-Group System; D011946:Receptors, Antigen; D012794:Sialic Acids; D012795:Sialoglycoproteins; D019158:N-Acetylneuraminic Acid