Identification of a human erythrocyte receptor for colonization factor antigen I pili expressed by H10407 enterotoxigenic Escherichia coli.
We have identified a receptor for colonization factor antigen I (CFA/I) pili in human erythrocyte membranes. Erythrocyte binding assays, using whole organisms, suggested that the CFA/I receptor was a glycoprotein containing important sialic acid moieties. Subsequently, human erythrocyte membranes were extracted with lithium diiodosalicylate to obtain a soluble glycoprotein fraction from which to isolate receptors. The extracted material caused agglutination of the CFA/I+ but not the CFA/I- organisms at a protein concentration of 0.5 mg/ml. The CFA/I receptor was identified in iodinated extract by an affinity isolation procedure, using whole bacterial cells. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography of the washed, extract-coated H10407 CFA/I+ organisms revealed a band with an apparent molecular weight of 26,000 which was present in the original extract but was not observed on extract-coated H10407 CFA/I- bacteria. The addition of purified CFA/I pili reduced binding of the 26,000-molecular-weight receptor to CFA/I+ bacteria. The CFA/I-specific receptor species also bound to wheat germ agglutinin-agarose. This observation supported the suggestion that the CFA/I receptor identified in this report is a sialoglycoprotein.
D000942:Antigens, Bacterial / Q000378:metabolism*; D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D001667:Binding, Competitive; D002846:Chromatography, Affinity; D004910:Erythrocyte Membrane / Q000382:microbiology*; D004926:Escherichia coli / Q000378:metabolism / Q000472:pathogenicity*; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D006801:Humans; D037102:Lectins; D008562:Membrane Glycoproteins / Q000097:blood*; D008970:Molecular Weight; D009439:Neuraminidase / Q000494:pharmacology; D011956:Receptors, Cell Surface / Q000097:blood*; D011971:Receptors, Immunologic / Q000302:isolation & purification*; D014357:Trypsin / Q000494:pharmacology
D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D037102:Lectins; D008562:Membrane Glycoproteins; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic; C047105:bacterial adhesin receptor; C022924:colonization factor antigens; D036781:Fimbriae Proteins; D009439:Neuraminidase; D014357:Trypsin