title: Adherence of Ureaplasma urealyticum to human erythrocytes.
abstract: Ureaplasma urealyticum (four serotypes and two clinical isolates) were metabolically labeled with radioactive methionine to a high specific activity. Labeling allowed the study of the mechanism of adherence to human erythrocytes. The adherence mechanism was complex and partially mediated by proteinaceous surface components. The binding sites on the erythrocytes were partially sensitive to neuraminidase treatment, and adherence was inhibited by glycophorin and dextran sulfate, indicating recognition of sialyl residues and sulfated compounds.
authors.affiliation: Department of Membrane and Ultrastructure Research, Hebrew University-Hadassah Medical School, Jerusalem, Israel.
authors.forename: A B
authors.initials: AB
authors.lastname: Saada
authors.forename: Y
authors.initials: Y
authors.lastname: Terespolski
authors.forename: A
authors.initials: A
authors.lastname: Adoni
authors.forename: I
authors.initials: I
authors.lastname: Kahane
mesh_terms: D001422:Bacterial Adhesion; D004912:Erythrocytes / Q000382:microbiology*; D006801:Humans; D066298:In Vitro Techniques; D019158:N-Acetylneuraminic Acid; D012794:Sialic Acids / Q000502:physiology; D014508:Urea / Q000494:pharmacology; D014509:Ureaplasma / Q000472:pathogenicity / Q000502:physiology*
chemical_list: D012794:Sialic Acids; D014508:Urea; D019158:N-Acetylneuraminic Acid