Copyright C 1991, American Society for Microbiology Adherence of Ureaplasma urealyticum to Human Erythrocytes

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. The ability to adhere is a prerequisite for pathogenesis by many microorganisms (2). The adherence mechanisms of a number of mycoplasmas, particularly that of Mycoplasma pneumoniae, have been extensively investigated (1, 5-9, 11-13, 15). It has been shown that the adherence of M. pneumoniae to both respiratory cells and erythrocytes uti-lizes similar mechanisms. For example, M. pneumoniae proteinaceous components mediate adherence to neuramini-dase-sensitive regions on both respiratory epithelium an