Adhesion of mycoplasmas to eukaryotic cells

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Updated: Oct 7, 2026

In Vitro Assay of Bacterial Adhesion onto Mammalian Epithelial Cells
05:57

In Vitro Assay of Bacterial Adhesion onto Mammalian Epithelial Cells

Published on: May 16, 2011

S Razin, I Kahane, M Banai

    Ciba Foundation Symposium
    |January 1, 1981
    PubMed

    Insights

    Pathogenic mycoplasmas adhere to host cells via specialized attachment structures. Researchers identified specific proteins on Mycoplasma pneumoniae responsible for binding to host cell receptors like glycophorin.

    Area of Science:

    • Microbiology
    • Cell Biology
    • Biochemistry

    Background:

    • Pathogenic mycoplasmas are surface parasites lacking cell walls, enabling close contact and potential membrane fusion with host cells.
    • Mycoplasma adhesion to host epithelial cells is mediated by specialized tip structures, crucial for colonization of respiratory and urogenital tracts.
    • Previous studies visualized Mycoplasma pneumoniae and Mycoplasma gallisepticum adhering to human red blood cells, highlighting their attachment mechanisms.

    Purpose of the Study:

    • To chemically define the specific host cell receptors and mycoplasma binding sites involved in parasite-host adhesion.
    • To elucidate the molecular interactions underlying the attachment of Mycoplasma pneumoniae to human red blood cells.

    Main Methods:

    • Affinity chromatography using glycophorin-Sepharose to isolate Mycoplasma pneumoniae membrane components with high affinity for glycophorin.
    • Analysis of isolated membrane proteins using techniques to determine their molecular mass and binding characteristics.
    • Inhibition assays using glycophorin and its moieties to confirm the specificity of mycoplasma binding.

    Main Results:

    • Glycophorin identified as a primary receptor for Mycoplasma gallisepticum and one of several receptors for Mycoplasma pneumoniae on human red blood cells.
    • Trypsin treatment of Mycoplasma pneumoniae abolished its attachment to red blood cells, indicating the protein nature of its binding sites.
    • Isolated Mycoplasma pneumoniae membrane fractions containing proteins of 25,000 and 45,000 molecular mass showed specific, albeit low, binding to red blood cells, inhibited by glycophorin.

    Conclusions:

    • Specific protein components of Mycoplasma pneumoniae mediate adhesion to host cell receptors, including glycophorin.
    • The binding sites on Mycoplasma pneumoniae are proteinaceous and their exposure may be influenced by the cell's electrochemical ion gradient.
    • Understanding these molecular interactions is key to developing strategies against mycoplasma infections.

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