Abstract
Summary Cell surface hydrophobicity of Mycoplasma hyopneumoniae was evaluated by phase partitioning in a hydro-carbon-aqueous mixture, by hydrophobic interaction chromatography, and by salting out with ammonium sulfate. Results obtained by use of these techniques gave evidence that the cell surface of M hyopneumoniae is weakly hydrophobic, compared with strongly hydrophobic Staphylococcus aureus Cowan I and hydrophilic Klebsiella pneumoniae. After treatment of the organisms with trypsin, M hyopneumoniae became less hydrophobic as measured by hydrophobic interaction chromatography. Significant changes in hydrophobicity were not seen after periodate treatment. Electron microscopy of M hyopneumoniae treated with polycationic ferritin revealed an intermediate, compact, unlabeled layer between the cytoplasmic membrane and an external, heavily labeled layer. Electron microscopy of ferritin-labeled M hyopneu-moniae after treatment with trypsin or periodate revealed the intermediate layer to be composed of a trypsin-sensitive protein(s). The outer layer was made of periodate-sensitive carbohydrate(s). Therefore, it appears that proteins in the intermediate layer confer at least part of the total hydrophobicity of the mycoplasmal cell and may contribute to adherence of M hyopneumoniae to target respiratory cells by hydrophobic interactions.
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