Adherence of Actinomyces pyogenes to HeLa cells mediated by hydrophobic surface proteins.
Determination of cell-surface hydrophobicity of Actinomyces pyogenes by hydrophobic interaction chromatography on phenyl-Sepharose revealed that all 42 cultures examined were strongly hydrophobic. The hydrophobic surface proteins were solubilized by mutanolysin treatment of the bacteria and isolated by hydrophobic interaction chromatography. In SDS-PAGE, they appeared with numerous protein bands and blocked the adhesion of whole bacterial cells to the gel matrix. The A. pyogenes cultures attached to HeLa cells in varying degrees. This attachment of A. pyogenes was greatly reduced in the presence of isolated hydrophobic proteins and in the presence of specific antibodies produced against hydrophobic surface proteins. The results of the present study demonstrate that hydrophobic surface proteins promote the capacity of A. pyogenes to adhere to HeLa cells.
Ding
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Institut für Bakteriologie und Immunologie, Justus-Liebig-Universität Giessen, Germany.
Lämmler
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Seleim
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RS
D000190:Actinomyces / Q000737:chemistry / Q000502:physiology*; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000737:chemistry*; D002850:Chromatography, Gel; D006367:HeLa Cells / Q000382:microbiology; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D012685:Sepharose / Q000031:analogs & derivatives
D001426:Bacterial Proteins; D008565:Membrane Proteins; C020927:phenyl-sepharose; D012685:Sepharose