Hydrophobic characterization of thermophilic Campylobacter species and adhesion to INT 407 cell membranes and fibronectin.
Cell surface hydrophobicity of Campylobacter jejuni, C. coli, C. lari and C. upsaliensis was tested by hydrophobic interaction chromatography on octylsepharose CL-4B. The hydrophobicity was influenced by cultivation mode, presence or absence of intact lipopolysaccharide (LPS) and outer membrane protein structures. Species-specific differences of hydrophobic characteristics were not detected. Bacteria grown in fluid medium exhibited a high degree of hydrophobicity. Agar-grown bacteria showed hydrophobic interaction to a significant lower extent. By oxidation of LPS with sodium meta-periodate the hydrophobicity of agar-grown bacteria was slightly increased. Bacteria pretreated with proteinase K exhibited a marked decrease of hydrophobic interaction, whereas pretreatment with trypsin did not influence the hydrophobic interaction. Live bacteria were allowed to adhere to INT 407 cell membranes. With exception of one aflagellate strain, bacteria grown in fluid medium adhered better to the cellular substrate than agar-grown bacteria. This difference was not found when adhesion to fibronectin was tested. LPS-oxidized bacteria adhered significantly better to both cell membranes and fibronectin, whereas proteinase K treated bacteria exhibited a significant loss of adhesion capacity for both substrates.
Moser
I
I
Institut für Mikrobiologie und Tierseuchen, Freie Universität Berlin, Germany.
Schröder
W
W
D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D002167:Campylobacter / Q000254:growth & development / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002478:Cells, Cultured; D002847:Chromatography, Agarose; D003470:Culture Media / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D019286:Endopeptidase K / Q000494:pharmacology; D005353:Fibronectins / Q000378:metabolism; D006801:Humans; D008070:Lipopolysaccharides / Q000378:metabolism; D010084:Oxidation-Reduction; D010504:Periodic Acid / Q000494:pharmacology; D013045:Species Specificity; D014357:Trypsin / Q000494:pharmacology; D014867:Water / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D003470:Culture Media; D005353:Fibronectins; D008070:Lipopolysaccharides; D014867:Water; D010504:Periodic Acid; C009288:metaperiodate; D014357:Trypsin; D019286:Endopeptidase K