title: Adherence, coaggregation, and hydrophobicity of Streptococcus gordonii associated with expression of cell surface lipoproteins.
abstract: Streptococcus gordonii Challis incorporated exogenous [3H]palmitate into 13 polypeptides extractable from intact cells with sodium dodecyl sulfate. A 76-kDa surface-exposed polypeptide, implicated previously as a cell aggregation determinant, was shown to be one of these lipid-modified polypeptides. Differences in sodium dodecyl sulfate-polyacrylamide gel electrophoresis patterns of lipopolypeptides were detected with mutants of S. gordonii that were altered in adherence, aggregation, coaggregation, or hydrophobicity. Lipid-modified polypeptides, tightly associated with the cell membrane, may be involved in the expression of cell surface properties of S. gordonii important for colonization of the human oral cavity.
authors.affiliation: Department of Oral Biology and Oral Pathology, University of Otago, Dunedin, New Zealand.
authors.forename: H F
authors.initials: HF
authors.lastname: Jenkinson
mesh_terms: D000595:Amino Acid Sequence; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000032:analysis*; D001483:Base Sequence; D008074:Lipoproteins / Q000032:analysis* / Q000502:physiology; D008969:Molecular Sequence Data; D009055:Mouth / Q000382:microbiology; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism; D013291:Streptococcus / Q000737:chemistry* / Q000502:physiology
chemical_list: D001426:Bacterial Proteins; D008074:Lipoproteins; D010169:Palmitic Acids; D019308:Palmitic Acid