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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.

Adherence, coaggregation, and hydrophobicity of Streptococcus gordonii associated with expression of cell surface lipoproteins