Cell surface components of XXXX : relationship to aggregation, adherence, and hydrophobicity.

@entity1133 @entity3208 @entity575 @entity72233 @entity885 @entity692 @entity2975 @entity4673 @entity214
Cell surfaces of aggregation, adherence, and hydrophilic variants of @entity885 were compared with cell surfaces of the parent strain with regard to their protein and antigenic constituents. Cell surface molecules were released by digestion with mutanolysin. Extraction with @entity3208 ( @entity214 ) @entity1133 , @entity72233 , and boiling water did not solubilize any material which stained with @entity4673 in an @entity214 - @entity2975 gel electrophoresis gel. The parent organism @entity885 12, which aggregates in saliva, adheres to saliva-coated @entity692 and is hydrophobic, was found to possess a prominently staining 160,000 molecular weight (MW) protein. This protein was almost completely absent from strain 12na, a hydrophobic nonaggregating variant, and was completely absent from the hydrophilic nonaggregating strain 12L. Trypsinization of strain 12 resulted in the coincident loss of the 160,000-MW protein and the ability to aggregate in saliva. Trypsin treatment reduced but did not eliminate the hydrophobic character of the cells. Boiling destroyed their ability to aggregate, but did not alter their hydrophobicity. Cell wall digests of strain 12 contained a number of proteins which were absent from strains 12na and 12L. Mutanolysin digests of cell walls of the hydrophilic strains contained almost no material that was visible in a @entity575 -stained @entity214 - @entity2975 gel electrophoresis gel. Culture supernatants contained a number of proteins which were immunologically cross-reactive with cell surface proteins. The hydrophilic organisms released a number of 60,000- to 90,000-MW proteins not seen in culture supernatants from the parent strain.
