Abstract
Hydrophobic strains of Streptococcus mutans were compared with paired variants showing reduced hydrophobicity. Extracts of hydrophobic cells contained a number of high-molecular-weight proteins which were not present on cells with decreased hydrophobicity. The proteins were found in purified cell walls, suggesting that they are located on the bacterial surface. Trypsin treatment of whole cells destroyed the proteins and reduced the hydrophobicity. Chemical analysis did not reveal any marked differences in the proportion of cell wall constituents. The amino acid compositions and lipoteichoic acid contents of hydrophobic and hydrophilic cell walls were similar. Culture supernatants from the hydrophilic variants contained high-molecular-weight proteins similar to those extracted from the cell walls of the hydrophobic parent strains, indicating that the variants were impaired in their ability to incorporate the hydrophobicity-associated proteins into the cell wall. The dominant protein had a molecular weight of 190,000, similar to that of antigen I/II (B) of S. mutans.