Identification of a 100-kilodalton putative coaggregation-mediating adhesin of Streptococcus gordonii DL1 (Challis).

Streptococcus gordonii DL1 (Challis) bears coaggregation-relevant surface proteins which mediate lactose-inhibitable coaggregations with other streptococci. Six spontaneously occurring coaggregation-defective (Cog-) mutants of wild-type strain S. gordonii DL1 unable to coaggregate with wild-type streptococcal partners were characterized. Antiserum raised against wild-type cells and absorbed with Cog- cells specifically blocked lactose-inhibitable coaggregations between S. gordonii DL1 and its streptococcal partner strains; it did not block lactose-noninhibitable coaggregations with actinomyces partners. Surface proteins were released from the cells by mild sonication treatment and separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A 100-kDa surface protein from S. gordonii DL1 was identified by immunoblot analysis with the mutant-absorbed antiserum. Each of the six Cog- mutants lacked the 100-kDa protein. Several other oral viridans streptococci that exhibit intrageneric lactose-inhibitable coaggregations expressed an immunoreactive protein with about the same size as the 100-kDa putative adhesin. It is proposed that the 100-kDa protein is the adhesin which mediates coaggregation between S. gordonii DL1 and its streptococcal partners. The role of this putative adhesin in accretion of streptococci in early colonization of the tooth surface is discussed.