Inactivation of a gene for a fibronectin-binding protein of the oral bacterium Streptococcus mutans partially impairs its adherence to fibronectin.

A sequence of 1647 base pairs in length of Streptococcus mutans DNA that encodes for a 63-kDa protein with significant amino acid similarity with fibronectin-binding proteins of Streptococcus pyogenes and Streptococcus gordonii was cloned. The putative recombinant fibronectin-binding protein of S. mutans was purified using affinity chromatography and the cloned protein was used to prepare polyclonal antibodies against the recombinant protein. In immunoblot assays, antibodies against the S. pyogenes fibronectin-binding protein, FBP54, were cross-reactive with the S. mutans protein that was designated SmFnB. Additionally, antibodies to the S. mutans SmFnB protein reacted with the S. pyogenes FBP54 protein. The S. mutans SmFnB protein was found to bind to immobilized fibronectin in a concentration dependant manner. A mutant strain of S. mutans M51 that was constructed by allelic exchange did not express the SmFnB protein. This mutant strain, S. mutans DeltaSmFnB, was determined in an ELISA to bind to immobilized fibronectin 30% less when compared to the parental strain S. mutans M51. The results are consistent with the conclusion that the 63-kDa SmFnB protein of S. mutans is a fibronectin-binding protein that may contribute to the interaction of S. mutans with damaged heart tissue during pathogenesis of infective endocarditis. Also, the study suggests that multiple molecules may mediate the interaction of S. mutans with fibronectin.