The interaction of oral streptococci with human fibrinogen was investigated. Streptococcus gordonii was chosen as a representative species to study the binding to fibrinogen. S. gordonii DL1 adhered to immobilized fibrinogen and bovine serum albumin. Binding to immobilized fibrinogen was saturable, concentration and temperature dependent. The binding of S. gordonii DL1 to fibrinogen was inhibited by anti-fibrinogen antibody. Heating of the bacteria for 1 h at 95 degrees C resulted in 90% inhibition of the binding. Trypsin treatment of the bacteria resulted in decreased binding. Neither lipoteichoic acid nor culturing of the bacteria in a sucrose-supplemented medium had any effect on the binding. S. gordonii, Streptococcus sanguinis, Streptococcus mitis, and Streptococcus oralis bound to the immobilized fibrinogen, but mutans streptococci did not. None of the oral streptococci tested bound to the fibrinogen in fluid phase. These results suggest that the binding of S. gordonii DL1 to immobilized fibrinogen is mediated through a specific protein adhesin-receptor interaction, and fibrinogen acts as a cryptitope.

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