A possible mechanism for the cellular coaggregation between Actinomyces viscosus ATCC 19246 and Streptococcus sanguis ATCC 10557.

The cells of Actinomyces viscosus ATCC 19246 (Av19246) and Streptococcus sanguis ATCC 10557 (Ss10557) coaggregated immediately after mixing in 40 mM-Tris/HCl buffer. Optimal conditions were pH 7.5 in the presence of Ca2+ at 0.1 mM or higher. Na2 EDTA and its analogues, Na2MgEDTA and Na2MnEDTA at 7.5 mM inhibited the coaggregation. Trypsin and heat treatment impaired the reactive site on Av19246 cells, but not on Ss10557 cells. The coaggregates, once formed, dissociated gradually during extended incubation at 37 degrees C; this was prevented by addition of sufficient Ca2+. The disaggregation appears to be a spontaneous denaturation of the proteinaceous reactive site on Av19246 cell surface. Thus, the coaggregation involves the interaction of a lectin-like substance on the surface of Av19246 with a carbohydrate site on Ss10557. Native Ss10557 cell walls possessed reactivity with Av19246 cells but 5% (w/v) TCA-extracted cell wall residues did not. A carbohydrate moiety extracted from Ss10557 exhibited a high potency in blocking coaggregation, and coaggregates were dissociated upon addition of the carbohydrate. Lactose, galactose and N-acetyl-D-galactosamine (the latter two are major constituents of the antigen extract) also significantly inhibited the coaggregation, but the other antigen components, glucose and rhamnose, did not. Relative inhibitory activity, expressed as molar potency, of carbohydrate antigen, lactose, galactose and N-acetyl-D-galactosamine respectively, was approximately 26 X 10(3):16:4:1. Ss10557 cells and cell walls reacted only with a Ricinus communis (castor bean) agglutinin-120 but not with Glycine max (soybean) agglutinin, Arachis hypogaea (peanut) agglutinin or Phaseolus vulgaris agglutinin (phytohaemagglutinin).(ABSTRACT TRUNCATED AT 250 WORDS)