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Monoclonal antibodies capable of inhibiting coaggregation between Capnocytophaga gingivalis DR2001 and Actinomyces israelii PK16 were used to identify the adhesin on C. gingivalis that mediates the interaction. The monoclonal antibodies were used to demonstrate that a 140-kilodalton polypeptide found in the outer membrane of C. gingivalis was the adhesin responsible for coaggregation. A coaggregation-defective mutant that was unable to coaggregate with A. israelii lacked this large polypeptide. The monoclonal antibodies were also used to estimate the number of binding sites on the surfaces of individual cells and show how the adhesin molecules were arranged on the outer membrane. Values of between 220 and 280 were obtained for the number of adhesin molecules per cell. Immunoelectron microscopy performed with the monoclonal antibodies revealed that the adhesin molecules were arranged nonuniformly on the bacterial surface and occurred singly, in pairs, and in small clusters.

Use of adhesin-specific monoclonal antibodies to identify and localize an adhesin on the surface of Capnocytophaga gingivalis DR2001