Abstract
A lectin-like substance (EcLS) was purified from the Eikenella corrodens 1073 cell and monoclonal antibodies were produced against it to confirm the role of EcLS in adhesive properties of E. corrodens such as hemagglutination and coaggregation with oral bacteria. Four hybridoma clones were selected. Two of the antibodies were of the IgG1 isotype and the others were of the IgG2b isotype. These monoclonal antibodies inhibited both the hemagglutination of E. corrodens and the coaggregation with Actinomyces viscosus or Streptococcus sanguis. The reactivity of the monoclonal antibody to E. corrodens 1073 was significantly higher than that to E. corrodens 1080 of which adhesive activity was weaker than that of E. corrodens 1073. These findings suggest the difference in adhesive properties is due to the difference in the amount of EcLS expressed on the cell surface. The immunoelectron microscopic study revealed that EcLS of E. corrodens 1073 was localized in the outer space of outer membrane, not in cell surface appendages such as fimbriae where bacteria possessed adhesin. These results suggest that coaggregation of E. corrodens with A. viscosus or S. sanguis was mediated by EcLS.
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