Contribution of the complement system to antibody-mediated binding of Trypanosoma gambiense to macrophages.
The role of complement in the process of binding of trypanosomes to macrophages in the presence of specific antibody was studied. The aggregation of trypanosomes observed at the optimal antigen-antibody ratio or in the presence of excess antigen inhibited the binding. Complement caused clumped trypanosomes to dissociate, and the free trypanosomes, which were presumed to be coated with antibody that had fixed complement, readily attached to surfaces of phagocytes. Thus, complement was shown to contribute at the site of the antigen-antibody reaction to the creation of an environment suitable for the binding. It seems likely that the trypanosomes dissociated by complement adhered to C3 receptors of the macrophage. However, in the absence of complement and in regions of antibody excess, free trypanosomes also attached to phagocytes. Thus phagocytes may also have receptors for the Fc portion of aggregated antibody. Complement activated by the alternate pathway also enhanced attachment of trypanosomes to phagocytes, but the effect was not as rapid as it was when complement was activated by classical means.
D000818:Animals; D000906:Antibodies / Q000276:immunology; D000937:Antigen-Antibody Reactions; D000953:Antigens, Protozoan / Q000276:immunology; D003170:Complement Pathway, Alternative; D003171:Complement Pathway, Classical; D003165:Complement System Proteins / Q000276:immunology*; D005260:Female; D008264:Macrophages / Q000276:immunology*; D011817:Rabbits; D014347:Trypanosoma brucei gambiense / Q000276:immunology*
D000906:Antibodies; D000953:Antigens, Protozoan; D003165:Complement System Proteins