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C 3 receptors on human lymphocyte subsets and recruitment of antibody dependent lymphocyte mediated cyto toxicity effector cells by c 3 fragments



C 3 receptors on human lymphocyte subsets and recruitment of antibody dependent lymphocyte mediated cyto toxicity effector cells by c 3 fragments



Journal of Immunology 130(6): 2831-2836



The presence of C3 [complement component 3] receptors on human peripheral blood lymphocytes (PBL) and on the ADCC[antibody dependent cellular cytotoxicity]-exhibiting subset (K [Killer] cells) thereof was analyzed by rosetting with bovine erythrocytes (Eb) or chicken erythrocytes (Ec) carrying human C3b, C3bi or C3d. The indicator cells were coated with 20,000 to 100,000 C3 fragments, obtained by C3 activation with purified proteins of the alternative pathway and trypsin treatment. ADCC was studied at the cellular level by means of a plaque assay, with complement-free or complement-carrying indicator cells as targets. Of the total lymphocytes, 12 to 14% bound EC3b; 6 to 8%, EC3bi; and .apprx. 2%, EC3d. Surface marker analysis indicated that .apprx. 75% of the C3b-binding lymphocytes in PBL were either B or null cells and .apprx. 60% of the C3bi-binding cells were T cells, as characterized by the monoclonal antibodies OKT3 and OKT4 or by presence of receptors for Helix pomatia hemagglutinin. Of the K cells, which constituted from 5 to 10% of the total lymphocytes, .apprx. 20% bound C3b; 30 to 35%, C3bi; and 7 to 8%, C3d. Here the majority of the C3b binders were null cells, and the majority of the C3bi and C3d binders were T cells. Of the C3b-binding K cells, 1/3 and 1/5 of the C3bi-binding K cells bound both fragments. The nature of these double binding cells is unknown. All C3d-binding K cells bound C3bi as well. C3 fragment-carrying target cells did not induce K cell-mediated lysis in the absence of anti-target antibodies but strongly enhanced ADCC in the presence of sublytic concentrations of such antibodies. The rank order for C3 fragment-induced enhancement, C3bi > C3d > C3b, reflected the relative proportions of effector cells binding the different fragments. Enhancement was the expression of effector cell recruitment rather than of increased cytolytic activity of individual K cells. This recruitment was selective in that C3b-carrying target cells primarily recruited effector cells of null type, binding C3b, while C3bi- or C3d-carrying targets primarily recruited C3bi and/or C3d-binding K cells of T.gamma. type. Apparently, at the effector cell level, cell-bound C3 fragments constitute important recognition structures, which strongly amplify ADCC both by recruiting the proper effector cells into the cytolytic reaction and by significantly decreasing the antibody concentration needed for its induction.

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Accession: 004864016

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