The effect of immunoglobulin G1 structure on macrophage binding to supported planar lipid monolayers.
We have studied the antibody-dependent binding of macrophages to supported planar lipid monolayers containing haptenated phospholipids (Tnp-Cap-DPPE). Eight monoclonal anti-TNP IgG1s, which had similar affinities to the TNP residues in solution and in the membranes, were used in the experiment. The results showed that mouse macrophages (P388D1 and J774.1) bound with different affinities to these IgG1-coated lipid monolayers. The monoclonal antibody shown to be deficient in macrophage binding was also relatively ineffective in activating complement. These results indicated that individual monoclonal antibodies of a given subclass may prove deficient in terms of the biological activities associated with the group as a whole.
D000818:Animals; D000915:Antibody Affinity; D002460:Cell Line; D003167:Complement Activation; D007074:Immunoglobulin G / Q000276:immunology*; D008055:Lipids; D008081:Liposomes; D008264:Macrophages / Q000276:immunology*; D051379:Mice; D010714:Phosphatidylethanolamines; D011961:Receptors, Fc / Q000276:immunology; D014301:Trinitrobenzenes / Q000276:immunology
D007074:Immunoglobulin G; D008055:Lipids; D008081:Liposomes; D010714:Phosphatidylethanolamines; D011961:Receptors, Fc; D014301:Trinitrobenzenes; C007510:1,2-dipalmitoyl-3-phosphatidylethanolamine