The selective binding of aggregated IgG to lipid A-rich bacterial lipopolysaccharides.
To explore the mechanism by which certain bacterial lipopolysaccharides (LPS) enhance platelet stimulation by aggregated IgG, we studied potential interactions between the two ligands. Lipid A or the lipid A-rich LPS from Salmonella minnesota R595 (LPS R595) selectively increased the sedimentation of aggregated rather than monomer IgG in sucrose density gradients. Insolubilized IgG aggregates adsorbed LPS R595 from solution. These two experiments suggested binding of IgG aggregates to LPS R595 or lipid A and this was confirmed by isopycnic density gradient ultracentrifugation studies. The presence of R595 LPS shifted the equilibrium density profile of aggregated IgG from its usual equilibrium density at 1.30 g/ml to a new position superimposable with that of the LPS R595. The possibility that a selective binding of IgG aggregates to LPS may represent a fundamental mechanism of the action of LPS on cellular mediation systems is proposed.
D000936:Antigen-Antibody Complex; D006801:Humans; D007074:Immunoglobulin G; D008050:Lipid A / Q000276:immunology*; D008070:Lipopolysaccharides / Q000276:immunology*; D011135:Polysaccharides, Bacterial / Q000276:immunology*; D012475:Salmonella / Q000276:immunology; D014461:Ultracentrifugation
D000936:Antigen-Antibody Complex; D007074:Immunoglobulin G; D008050:Lipid A; D008070:Lipopolysaccharides; D011135:Polysaccharides, Bacterial