Non-immune IgG F(ab')2 binding to group C and G streptococci is mediated by structures on gamma chains.

The present investigation was designed to determine whether the heavy or the light immunoglobulin chain is involved in the non-immune binding of IgG F(ab')2 fragments to specific surface receptors on human group C and G streptococci. Purified human polyclonal IgG was mildly reduced with dithiothreitol and alkylated with iodoacetamide. Light (L) and heavy (H) chains were separated. Intact IgG and purified L and H chains of polyclonal immunoglobulin G were tested in an inhibition assay for non-immune IgG F(ab')2-mediated binding to group C and G streptococci. H chains inhibited the uptake of isotope-labelled IgG F(ab')2 fragments. Isolated L chains were non-reactive. Intact IgG molecules were more potent inhibitors than isolated H chains tested in equimolar concentrations. These results indicate that the non-immune interaction between human group C and G streptococci and F(ab')2 fragments of human IgG is mediated by reactive sites exposed on the immunoglobulin G H chains. The observation that intact IgG on a molar basis was more inhibitory than purified gamma chains suggests that the L chains may contribute to the reactivity, presumably by passive stabilization of the immunoglobulin molecule.