Two dual-specific (anti-IgG and anti-dsDNA) monoclonal autoantibodies derived from the NZB/NZW F1 recognize an epitope in the hinge region

The anti-IgG properties of two dual-specific (anti-dsDNA and anti-IgG) monoclonal NZB/NZW F1-derived autoantibodies, BV 17–45 and BV 16–13, were studied to resolve the location and possible commonality of the IgG epitope. To determine if BV 17–45 and BV 16–13 recognized the same IgG epitope, the relative temperature sensitivity of the conformational IgG epitopes were evaluated using the conformational sensitive immunoassay. Comparison of the temperature sensitivity of the conformational immunoglobulin epitopes over a temperature range of 25–100°C suggested that the epitope recognized by BV 17–45 was the same as the IgG epitope recognized by BV 16–13. Further studies with papain- and pepsin-generated F(ab′) 2 , Fab, and Fc fragments of BV 17–45 and BV 16–13 revealed that the dual-specific autoantibodies BV 17–45 and BV 16–13 both bound an epitope in the hinge region of the IgG molecule. The potential correlation between these studies and the pathogenic nature of dual-specific autoantibodies is discussed.