![]() Our findings suggest that heparan sulfate might serve as a target antigen in vivo for cross-reactive anti-DNA antibodies. Heparan sulfate is the major glycosaminoglycan constituent of the glomerular basement membrane. Antibodies eluted from human and mouse kidneys with diffuse SLE glomerulonephritis showed a similar binding to DNA and heparan sulfate when these eluted antibodies were tested in vitro. 26,27 A study on the actual binding sites of anti-adalimumab antibodies revealed that the antibody response. 25-27 Notably, for both monoclonal and polyclonal anti-adalimumab antibodies, no cross-reactivity was observed to infliximab. That this reaction is due to crossreactivity of anti-DNA antibodies was further substantiated by the finding that two monoclonal anti-DNA antibodies also bound to heparan sulfate. The specificities of the anti-drug antibodies have been characterized for different anti-TNF therapeutics. By inhibition studies it was demonstrated that heparan sulfate could inhibit the binding of anti-DNA antibodies to DNA, whereas DNA could block the binding to heparan sulfate. The anti-heparan sulfate titers showed a significant correlation with the anti-DNA antibody titers. Affinity, which can be determined experimentally, is a measure of the binding strength between an antibodys binding site and an epitope, whereas avidity is the total strength of all the interactions in an antibody-antigen complex (which. In 30 of 33 human systemic lupus erythematosus (SLE) sera and in 10 sera from MRL/l mice with spontaneous SLE, antibodies against heparan sulfate were detected. Cross-reactivity is more likely to occur between antibodies and antigens that have low affinity or avidity.
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