PMID: 8596057Mar 1, 1996Paper

Epitope mapping of C1 inhibitor autoantibodies from patients with acquired C1 inhibitor deficiency

The Journal of Immunology : Official Journal of the American Association of Immunologists
S HeK Whaley

Abstract

We report six patients with acquired C1 inhibitor (C1-inh) deficiency associated with serum C1-inh autoantibodies and circulating cleaved (96 kDa), functionally inactive C1-inh. In three patients, all of whom had IgG-kappa paraproteins in their sera, the Abs were IgG-kappa. In the remaining three patients, the Abs were IgM (2 kappa, 1 lambda). These data suggest that all the Abs were monoclonal. The autoantibodies recognized two synthetic peptides (peptides 2 and 3), which spanned the reactive center of C1-inh. Binding to peptide 3 (residues 448-459) was greater than to peptide 2 (residues 438-449), suggesting that the epitope recognized by the autoantibodies was expressed principally by peptide 3. Both peptides inhibited the binding of the autoantibodies to C1-inh. None of the autoantibodies recognized peptide 1 (residues 428-440), and this peptide did not inhibit the binding of the autoantibodies to C1-inh. The use of substituted peptides suggested that residues Q452 and Q453 made significant contributions to the epitope, and computer modeling studies showed their side chains to be surface exposed in the intact molecule. However, computer modeling also showed that none of the side chains of the polar residues in peptide 2 wer...Continue Reading

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