Interrelationship between autoepitope, DNA-binding domain, and CRP-binding domain on a histone H1 molecule.

The interrelationship between autoepitopes, DNA-binding domains, and C-reactive protein (CRP)-binding domains on a histone H1 molecule was examined using fusion proteins of beta-galactosidase and truncated histone H1 molecules. At least two CRP-binding sites were detected on a histone H1 molecule. Site 1 was composed of approximately 25 amino acids and calcium ion was required for the binding of CRP. Site 2, composed of approximately 20 amino acids and not requiring calcium ion, was identical or located very close to a DNA-binding domain and an epitope of anti-histone H1 autoantibodies in SLE sera. These data suggest that, at physiological ionic strength, histone H1 of either free or immune-complexed form could bind to CRP via site 1. These data are discussed with respect to the possible role of CRP in the handling and clearance of immune complexes in patients with systemic lupus erythematosus.