Relationship Between Autoepitope and DNA-Binding Site on a Histone H1 Molecule

Seiji Minota Third Department of Internal Medicine and the Department of Internal Medicine and Physical Therapy, University of Tokyo, Tokyo

Hitoshi Miura Third Department of Internal Medicine and the Department of Internal Medicine and Physical Therapy, University of Tokyo, Tokyo

Yoshikata Misaki Third Department of Internal Medicine and the Department of Internal Medicine and Physical Therapy, University of Tokyo, Tokyo

Kazuhiko Yamamoto Third Department of Internal Medicine and the Department of Internal Medicine and Physical Therapy, University of Tokyo, Tokyo

Noritsugu Morino Third Department of Internal Medicine and the Department of Internal Medicine and Physical Therapy, University of Tokyo, Tokyo

Hiroyuki Sakurai Third Department of Internal Medicine and the Department of Internal Medicine and Physical Therapy, University of Tokyo, Tokyo

Akira Yamada Third Department of Internal Medicine and the Department of Internal Medicine and Physical Therapy, University of Tokyo, Tokyo

Yoshio Yazaki Third Department of Internal Medicine and the Department of Internal Medicine and Physical Therapy, University of Tokyo, Tokyo

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Abstract

Autoepitope and DNA-binding domain on a histone H1 molecule were compared using truncated histone H1 peptides as antigens. At least two epitopes (epitope A, N-terminal side; epitope B, C-terminal side) were found both of which were composed of ∼20 amino acids. IgM from all 17 anti-histone H1-positive SLE sera reacted with epitope A. IgG from 12 sera reacted with epitope A and IgG from 4 sera reacted with epitope B. In one case, no IgG anti-histone H1 reactivities were found while IgM from the same patient reacted with epitope A. Epitope A had the ability to bind DNA. The reactivities against histone H1 of affinity-purified anti-epitope A autoantibodies were inhibited by DNA. These data suggest that some anti-histone H1 antibodies are directed against a histone H1 DNA-binding site, raising the possibility that an idiotype/anti-idiotype network, at least in part, is involved in the generation of anti-histone H1 autoantibodies.

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Relationship Between Autoepitope and DNA-Binding Site on a Histone H1 Molecule

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Relationship Between Autoepitope and DNA-Binding Site on a Histone H1 Molecule

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