Pauls J D, Gohill J, Fritzler M J
Division of Rheumatology and Clinical Immunology, Faculty of Medicine, University of Calgary, Alberta, Canada.
Mol Immunol. 1990 Aug;27(8):701-11. doi: 10.1016/0161-5890(90)90079-f.
The antigenic domains of histone 5 (H5), a highly conserved variant of histone 1 (H1), were studied in relation to their reactivity with autoantibodies found in the sera of patients with systemic lupus erythematosus (SLE) and drug-induced lupus (DIL). While some H5 antibodies cross-react with H1, adsorption and immunoblotting studies have identified H5-specific antibodies as well. After proteolytic cleavage of H5 peptides, the reactivity of sera from these patients was tested by Western immunoblotting. All SLE (9/9) and DIL (7/7) sera bound an antigenic determinant in the carboxyl (C) terminus of H5 while none of the sera bound to the amino (N) terminus or the central hydrophobic domain. Although the reactivity of DIL sera with the purified H5 peptides was weaker than that of SLE sera, the antigenic domains bound by both groups of sera were the same. These observations demonstrate that the H5 domains reacting with DIL sera are restricted to the carboxyl terminus and are therefore no less restricted than those reacting with SLE sera. Further, the potential epitopes in the carboxyl terminus of H5 do not have a high degree of sequence identity with known mammalian peptides.
组蛋白5（H5）是组蛋白1（H1）的一种高度保守的变体，研究了其抗原结构域与系统性红斑狼疮（SLE）和药物性狼疮（DIL）患者血清中自身抗体的反应性。虽然一些H5抗体与H1交叉反应，但吸附和免疫印迹研究也鉴定出了H5特异性抗体。对H5肽进行蛋白水解切割后，通过Western免疫印迹检测这些患者血清的反应性。所有SLE（9/9）和DIL（7/7）血清均与H5羧基（C）末端的一个抗原决定簇结合，而没有血清与氨基（N）末端或中央疏水结构域结合。虽然DIL血清与纯化的H5肽的反应性比SLE血清弱，但两组血清结合的抗原结构域相同。这些观察结果表明，与DIL血清反应的H5结构域仅限于羧基末端，因此与与SLE血清反应的结构域一样受到限制。此外，H5羧基末端的潜在表位与已知的哺乳动物肽没有高度的序列同一性。
