Pauls J D, Edworthy S M, Fritzler M J
Joint Injury and Arthritis Research Group, Faculty of Medicine, University of Medicine, University of Calgary, Alberta, Canada.
Mol Immunol. 1993 Jun;30(8):709-19. doi: 10.1016/0161-5890(93)90142-x.
To define the linear epitopes on H5 that react with systemic lupus erythematosus (SLE) and drug-induced lupus (DIL) sera, concurrent overlapping hexameric peptides corresponding to the sequence of H5 were synthesized by stepwise elongation of the polypeptide chains on polyethylene supports. The hexapeptides were tested for reactivity with 8 SLE and 8 DIL sera using an enzyme linked immunosorbent assay (ELISA). SLE and hydralazine-induced lupus (HIL) antibodies were most reactive with peptide 45 (SSRQSI) and patients with procainamide-induced lupus (PIL) were most reactive with peptide 24 (SHPTYS). The epitopes of highest reactivity were in the globular domain of H5. Low reactivity was observed with carboxyl terminal peptides. These findings differ from immunoblotting studies of protease cleaved peptides which have previously shown that the H5 determinants are in the carboxyl terminus.
为了确定与系统性红斑狼疮(SLE)和药物性狼疮(DIL)血清发生反应的H5上的线性表位,通过在聚乙烯支持物上逐步延长多肽链,合成了与H5序列相对应的同时重叠六聚体肽。使用酶联免疫吸附测定(ELISA)检测这些六肽与8份SLE血清和8份DIL血清的反应性。SLE和肼屈嗪诱导的狼疮(HIL)抗体与肽45(SSRQSI)反应性最强,而普鲁卡因胺诱导的狼疮(PIL)患者与肽24(SHPTYS)反应性最强。反应性最高的表位位于H5的球状结构域。在羧基末端肽中观察到低反应性。这些发现与先前对蛋白酶切割肽的免疫印迹研究不同,后者表明H5决定簇位于羧基末端。