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抗核糖体抗体与Sm蛋白D和B/B'结合。

Anti-ribosomal antibodies bind the Sm proteins D and B/B'.

作者信息

Caponi L, Bombardieri S, Migliorini P

机构信息

Clinical Immunology Unit, Istituto di Patologia Medica, University of Pisa, Italy.

出版信息

Clin Exp Immunol. 1998 Apr;112(1):139-43. doi: 10.1046/j.1365-2249.1998.00545.x.

DOI:10.1046/j.1365-2249.1998.00545.x
PMID:9566802
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1904945/
Abstract

In order to analyse the specificity of human anti-ribosomal P protein antibodies, anti-ribosomal P protein antibodies were affinity-purified from the sera of lupus patients. Their binding capacity towards recombinant SmD protein and recombinant SmB/B' protein was evaluated by immunoblot and ELISA. Epitope mapping of SmD was performed by means of synthetic peptides. Anti-ribosomal P protein antibodies bound recombinant SmD (5/10) and SmB/B' (4/10) on immunoblot; 6/10 showed binding capacity to SmD on ELISA. Inhibition experiments using ELISA confirmed the specificity of this binding. Our data indicate the cross-reactivity of spontaneously developed anti-ribosomal P protein antibodies with the B/B' and D constituents of the Sm complex. The coexistence of anti-Sm and anti-ribosomal antibodies in lupus sera may therefore be due, at least in part, to the reactivity of a single autoantibody population.

摘要

为了分析人抗核糖体P蛋白抗体的特异性,从狼疮患者血清中亲和纯化抗核糖体P蛋白抗体。通过免疫印迹和酶联免疫吸附测定(ELISA)评估它们对重组SmD蛋白和重组SmB/B'蛋白的结合能力。利用合成肽对SmD进行表位作图。抗核糖体P蛋白抗体在免疫印迹上能结合重组SmD(5/10)和SmB/B'(4/10);在ELISA中,6/10显示出对SmD的结合能力。使用ELISA的抑制实验证实了这种结合的特异性。我们的数据表明自发产生的抗核糖体P蛋白抗体与Sm复合物的B/B'和D成分存在交叉反应性。因此,狼疮血清中抗Sm抗体和抗核糖体抗体的共存可能至少部分归因于单一自身抗体群体的反应性。

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