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首页> 外文期刊>Infection and immunity >Immunoreactive epitopes on an expressed recombinant flagellar protein of Borrelia burgdorferi.
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Immunoreactive epitopes on an expressed recombinant flagellar protein of Borrelia burgdorferi.

机译：伯氏疏螺旋体表达的重组鞭毛蛋白上的免疫反应性表位。

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摘要

A recombinant Borrelia burgdorferi flagellin protein expressed in Escherichia coli is bound by a murine monoclonal antiflagellin antibody (H9724) and by antibodies in the sera of patients with Lyme disease. Immunoreactive epitopes on the flagellar protein were identified by immunoblot analysis of antibody binding to expressed truncated flagellar proteins. The epitope recognized by the murine monoclonal antibody is within the central heterologous region of the flagellar protein (amino acids 90 to 266). However, antiflagellin antibodies in the sera of patients with Lyme arthritis bound an epitope entirely within, or whose conformation was partly formed by, the 90 NH2-terminal amino acids of the flagellar protein. The binding of antibodies in the sera of patients with Lyme arthritis to the NH2-terminal region of the flagellar protein, a region with sequence homology to the flagellar proteins of other bacterial species, suggests the possibility that antigenic mimicry contributes to the immunopathogenesis of Lyme disease. The fact that human antibodies bind to a highly conserved and hence shared portion of the flagellin reduces the specificity of serological assays for the diagnosis of Lyme disease which use the flagellar protein as antigen.
机译：在大肠杆菌中表达的重组疏螺旋体伯氏疏螺旋体鞭毛蛋白与鼠单克隆抗鞭毛蛋白抗体（H9724）和莱姆病患者血清中的抗体结合。通过对结合表达的截短鞭毛蛋白的抗体进行免疫印迹分析，鉴定了鞭毛蛋白上的免疫反应性抗原决定簇。鼠单克隆抗体识别的表位在鞭毛蛋白（氨基酸90至266）的中央异源区域内。然而，莱姆关节炎患者血清中的抗鞭毛蛋白抗体完全结合鞭毛蛋白的90个NH2末端氨基酸内部的表位或部分构象。莱姆关节炎患者血清中的抗体与鞭毛蛋白的NH2末端区域（与其他细菌的鞭毛蛋白具有序列同源性的区域）的结合表明抗原模仿可能有助于莱姆病的免疫发病机理。人抗体与鞭毛蛋白的高度保守的并因此共享的部分结合的事实降低了使用鞭毛蛋白作为抗原的血清学测定法诊断莱姆病的特异性。

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