Interactions of OspA monoclonal antibody C3.78 with Borrelia burgdorferi within ticks

Interactions of OspA monoclonal antibody C3.78 with Borrelia burgdorferi within ticks
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DOI:
10.1128/iai.73.3.1644-1647.2005
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发表时间:
2005-03-01
影响因子:
3.1
通讯作者:
de Silva, AM
de Silva, AM
中科院分区:
医学2区
文献类型:
--
作者:
Gipson, CL;de Silva, AM

文献摘要

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伯氏疏螺旋体外表面蛋白A (OspA)疫苗可诱导抗体,防止蜱虫向宿主传播。在这里,我们描述了用OspA单克隆抗体(C3.78)进行的研究,以了解进入蜱虫的抗体阻止伯氏疏螺旋体传播的机制。蜱虫血粉中的宿主补体没有起到保护作用,因为无论被感染的蜱虫以正常或补体缺乏的小鼠为食,抗体都同样有效。由于C3.78 Fab'片段与整个抗体分子一样有效,因此不需要抗体介导的细菌交联或OspA分子交联来保护。在低C3.78浓度下,尽管蜱体内存在许多活螺旋体,但传播被阻断,这证实不需要清除伯氏疏螺旋体来阻止传播。我们提出OspA抗体结合到螺旋体表面通过不需要杀死细菌的机制阻止传播。
The Borrelia burgdorferi outer surface protein A (OspA) vaccine induces antibodies that prevent transmission from the tick to the host. Here we describe studies with an OspA monoclonal antibody (C3.78) to understand the mechanism by which antibodies entering the tick block Borrelia transmission. Host complement in the tick's blood meal did not contribute to protection because the antibody was equally effective whether infected ticks fed on normal or complement-deficient mice. Antibody-mediated cross-linking of bacteria or cross-linking of OspA molecules was not required for protection because C3.78 Fab' fragments were as effective as whole antibody molecules. At low C3.78 concentrations, transmission was blocked despite the presence of many live spirochetes within the tick, confirming that clearance of Borrelia organisms was not required to block transmission. We propose that OspA antibody binding to the surface of spirochetes blocks transmission by a mechanism that does not require bacterial killing.