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针对1型单纯疱疹病毒糖蛋白的单克隆抗体表明,表位位置会影响病毒中和作用。

Monoclonal antibodies to herpes simplex virus type 1 glycoproteins show that epitope location influences virus neutralization.

作者信息

La Thangue N B, Chan W L, Almeida J D

出版信息

J Med Virol. 1984;13(3):227-42. doi: 10.1002/jmv.1890130305.

Abstract

Three monoclonal antibodies, G8D1 , C2D2 , and TI57 , reacting with herpes simplex virus type 1 glycoproteins have been characterised according to the location of their epitope and ability to neutralize infective virus. Immune electron microscopy and a blocking radioimmunoassay were used to locate the epitopes. The results indicate that the epitope recognised by G8D1 is located on the surface of the glycoprotein fringe, whereas those recognized by C2D2 and TI57 are interior with respect to this. Only G8D1 has neutralizing activity alone, whereas C2D2 can neutralize when antiglobulin is added. Thus, epitope location and density determine the neutralizing capacity of individual antibody molecules.

摘要

已根据三种与1型单纯疱疹病毒糖蛋白反应的单克隆抗体G8D1、C2D2和TI57的表位位置及中和感染性病毒的能力对其进行了表征。采用免疫电子显微镜和阻断放射免疫测定法来定位表位。结果表明,G8D1识别的表位位于糖蛋白边缘的表面,而C2D2和TI57识别的表位相对于此位于内部。只有G8D1单独具有中和活性,而添加抗球蛋白时C2D2可以中和。因此,表位位置和密度决定了单个抗体分子的中和能力。

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