肿瘤坏死因子单抗表位特异性的研究

PRELIMINARY STUDY ON FUNCTIONAL SITES OF TUMOR NECROSIS FACTOR

本研究所制备的6株抗肿瘤坏死因子单克隆抗体中,有3株能够中和肿瘤坏死因子对L929细胞的细胞毒性,但它们的表位特异性却不甚相同。在受体结合测定实验中,中和性单克隆抗体与非中和性单克隆抗体均不能阻断肿瘤坏死因子与L929细胞表面受体的结合。这些初步结果提示肿瘤坏死因子分子上可能有多个部位与其细胞毒性相关,而且其受体结合部位与细胞毒性部位可能是相互分离的。

Auong six monoclonal antibodies (McAbs) against recombinant human tumor necrosis factor (TNF), three were found to be able to neutralize the cytotoxicity of TNF to L929 cells, and their epitope specificities were different in the competition test (ELISA). In the receptor binding assay, the neutralizing McAbs (1B2 and 5A7), as well as the non-neutralizing MoAbs (1G9 and 5B5), failed to block the binding of TNF to its receptor on L929 cells. These results suggested that there might be several sites involved in the TNF cytotoxicity, and these sites might be discrete from the receptor binding sites on L929 cells.