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首页> 外文期刊>Infection and immunity >Production and characterization of monoclonal antibodies against the lethal factor component of Bacillus anthracis lethal toxin.
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Production and characterization of monoclonal antibodies against the lethal factor component of Bacillus anthracis lethal toxin.

机译：抗炭疽芽孢杆菌致死毒素致死因子成分的单克隆抗体的生产和表征。

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The lethal toxin of Bacillus anthracis consists of two components, protective antigen and lethal factor. Protective antigen is cleaved after binding to cell receptors, yielding a receptor-bound fragment that binds lethal factor. Sixty-one monoclonal antibodies to the lethal factor protein have been characterized for specificity, antibody subtype, and ability to neutralize lethal toxin. Three monoclonal antibodies (10G3, 2E7, and 3F6) neutralized lethal toxin in Fisher 344 rats. However, in a macrophage cytolysis assay, monoclonal antibodies 10G3, 2E7, 10G4, 10D4, 13D10, and 1D8, but not 3F6, were found to neutralize lethal toxin. Binding studies showed that five of the monoclonal antibodies that neutralized lethal toxin in the macrophage assay (10G3, 2E7, 10G4, 10D4, and 13D10) did so by inhibiting the binding of lethal factor to the protective antigen fragment bound to cells. Monoclonal antibody 1D8, which was also able to neutralize lethal toxin activity after lethal factor was prebound to cell-bound protective antigen, only partially inhibited binding of lethal factor to protective antigen. Monoclonal antibody 3F6 did not inhibit the binding of lethal factor to protective antigen. A competitive-binding enzyme-linked immunosorbent assay showed that at least four different antigenic regions on lethal factor were recognized by these seven neutralizing hybridomas. The anomalous behavior of 3F6 suggests that it may induce a conformational change in lethal factor. Differences in neutralizing activity of monoclonal antibodies were related to their relative affinity and epitope specificity and the type of assay.
机译：炭疽芽孢杆菌的致死毒素由两部分组成，保护性抗原和致死因子。结合细胞受体后，保护性抗原被切割，产生结合致死因子的受体结合片段。已经针对特异性，抗体亚型和中和致死毒素的能力对针对致死因子蛋白的六十一种单克隆抗体进行了表征。三种单克隆抗体（10G3、2E7和3F6）中和了Fisher 344大鼠的致命毒素。但是，在巨噬细胞细胞溶解测定中，发现单克隆抗体10G3、2E7、10G4、10D4、13D10和1D8而非3F6可以中和致命毒素。结合研究表明，在巨噬细胞分析中，有五种中和致死毒素的单克隆抗体（10G3、2E7、10G4、10D4和13D10）通过抑制致死因子与与细胞结合的保护性抗原片段的结合来实现。单克隆抗体1D8在将致死因子预先结合到细胞结合的保护性抗原后也能够中和致死毒素的活性，仅部分抑制了致死因子与保护性抗原的结合。单克隆抗体3F6不会抑制致死因子与保护性抗原的结合。竞争性结合酶联免疫吸附试验表明，这七个中和杂交瘤可识别致死因子上至少四个不同的抗原区域。 3F6的异常行为表明它可能诱发致死因子的构象变化。单克隆抗体的中和活性差异与它们的相对亲和力和表位特异性以及检测类型有关。

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