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首页> 外文期刊>Cell Reports >Antibody Treatment of Ebola and Sudan Virus Infection via a Uniquely Exposed Epitope within the Glycoprotein Receptor-Binding Site
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Antibody Treatment of Ebola and Sudan Virus Infection via a Uniquely Exposed Epitope within the Glycoprotein Receptor-Binding Site

机译：通过糖蛋白受体结合位点内唯一暴露的表位治疗埃博拉和苏丹病毒感染的抗体

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Previous efforts to identify cross-neutralizing antibodies to the receptor-binding site (RBS) of ebolavirus glycoproteins have been unsuccessful, largely because the RBS is occluded on the viral surface. We report a monoclonal antibody (FVM04) that targets a uniquely exposed epitope within the RBS; cross-neutralizes Ebola (EBOV), Sudan (SUDV), and, to a lesser extent, Bundibugyo viruses; and shows protection against EBOV and SUDV in mice and guinea pigs. The antibody cocktail ZMapp(TM) is remarkably effective against EBOV (Zaire) but does not cross-neutralize other ebolaviruses. By replacing one of the ZMapp(TM) components with FVM04, we retained the anti-EBOV efficacy while extending the breadth of protection to SUDV, thereby generating a cross-protective antibody cocktail. In addition, we report several mutations at the base of the ebolavirus glycoprotein that enhance the binding of FVM04 and other cross-reactive antibodies. These findings have important implications for pan-ebolavirus vaccine development and defining broadly protective antibody cocktails.
机译：先前鉴定针对埃博拉病毒糖蛋白的受体结合位点（RBS）的交叉中和抗体的努力并未成功，这主要是因为RBS闭塞在病毒表面。我们报告了针对RBS中唯一暴露的表位的单克隆抗体（FVM04）;交叉中和埃博拉（EBOV），苏丹（SUDV），以及较小程度的Bundibugyo病毒;并且在小鼠和豚鼠中显示出针对EBOV和SUDV的保护作用。抗体混合物ZMapp TM对EBOV（Zaire）具有显着的效力，但不能交叉中和其他埃博拉病毒。通过用FVM04替代ZMapp™组件之一，我们保留了抗EBOV功效，同时将保护范围扩展至SUDV，从而产生了交叉保护性抗体混合物。此外，我们报告了埃博拉病毒糖蛋白基础上的几个突变，这些突变增强了FVM04和其他交叉反应抗体的结合。这些发现对泛埃博拉病毒疫苗的开发和定义广泛的保护性抗体混合物具有重要意义。

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