Diamond Michael S, Pierson Theodore C, Fremont Daved H
Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO 63110, USA.
Immunol Rev. 2008 Oct;225:212-25. doi: 10.1111/j.1600-065X.2008.00676.x.
Recent investigations of the interaction between the West Nile virus (WNV) envelope protein (E) and monoclonal antibodies (mAbs) have elucidated fundamental insights into the molecular mechanisms of neutralization. Structural studies have defined an epitope on the lateral ridge of domain III (DIII-lr) of the WNV E protein that is recognized by antibodies with the strongest neutralizing activity in vitro and in vivo. Antibodies that bind this epitope are highly potent because they efficiently block at a post-entry step of viral infection with relatively low virion occupancy requirements. In this review, we discuss the structural, molecular, and immunologic basis for antibody-mediated protection against WNV, and its implications for novel therapeutic or vaccine strategies.
最近对西尼罗河病毒(WNV)包膜蛋白(E)与单克隆抗体(mAb)之间相互作用的研究,阐明了中和作用分子机制的基本见解。结构研究确定了WNV E蛋白结构域III(DIII-lr)外侧脊上的一个表位,该表位在体外和体内被具有最强中和活性的抗体识别。结合该表位的抗体效力很高,因为它们能在病毒感染的进入后步骤有效阻断,且对病毒粒子占据率的要求相对较低。在本综述中,我们讨论了抗体介导的针对WNV的保护作用的结构、分子和免疫学基础,及其对新型治疗或疫苗策略的意义。