U.S. Army Medical Research Institute of Infectious Disease, Virology Division, Fort Detrick, Frederick, MD 21702, USA.
J Virol. 2010 Dec;84(24):12683-90. doi: 10.1128/JVI.01345-10. Epub 2010 Oct 6.
Six monoclonal antibodies were isolated that exhibited specificity for a furin cleavage site deletion mutant (V3526) of Venezuelan equine encephalitis virus (VEEV). These antibodies comprise a single competition group and bound the E3 glycoprotein of VEEV subtype I viruses but failed to bind the E3 glycoprotein of other alphaviruses. These antibodies neutralized V3526 virus infectivity but did not neutralize the parental strain of Trinidad donkey (TrD) VEEV. However, the E3-specific antibodies did inhibit the production of virus from VEEV TrD-infected cells. In addition, passive immunization of mice demonstrated that antibody to the E3 glycoprotein provided protection against lethal VEEV TrD challenge. This is the first recognition of a protective epitope in the E3 glycoprotein. Furthermore, these results indicate that E3 plays a critical role late in the morphogenesis of progeny virus after E3 appears on the surfaces of infected cells.
六种单克隆抗体被分离出来，它们对委内瑞拉马脑炎病毒（VEEV）的弗林裂解位点缺失突变体（V3526）表现出特异性。这些抗体构成了一个单一的竞争组，结合了 VEEV 亚型 I 病毒的 E3 糖蛋白，但未能结合其他甲病毒的 E3 糖蛋白。这些抗体中和了 V3526 病毒的感染性，但不能中和亲本的特立尼达驴（TrD）VEEV。然而，E3 特异性抗体确实抑制了从 VEEV TrD 感染的细胞中产生病毒。此外，对小鼠的被动免疫表明，针对 E3 糖蛋白的抗体提供了针对致死性 VEEV TrD 挑战的保护。这是首次在 E3 糖蛋白中识别出保护性表位。此外，这些结果表明，E3 在 E3 出现在感染细胞表面后，在子代病毒形态发生的后期发挥关键作用。
