Yu M, Wang L F, Shiell B J, Morrissy C J, Westbury H A
CSIRO Australian Animal Health Laboratory, Geelong, Victoria, Australia.
Virology. 1996 Aug 1;222(1):289-92. doi: 10.1006/viro.1996.0423.
Envelope glycoprotein E2 (gp51 to gp54) is the major neutralizing antigen of pestiviruses, which include classical swine fever virus (CSFV), bovine viral diarrhoea virus (BVDV), and border disease virus (BVD). Previous studies carried out using a panel of monoclonal antibodies raised against CSFV strain Brescia have revealed the existence of four antigenic domains, A to D, of the E2 protein, all of which are located at the N-terminal half of the molecule. Here we report the detailed mapping, using three complementary techniques, of a novel linear epitope located at the C-terminal part of the molecule, which reacted with a monoclonal antibody (4-9D4) as well as polyclonal animal sera. This epitope is highly conserved in the three different members of pestiviruses and hence can be used as a genus-specific diagnosis tool. The observation that this epitope is not accessible on the native virus surface, together with its C-terminal location, supports a recently proposed structural model, indicating that the C-terminal part of E2 is membrane-bound while the N-terminal half of the molecule is exposed on the virus surface.
包膜糖蛋白E2（gp51至gp54）是瘟病毒的主要中和抗原，瘟病毒包括经典猪瘟病毒（CSFV）、牛病毒性腹泻病毒（BVDV）和边境病病毒（BVD）。先前使用针对CSFV Brescia株产生的一组单克隆抗体进行的研究揭示了E2蛋白存在四个抗原结构域，A至D，所有这些结构域都位于分子的N端半部分。在此，我们报告了使用三种互补技术对位于分子C端部分的一个新型线性表位进行的详细定位，该表位与一种单克隆抗体（4-9D4）以及多克隆动物血清发生反应。该表位在瘟病毒的三个不同成员中高度保守，因此可作为属特异性诊断工具。该表位在天然病毒表面不可接近以及其C端位置的观察结果支持了最近提出的结构模型，表明E2的C端部分与膜结合，而分子的N端半部分暴露在病毒表面。
