Schlicht H J, Wasenauer G, Köck J
Department of Virology, University of Ulm, Federal Republic of Germany.
Arch Virol Suppl. 1993;8:43-52. doi: 10.1007/978-3-7091-9312-9_5.
All hepatitis B viruses examined to date code for at least two different core-gene products which are referred to as the c- and the e-protein. In the case of the human hepatitis B virus, they are known as the HBcAg and the HBeAg. Although these proteins share most of their primary amino acid sequence, they exhibit quite distinct properties. The e-protein is located in the cytoplasm and the nucleus of infected cells and very efficiently assembles into nucleocapsids. By contrast, the e-protein does not form particles. It enters the secretory pathway and is actively secreted by the cells. Here we describe the biosynthetic pathways by which the c- and e-proteins are expressed and summarize recent data from our laboratory showing that the antigenic and biophysical properties which distinguish the HBeAg from the HBcAg are primarily due to the 10 amino acid long portion of the HBeAg leader sequence that remains attached to the HBeAg after cleavage.
迄今为止检测的所有乙型肝炎病毒至少编码两种不同的核心基因产物,分别称为c蛋白和e蛋白。就人类乙型肝炎病毒而言,它们分别被称为乙肝核心抗原(HBcAg)和乙肝e抗原(HBeAg)。尽管这些蛋白质大部分初级氨基酸序列相同,但它们表现出截然不同的特性。e蛋白位于受感染细胞的细胞质和细胞核中,能非常高效地组装成核衣壳。相比之下,c蛋白不形成颗粒。它进入分泌途径并被细胞主动分泌。在此,我们描述了c蛋白和e蛋白的表达所通过的生物合成途径,并总结了我们实验室最近的数据,这些数据表明,将HBeAg与HBcAg区分开来的抗原和生物物理特性主要归因于HBeAg前导序列中10个氨基酸长的部分,该部分在切割后仍与HBeAg相连。