Wengler G
Institut für Virologie, Justus-Liebig-Universität Giessen, Germany.
Behring Inst Mitt. 1991 Jul(89):209-16.
In many viral systems the genome is part of a stable nucleoprotein complex which has to be dissociated early in infection, in order to make the genome accessible for transcription or translation. It is not directly evident how a nucleoprotein generated as a stable complex during virus assembly can be dissociated during the initial steps of viral multiplication. During analyses of the molecular biology of alphavirus replication it has been shown that the core protein of these viruses is a multifunctional protein. In this manuscript I propose that one of the functions of the core protein, namely its ability to bind to the large subunit of the cellular ribosomes both during synthesis and as a mature protein, allows to regulate the assembly and disassembly of alphavirus cores. I propose that in the early stages of virus infection the core protein is transferred from the core of the incoming virus to the cellular ribosomes, whereas in the late stages of infection when a significant part of the ribosomes contain bound, newly synthesized core protein an efficient transfer of newly synthesized core protein into cores can occur.
在许多病毒系统中，基因组是稳定核蛋白复合体的一部分，在感染早期该复合体必须解离，以便使基因组能够进行转录或翻译。病毒组装过程中作为稳定复合体产生的核蛋白如何在病毒增殖的初始阶段解离，这一点并不直接明了。在对甲病毒复制分子生物学的分析过程中，已表明这些病毒的核心蛋白是一种多功能蛋白。在本手稿中，我提出核心蛋白的功能之一，即在合成过程中和作为成熟蛋白时与细胞核糖体大亚基结合的能力，能够调节甲病毒核心的组装和解离。我提出在病毒感染的早期阶段，核心蛋白从进入病毒的核心转移到细胞核糖体，而在感染后期，当相当一部分核糖体含有结合的新合成核心蛋白时，新合成的核心蛋白能够有效地转移到核心中。
