Cadd T L, MacBeth K, Furlong D, Patterson J L
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts.
J Virol. 1994 Dec;68(12):7738-45. doi: 10.1128/JVI.68.12.7738-7745.1994.
The virion of Leishmania RNA virus is predicted to be composed of a 742-amino-acid major capsid protein and a small percentage of capsid-polymerase fusion molecules. Recently, the capsid protein alone was expressed and shown to spontaneously assemble into viruslike particles. Since the major structural protein of the virion shell self-assembles into viruslike particles when expressed in the baculovirus expression system, assembly of the virion can be studied by mutational analysis and expression of a single open reading frame. In this study, several deletions and one addition of the capsid protein of Leishmania RNA virus LRV1-4 were generated. These mutants show different degrees of assembly. Assembly domains are being identified such that the capsid protein may be used as a macromolecular packaging and delivery system for Leishmania species.
利什曼原虫RNA病毒的病毒粒子预计由一种742个氨基酸的主要衣壳蛋白和一小部分衣壳-聚合酶融合分子组成。最近，单独表达了衣壳蛋白，并显示其能自发组装成病毒样颗粒。由于病毒粒子外壳的主要结构蛋白在杆状病毒表达系统中表达时会自组装成病毒样颗粒，因此可以通过突变分析和单个开放阅读框的表达来研究病毒粒子的组装。在本研究中，构建了利什曼原虫RNA病毒LRV1-4衣壳蛋白的几个缺失突变体和一个添加突变体。这些突变体表现出不同程度的组装。正在鉴定组装结构域，以便衣壳蛋白可作为利什曼原虫属的大分子包装和递送系统。
