Deminie C A, Emerman M
Program in Molecular Medicine, Fred Hutchinson Cancer Research Center, Seattle, Washington 98104-2092.
J Virol. 1993 Nov;67(11):6499-506. doi: 10.1128/JVI.67.11.6499-6506.1993.
The retroviral Gag polyprotein is necessary and sufficient for assembly and budding of viral particles. However, the exact inter- and intramolecular interactions of the Gag polyproteins during this process are not known. To locate functional domains within Gag, we generated chimeric proviruses between human immunodeficiency virus type 1 (HIV-1) and murine leukemia virus (MuLV). In these chimeric proviruses, the matrix or capsid proteins of MuLV were precisely replaced with the matrix or capsid proteins of HIV-1. Although the chimeric proviruses were unable to efficiently assemble into mature viral particles by themselves, coexpression of wild-type MuLV Gag rescued the HIV proteins into virions. The specificity of the rescue of HIV proteins into MuLV virions shows that specific interactions involving homologous matrix or capsid regions of Gag are necessary for retroviral particle formation.
逆转录病毒Gag多聚蛋白对于病毒颗粒的组装和出芽是必需且充分的。然而,在此过程中Gag多聚蛋白确切的分子间和分子内相互作用尚不清楚。为了定位Gag中的功能结构域,我们构建了1型人类免疫缺陷病毒(HIV-1)和鼠白血病病毒(MuLV)之间的嵌合前病毒。在这些嵌合前病毒中,MuLV的基质或衣壳蛋白被HIV-1的基质或衣壳蛋白精确取代。尽管嵌合前病毒自身无法有效地组装成成熟的病毒颗粒,但野生型MuLV Gag的共表达将HIV蛋白拯救到了病毒粒子中。HIV蛋白被拯救到MuLV病毒粒子中的特异性表明,涉及Gag同源基质或衣壳区域的特定相互作用对于逆转录病毒颗粒的形成是必需的。