Ueno Tomonori, Tokunaga Kenzo, Sawa Hirofumi, Maeda Masae, Chiba Joe, Kojima Asato, Hasegawa Hideki, Shoya Yuko, Sata Tetsutaro, Kurata Takeshi, Takahashi Hidehiro
Department of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
Microbiol Immunol. 2004;48(2):111-8. doi: 10.1111/j.1348-0421.2004.tb03496.x.
Gag proteins of human immunodeficiency virus type 1 (HIV-1) play a pivotal role in the budding of the virion, in which the zinc finger motifs of the gag proteins recognize the packaging signal of genomic RNA. Nucleolin, an RNA-binding protein, is identified as a cellular protein that binds to murine leukemia virus (MuLV) gag proteins and regulates the viral budding, suggesting that HIV-1 gag proteins, the packaging signal, psi and nucleolin affect the budding of HIV-1. Here we report that nucleolin enhances the release of HIV-1 virions which contain psi. Furthermore, nucleolin and gag proteins form a complex incorporated into virions, and nucleolin promotes the infectivity of HIV-1. Our results suggest that an empty particle which contains neither nucleolin nor the genomic RNA is eliminated during the budding process, and this mechanism is beneficial for escape from the host immune response against HIV-1.
1型人类免疫缺陷病毒（HIV-1）的Gag蛋白在病毒粒子出芽过程中起关键作用，其中Gag蛋白的锌指基序识别基因组RNA的包装信号。核仁素是一种RNA结合蛋白，被鉴定为一种与鼠白血病病毒（MuLV）Gag蛋白结合并调节病毒出芽的细胞蛋白，这表明HIV-1 Gag蛋白、包装信号ψ和核仁素会影响HIV-1的出芽。在此我们报告，核仁素增强了含有ψ的HIV-1病毒粒子的释放。此外，核仁素与Gag蛋白形成复合物并整合到病毒粒子中，并且核仁素促进HIV-1的感染性。我们的结果表明，在出芽过程中不含核仁素和基因组RNA的空病毒粒子被清除，并且这种机制有利于逃避宿主针对HIV-1的免疫反应。
