Ono Akira
Department of Microbiology and Immunology, University of Michigan Medical School.
Uirusu. 2014;64(2):155-64. doi: 10.2222/jsv.64.155.
Location of virus assembly in infected cells has major influences on efficiencies of virus assembly and release and on post-assembly processes including cell-to-cell transmission. Therefore, for better understanding of virus spread and for developing new antiviral strategies, it is important to elucidate mechanisms by which the subcellular site of virus particle assembly is determined. Retrovirus particle assembly is driven by viral structural protein Gag. In the case of HIV-1, Gag binds to the plasma membrane (PM) via the N-terminal MA domain and forms nascent particles at this location. Recent studies reveled that PM-specific phospholipid PI(4,5)P2 plays an important role in directing Gag to the PM through its interaction with MA. In this review, I will summarize our current understanding of relationships between retroviral MA domains and phospholipids in cellular membranes and discuss possible mechanisms by which lipids and other factors regulate membrane binding and subcellular localization of retroviral Gag proteins.
病毒在受感染细胞中的组装位置对病毒组装和释放的效率以及包括细胞间传播在内的组装后过程有重大影响。因此，为了更好地理解病毒传播并开发新的抗病毒策略，阐明病毒粒子组装的亚细胞位点是如何确定的机制很重要。逆转录病毒粒子的组装由病毒结构蛋白Gag驱动。就HIV-1而言，Gag通过N端MA结构域与质膜（PM）结合，并在此位置形成新生颗粒。最近的研究表明，PM特异性磷脂PI(4,5)P2通过与MA的相互作用在将Gag引导至PM方面发挥重要作用。在这篇综述中，我将总结我们目前对逆转录病毒MA结构域与细胞膜中磷脂之间关系的理解，并讨论脂质和其他因素调节逆转录病毒Gag蛋白的膜结合和亚细胞定位的可能机制。
