Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
J Mol Biol. 2011 Jul 22;410(4):491-500. doi: 10.1016/j.jmb.2011.04.021.
Assembly of human immunodeficiency virus type 1 is driven by oligomerization of the Gag polyprotein at the plasma membrane of an infected cell, leading to membrane envelopment and budding of an immature virus particle. Proteolytic cleavage of Gag at five positions subsequently causes a dramatic rearrangement of the interior virion organization to form an infectious particle. Within the mature virus, the genome is encased within a conical capsid core. Here, we describe the molecular architecture of the virus assembly site, the immature virus, the maturation intermediates and the mature virus core and highlight recent advances in our understanding of these processes from electron microscopy and X-ray crystallography studies.
人类免疫缺陷病毒 1 型的组装是由受感染细胞的质膜上 Gag 多聚蛋白的寡聚化驱动的,导致不成熟病毒颗粒的膜包裹和出芽。Gag 在五个位置的蛋白水解切割随后导致内部病毒结构的剧烈重排,形成感染性颗粒。在成熟病毒中,基因组被包裹在锥形衣壳核心内。在这里,我们描述了病毒组装部位、不成熟病毒、成熟中间体以及成熟病毒核心的分子结构,并强调了电子显微镜和 X 射线晶体学研究对这些过程的最新理解进展。