Structure and assembly of immature HIV

Structure and assembly of immature HIV
复制标题

DOI:
10.1073/pnas.0903535106
复制
发表时间:
2009-07-07
影响因子:
11.1
通讯作者:
Kraeusslich, H.-G.
Kraeusslich, H.-G.
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Briggs, J. A. G.;Riches, J. D.;Kraeusslich, H.-G.

文献摘要

被引文献

相似文献

HIV的主要结构成分是一个55-kDa的多蛋白Gag。粒子形成是由Gag自组装成弯曲的六聚晶格驱动的,其结构尚不清楚。我们使用低温电子断层扫描和对比度传递函数校正亚断层扫描平均来研究组装的未成熟Gag晶格的结构,接近17埃的分辨率。Gag在未成熟病毒中以单一、连续但不完整的六聚体晶格排列,其曲率是介导的,不需要五聚体缺陷。该结构的分辨率允许对单个蛋白质结构域进行定位。高分辨率的晶体结构被安装到重建中,以定位Gag组装中涉及的蛋白质-蛋白质界面,并确定与病毒成熟相关的结构转化。这项研究的结果提出了一个概念,形成可变大小的非对称包膜病毒。
The major structural components of HIV are synthesized as a 55-kDa polyprotein, Gag. Particle formation is driven by the self-assembly of Gag into a curved hexameric lattice, the structure of which is poorly understood. We used cryoelectron tomography and contrast-transfer-function corrected subtomogram averaging to study the structure of the assembled immature Gag lattice to approximate to 17-angstrom resolution. Gag is arranged in the immature virus as a single, continuous, but incomplete hexameric lattice whose curvature is mediated without a requirement for pentameric defects. The resolution of the structure allows positioning of individual protein domains. High-resolution crystal structures were fitted into the reconstruction to locate protein-protein interfaces involved in Gag assembly, and to identify the structural transformations associated with virus maturation. The results of this study suggest a concept for the formation of nonsymmetrical enveloped viruses of variable sizes.