Structure and assembly of immature HIV

被引:288
作者
Briggs, J. A. G. [1 ]
Riches, J. D. [1 ]
Glass, B. [2 ]
Bartonova, V. [2 ]
Zanetti, G. [1 ,3 ]
Kraeusslich, H.-G. [2 ]
机构
[1] European Mol Biol Lab, Struct & Computat Biol Unit, D-69117 Heidelberg, Germany
[2] Univ Klinikum Heidelberg, Abt Virol, D-69120 Heidelberg, Germany
[3] Univ Oxford, Wellcome Trust Ctr Human Genet, Div Struct Biol, Oxford OX3 7BN, England
关键词
cryoelectron tomography; virus assembly; contrast transfer function; capsid; retrovirus; HUMAN-IMMUNODEFICIENCY-VIRUS; AMINO-TERMINAL DOMAIN; CAPSID PROTEIN; ELECTRON CRYOTOMOGRAPHY; 3-DIMENSIONAL STRUCTURE; HELICAL STRUCTURE; CYCLOPHILIN-A; TYPE-1; GAG; VIRIONS; REVEALS;
D O I
10.1073/pnas.0903535106
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:11090 / 11095
页数:6
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