Structural organization of authentic, mature HIV-1 virions and cores

被引:373
作者
Briggs, JAG
Wilk, T
Welker, R
Kräusslich, HG
Fuller, SD
机构
[1] Univ Oxford, Wellcome Trust Ctr Human Genet, Div Struct Biol, Oxford OX3 7BN, England
[2] Univ Heidelberg Klinikujm, Abt Virol, Heidelberg, Germany
基金
英国惠康基金;
关键词
capsid protein; cryo-electron microscopy; fullerenes; macromolecular assembly; retrovirus;
D O I
10.1093/emboj/cdg143
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Mature, infectious HIV-1 particles contain a characteristic cone-shaped core that encases the viral RNA and replication proteins. The architectures of mature virions and isolated cores were studied using cryoelectron microscopy. The average size (similar to145 nm) of the virion was unchanged during maturation. Most virions contained a single core but roughly one-third contained two or more cores. Consideration of the capsid protein concentration during core assembly indicated that core formation in vivo is template-mediated rather than concentration-driven. Although most cores were conical, 7% were tubular. These displayed a stacked-disc arrangement with 7-, 8-, 9- or 10-fold axial symmetry. Layer line filtration of these images showed that the capsid subunit arrangement is consistent with a 9.6 nm hexamer resembling that previously seen in the helical tubes assembled from purified capsid protein. A common reflection (1/3.2 nm) shared between the tubular and conical cores suggested they share a similar organization. The extraordinary flexibility observed in the assembly of the mature core appears to be well suited to accommodating variation and hence there may be no single structure for the infectious virion.
引用
收藏
页码:1707 / 1715
页数:9
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