Abstract
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 ≈17-Å 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.
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Dates
Type | When |
---|---|
Created | 16 years, 2 months ago (June 22, 2009, 10:04 p.m.) |
Deposited | 3 years, 4 months ago (April 12, 2022, 6:16 p.m.) |
Indexed | 3 weeks, 5 days ago (Aug. 6, 2025, 9:48 a.m.) |
Issued | 16 years, 1 month ago (July 7, 2009) |
Published | 16 years, 1 month ago (July 7, 2009) |
Published Online | 16 years, 1 month ago (July 7, 2009) |
Published Print | 16 years, 1 month ago (July 7, 2009) |
@article{Briggs_2009, title={Structure and assembly of immature HIV}, volume={106}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0903535106}, DOI={10.1073/pnas.0903535106}, number={27}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Briggs, J. A. G. and Riches, J. D. and Glass, B. and Bartonova, V. and Zanetti, G. and Kräusslich, H.-G.}, year={2009}, month=jul, pages={11090–11095} }