Structure and assembly of immature HIV

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 subtomo...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 106; no. 27; pp. 11090 - 11095
Main Authors Briggs, J.A.G, Riches, J.D, Glass, B, Bartonova, V, Zanetti, G, Kräusslich, H.-G
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 07.07.2009
National Acad Sciences
Subjects
Biological Sciences
Capsid
Capsid - chemistry
Cell Line
Crystal lattices
Crystal structure
Curvature
Dimerization
Dimers
gag Gene Products, Human Immunodeficiency Virus - chemistry
Gag protein
HIV
HIV 1
HIV-1 - chemistry
HIV-1 - physiology
Human immunodeficiency virus
Humans
Mathematical lattices
Models, Molecular
Molecular structure
polyproteins
Protein Structure, Tertiary
Proteins
Self-assembly
Studies
Tomography
Transformation
Virion - chemistry
Virions
Virus Assembly
Viruses
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Summary: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 [almost equal 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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Edited by John M. Coffin, Tufts University School of Medicine, Boston, MA, and approved May 19, 2009
Author contributions: J.A.G.B. and H.-G.K. designed research; J.A.G.B., J.D.R., B.G., and V.B. performed research; G.Z. contributed new reagents/analytic tools; J.A.G.B. and J.D.R. analyzed data; and J.A.G.B. and H.-G.K. wrote the paper.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0903535106