Electron cryotomography of immature HIV‐1 virions reveals the structure of the CA and SP1 Gag shells
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The major structural elements of retroviruses are contained in a single polyprotein, Gag, which in human immunodeficiency virus type 1 (HIV-1) comprises the MA, CA, spacer peptide 1 (SP1), NC, SP2, and p6 polypeptides. In the immature HIV-1 virion, the domains of Gag are arranged radially with the N-terminal MA domain at the membrane and C-terminal NC-SP2-p6 region nearest to the center. Here, we report the three-dimensional structures of individual immature HIV-1 virions, as obtained by electron cryotomography. The concentric shells of the Gag polyprotein are clearly visible, and radial projections of the different Gag layers reveal patches of hexagonal order within the CA and SP1 shells. Averaging well-ordered unit cells leads to a model in which each CA hexamer is stabilized by a bundle of six SP1 helices. This model suggests why the SP1 spacer is essential for assembly of the Gag lattice and how cleavage between SP1 and CA acts as a structural switch controlling maturation.
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Early cryo-ET and subtomogram averaging work revealed that the immature HIV-1 Gag lattice within virus particles adopts a wide range of curvatures and incorporates regions where no ordered Gag protein is seen.
“Early cryo-ET and subtomogram averaging work revealed that the immature HIV-1 Gag lattice within virus particles adopts a wide range of curvatures and incorporates regions where no ordered Gag protein is seen [24].”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [24]
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Cites
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“MA is cotranslationally myristoylated and serves to anchor Gag to the membrane ( Massiah et al, 1994; Hill et al, 1996; Saad et al, 2006).”
Self-citationStructures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution
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- Authors
- Wright, E. R., Schooler, J. B., Ding, H. J., Kieffer, C., Fillmore, C., Sundquist, W. I., & Jensen, G. J.
- Affiliations
- California Institute of Technology (US)
- University of Utah (US)
- Corresponding author
- Jensen, Grant J
- ORCID
- Venue
- The EMBO Journal
- Published
- 2007-03-29
- Volume
- 26
- Issue
- 8
- Pages
- 2218-2226
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC1852790
- OpenAlex
- W2152539875
- Cited by
- 325
- References
- 9
- Citations by year
- 2026: 8 · 2025: 6 · 2024: 12 · 2023: 12 · 2022: 9 · 2021: 14 · 2020: 14 · 2019: 9 · 2018: 12 · 2017: 13 · 2016: 18 · 2015: 19 · 2014: 21 · 2013: 22 · 2012: 29
- FWCI
- 19.85
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- Gordon and Betty Moore Foundation
- Ralph M. Parsons Foundation
- National Institutes of Health
- U.S. Public Health Service (A145405)
- Beckman Institute, California Institute of Technology
- National Institute of General Medical Sciences (P01 GM66521, P50GM082545, P01GM066521, F32GM075543)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Keywords
- HIV-1, immature virions, Gag protein, retroviral assembly, virion maturation, hexagonal order, three-dimensional structure
- MeSH terms
- Models, Molecular, Peptides, Tomography, Virion, HIV-1, Gene Products, gag, Capsid Proteins
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