The stoichiometry of Gag protein in HIV-1
Abstract
The major structural components of HIV-1 are encoded as a single polyprotein, Gag, which is sufficient for virus particle assembly. Initially, Gag forms an approximately spherical shell underlying the membrane of the immature particle. After proteolytic maturation of Gag, the capsid (CA) domain of Gag reforms into a conical shell enclosing the RNA genome. This mature shell contains 1,000-1,500 CA proteins assembled into a hexameric lattice with a spacing of 10 nm. By contrast, little is known about the structure of the immature virus. We used cryo-EM and scanning transmission EM to determine that an average (145 nm diameter) complete immature HIV particle contains approximately 5,000 structural (Gag) proteins, more than twice the number from previous estimates. In the immature virus, Gag forms a hexameric lattice with a spacing of 8.0 nm. Thus, less than half of the CA proteins form the mature core.
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The mature CA lattice has a hexamer-hexamer spacing larger than that seen in the immature virus particle.
“The mature CA lattice has a hexamer-hexamer spacing larger than that seen in the immature virus particle”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [51]
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- Authors
- Briggs, J. A. G., Simon, M. N., Gross, I., Kräusslich, H.-G., Fuller, S. D., Vogt, V. M., & Johnson, M. C.
- Affiliations
- Centre for Human Genetics (GB)
- Brookhaven National Laboratory (US)
- Cornell University (US)
- Heidelberg University (DE)
- Corresponding author
- Johnson, Marc C
- Venue
- Nature Structural & Molecular Biology
- Published
- 2004-06-20
- Volume
- 11
- Issue
- 7
- Pages
- 672-675
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W1986015062
- Cited by
- 539
- References
- 3
- Citations by year
- 2026: 15 · 2025: 11 · 2024: 18 · 2023: 10 · 2022: 19 · 2021: 25 · 2020: 25 · 2019: 18 · 2018: 18 · 2017: 23 · 2016: 21 · 2015: 22 · 2014: 30 · 2013: 28 · 2012: 44
- FWCI
- 10.06
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Center for Research Resources (P41-RR01777, P41RR001777)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Keywords
- HIV-1, Gag protein, capsid protein, viral assembly, stoichiometry, proteolytic maturation, cryo-electron microscopy, scanning transmission electron microscopy
- MeSH terms
- Microscopy, Electron, Scanning, HIV-1, Gene Products, gag, Cryoelectron Microscopy
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