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Cryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly
Open accessAbstract
Significance: HIV-1 undergoes a two-step assembly process. First, an immature noninfectious particle is assembled, which leaves the infected cell. Second, the structural protein, Gag, is cleaved in the virus by the viral protease, and this leads to formation of the infectious virus. The immature virus particle therefore represents the key intermediate in HIV-1 assembly. There is currently no high-resolution information available on the arrangement of Gag within immature HIV-1. We have assembled part of HIV-1 Gag in vitro to form immature virus-like tubular protein arrays, and have solved a subnanometer-resolution structure of these arrays by using cryo-EM and tomography. This structure reveals interactions of the C-terminal capsid domain of Gag that are critical for HIV-1 assembly.
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“Secondly, a mutated HIV-1 CANC construct has been shown to assemble arrays in vitro in which the CA-CTD arrangement matches that seen in native immature HIV-1 virus particles, while the CA-NTD adopts an arrangement that would be unable to form a hexameric lattice in spherical virions”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [37]
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Cites
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 46,047
HIV-1 Antiretroviral Drug TherapyPreprint
Arts, E. J., & Hazuda, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a007161 · Cited by 949
Flexible Fitting of Atomic Structures into Electron Microscopy Maps Using Molecular Dynamics
Trabuco, L. G., Villa, E., Mitra, K., Frank, J., & Schulten, K. J. (2008) · Structure · doi:10.1016/j.str.2008.03.005 · Cited by 866
HIV-1 assembly, budding, and maturation
Sundquist, W. I., & Krausslich, H.-G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006924 · Cited by 814
Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics
Zhao, G., Perilla, J. R., Yufenyuy, E. L., Meng, X., Chen, B., Ning, J., Ahn, J., Gronenborn, A. M., Schulten, K., Aiken, C., et al. (2013) · Nature · doi:10.1038/nature12162 · Cited by 801
The stoichiometry of Gag protein in HIV-1
Briggs, J. A. G., Simon, M. N., Gross, I., Kräusslich, H.-G., Fuller, S. D., Vogt, V. M., & Johnson, M. C. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb785 · Cited by 539
Self-citationX-Ray Structures of the Hexameric Building Block of the HIV Capsid
Pornillos, O., Ganser-Pornillos, B. K., Kelly, B. N., Hua, Y., Whitby, F. G., Stout, C. D., Sundquist, W. I., Hill, C. P., & Yeager, M. (2009) · Cell · doi:10.1016/j.cell.2009.04.063 · Cited by 523
Synthesis, Assembly, and Processing of Viral Proteins
Swanstrom, R. I., & Wills, J. (1997) · Europe PMC (PubMed Central) · Cited by 518
Image reconstructions of helical assemblies of the HIV-1 CA protein
Li, S., Hill, C. P., Sundquist, W. I., & Finch, J. T. (2000) · Nature · doi:10.1038/35030177 · Cited by 500
Atomic-level modelling of the HIV capsid
Pornillos, O., Ganser-Pornillos, B. K., & Yeager, M. (2011) · Nature · doi:10.1038/nature09640 · Cited by 372
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Manocheewa, S., Mittler, J. E., Samudrala, R., & Mullins, J. I. (2015) · Viruses · doi:10.3390/v7112901 · Cited by 9
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Fender, P., Moriscot, C., Ruigrok, R. W. H., & Schoehn, G. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.02563-0 · Cited by 3
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Metadata
- Authors
- Bharat, T. A. M., Castillo Menendez, L. R., Hagen, W. J. H., Lux, V., Igonet, S., Schorb, M., Schur, F. K. M., Kräusslich, H.-G., & Briggs, J. A. G.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Molecular Medicine Partnership Unit, European Molecular Biology Laboratory/Universitätsklinikum Heidelberg, Heidelberg, Germany;
- European Molecular Biology Laboratory (DE)
- University Hospital Heidelberg (DE)
- Unité de Virologie Structurale, Departement Virologie, Institut Pasteur, 75724 Paris, France; and
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-05-19
- Volume
- 111
- Issue
- 22
- Pages
- 8233-8238
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4050629
- OpenAlex
- W1994410560
- Cited by
- 107
- References
- 44
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 6 · 2023: 9 · 2022: 7 · 2021: 10 · 2020: 6 · 2019: 11 · 2018: 6 · 2017: 4 · 2016: 16 · 2015: 20 · 2014: 5
- FWCI
- 6.69
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Molecular Biology Laboratory
- Deutsche Forschungsgemeinschaft (KR 906/7-1, BR 3635/2-1)
- 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 › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- HIV-1 Gag, capsid protein, six-helix bundle, Mason-Pfizer monkey virus, retroviral assembly
- MeSH terms
- Virion, HIV-1, Protein Structure, Secondary, Protein Structure, Tertiary, Crystallography, X-Ray, Cryoelectron Microscopy, Capsid Proteins, Nanotubes, gag Gene Products, Human Immunodeficiency Virus
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