Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography
Abstract
Retroviral capsids in their native form: Capsid proteins of retroviruses form protective lattices around viral RNA molecules. The precise molecular details of how individual, full-length capsid proteins assemble to shield the viral genome; however, are not well understood. Obal et al. and Gres et al. now report high resolution crystal structures of the full length capsid proteins from Bovine Leukemia Virus and HIV-1, respectively. The two studies complement each other to reveal the dynamic nature of capsid protein assembly and of how individual capsid proteins interact in the lattice. The findings may have relevance for drug design. Science , this issue p. 95 ; see also p. 99
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The variable local curvatures of the hexameric CA lattice require considerable structural flexibility of the CA lattice, which has been suggested to be accommodated by the flexible linker between CA-NTD and CA-CTD, by rotations around the dimeric CA-CTD interface, and by structural changes at the trimeric CA-CTD interface.
“This requires considerable structural flexibility of the CA lattice that has been suggested to be accommodated by the flexible linker between CA-NTD and CA-CTD [44,45 ], by rotations around the dimeric CA-CTD interface [43 ], and by structural changes at the trimeric CA-CTD interface”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [46]
While in-virus structures are currently lacking, in vitro studies indicate that the arrangement of CA in mature retroviruses is well conserved.
“While in-virus structures are currently lacking, these in vitro studies indicate that the arrangement of CA in mature retroviruses is well conserved”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [46]
In HIV, six CA-NTDs form a hexameric ring with a central 18 helix bundle formed by helices 1, 2, and 3, providing the main intrahexamer stability.
“In HIV six CA-NTDs form a hexameric ring with a central 18 helix bundle formed by helices 1, 2, and 3, providing the main intrahexamer stability”
From Retrovirus maturation-an extraordinary structural transformation (2016) · cites this paper as [46]
Cites
Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
Gamble, T. R., Yoo, S., Vajdos, F. F., von Schwedler, U. K., Worthylake, D. K., Wang, H., McCutcheon, J. P., Sundquist, W. I., & Hill, C. P. (1997) · Science · doi:10.1126/science.278.5339.849 · Cited by 598 · see citing works
Structure of Full-Length HIV-1 CA: A Model for the Mature Capsid Lattice
Ganser-Pornillos, B. K., Cheng, A., & Yeager, M. (2007) · Cell · doi:10.1016/j.cell.2007.08.018 · Cited by 321 · see citing works
Assembly Properties of the Human Immunodeficiency Virus Type 1 CA Protein
Ganser-Pornillos, B. K., von Schwedler, U. K., Stray, K. M., Aiken, C., & Sundquist, W. I. (2004) · Journal of Virology · doi:10.1128/jvi.78.5.2545-2552.2004 · Cited by 302 · see citing works
Price, A. J., Jacques, D. A., McEwan, W. A., Fletcher, A. J., Essig, S., Chin, J. W., Halambage, U. D., Aiken, C., & James, L. C. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004459 · Cited by 284 · see citing works
Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution
Worthylake, D. K., Wang, H., Yoo, S., Sundquist, W. I., & Hill, C. P. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998007689 · Cited by 235 · see citing works
Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
Tang, C., Ndassa, Y., & Summers, M. F. (2002) · Nature Structural Biology · doi:10.1038/nsb806 · Cited by 205 · see citing works
High-resolution structure of a retroviral capsid hexameric amino-terminal domain
Mortuza, G. B., Haire, L. F., Stevens, A., Smerdon, S. J., Stoye, J. P., & Taylor, I. A. (2004) · Nature · doi:10.1038/nature02915 · Cited by 185 · see citing works
Campos-Olivas, R., Newman, J. L., & Summers, M. F. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3475 · Cited by 119 · see citing works
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Retrovirus maturation-an extraordinary structural transformation
Mattei, S., Schur, F. K., & Briggs, J. A. (2016) · Current Opinion in Virology · doi:10.1016/j.coviro.2016.02.008 · Cited by 72 · see citing works
“In HIV six CA-NTDs form a hexameric ring with a central 18 helix bundle formed by helices 1, 2, and 3, providing the main intrahexamer stability [44,45 ,46 ,52].”
Background
- Authors
- Obal, G., Trajtenberg, F., Carrión, F., Tomé, L., Larrieux, N., Zhang, X., Pritsch, O., & Buschiazzo, A.
- Affiliations
- Universidad de la República de Uruguay (UY)
- Institut Pasteur de Montevideo (UY)
- Institut Pasteur de Montevideo, Unit of Protein Biophysics, Mataojo 2020, 11400, Montevideo, Uruguay.
- Centre National de la Recherche Scientifique (FR)
- Institut Pasteur (FR)
- Corresponding author
- Obal, G.
- Trajtenberg, F.
- Pritsch, O.
- Buschiazzo, A.
- Venue
- Science
- Published
- 2015-07-03
- Volume
- 349
- Issue
- 6243
- Pages
- 95-98
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1925820368
- Cited by
- 39
- References
- 8
- Citations by year
- 2025: 3 · 2024: 1 · 2022: 4 · 2021: 3 · 2020: 4 · 2019: 4 · 2018: 4 · 2017: 4 · 2016: 9 · 2015: 3
- FWCI
- 2.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Keywords
- bovine leukemia virus, capsid self-assembly, conformational plasticity, capsid lattice, dimer interface, long-range interactions
- MeSH terms
- Amino Acid Sequence, Animals, Leukemia Virus, Bovine, Capsid, Cattle, Molecular Sequence Data, Mutation, Protein Structure, Secondary, Crystallography, X-Ray, Capsid Proteins, Protein Multimerization
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