High-resolution structure of a retroviral capsid hexameric amino-terminal domain
Abstract
Retroviruses are the aetiological agents of a range of human diseases including AIDS and T-cell leukaemias. They follow complex life cycles, which are still only partly understood at the molecular level. Maturation of newly formed retroviral particles is an essential step in production of infectious virions, and requires proteolytic cleavage of Gag polyproteins in the immature particle to form the matrix, capsid and nucleocapsid proteins present in the mature virion. Capsid proteins associate to form a dense viral core that may be spherical, cylindrical or conical depending on the genus of the virus. Nonetheless, these assemblies all appear to be composed of a lattice formed from hexagonal rings, each containing six capsid monomers. Here, we describe the X-ray structure of an individual hexagonal assembly from N-tropic murine leukaemia virus (N-MLV). The interface between capsid monomers is generally polar, consistent with weak interactions within the hexamer. Similar architectures are probably crucial for the regulation of capsid assembly and disassembly in all retroviruses. Together, these observations provide new insights into retroviral uncoating and how cellular restriction factors may interfere with viral replication.
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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 [11]
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- Authors
- Mortuza, G. B., Haire, L. F., Stevens, A., Smerdon, S. J., Stoye, J. P., & Taylor, I. A.
- Affiliations
- National Institute for Medical Research (GB)
- Corresponding author
- Taylor, Ian A.
- Venue
- Nature
- Published
- 2004-09-23
- Volume
- 431
- Issue
- 7007
- Pages
- 481-485
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2055643881
- Cited by
- 185
- References
- 29
- Citations by year
- 2025: 2 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 3 · 2019: 4 · 2018: 5 · 2017: 4 · 2016: 8 · 2015: 7 · 2014: 8 · 2013: 11 · 2012: 15
- FWCI
- 6.12
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Science and Technology Facilities Council (submittedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- retroviral capsid, N-terminal domain, capsid assembly, capsid disassembly, viral uncoating, Gag protein, capsid lattice, cellular restriction factors, viral replication
- MeSH terms
- Amino Acid Sequence, Binding Sites, Capsid, Models, Molecular, Molecular Sequence Data, Leukemia Virus, Murine, Protein Structure, Tertiary, Crystallography, X-Ray, Virus Assembly, Protein Structure, Quaternary, Capsid Proteins
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