Cited by 186HIV Research and TreatmentT-cell and Retrovirus StudiesEnzyme Structure and Function

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High-resolution structure of a retroviral capsid hexameric amino-terminal domain

Mortuza, Gulnahar B., Haire, Lesley F., Stevens, Anthony, Smerdon, Stephen J., Stoye, Jonathan P., Taylor, Ian A.·2004·Nature

DOI 10.1038/nature02915

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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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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.
ORCID: Mortuza, Gulnahar B.
Smerdon, Stephen J.
Stoye, Jonathan P.
Taylor, Ian A.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2004-09-23
Volume: 431
Issue: 7007
Pages: 481-485
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature02915
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
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › 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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High-resolution structure of a retroviral capsid hexameric amino-terminal domain

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