Cited by 671HIV Research and TreatmentT-cell and Retrovirus StudiesAdvanced Electron Microscopy Techniques and Applications

Assembly and Analysis of Conical Models for the HIV-1 Core

Ganser, Barbie K., Li, Su, Klishko, Victor Y., Finch, John T., Sundquist, Wesley I.·1999·Science

Abstract

The genome of the human immunodeficiency virus (HIV) is packaged within an unusual conical core particle located at the center of the infectious virion. The core is composed of a complex of the NC (nucleocapsid) protein and genomic RNA, surrounded by a shell of the CA (capsid) protein. A method was developed for assembling cones in vitro using pure recombinant HIV-1 CA-NC fusion proteins and RNA templates. These synthetic cores are capped at both ends and appear similar in size and morphology to authentic viral cores. It is proposed that both viral and synthetic cores are organized on conical hexagonal lattices, which by Euler's theorem requires quantization of their cone angles. Electron microscopic analyses revealed that the cone angles of synthetic cores were indeed quantized into the five allowed angles. The viral core and most synthetic cones exhibited cone angles of approximately 19 degrees (the narrowest of the allowed angles). These observations suggest that the core of HIV is organized on the principles of a fullerene cone, in analogy to structures recently observed for elemental carbon.

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Crossref · 10.1126/science.283.5398.80

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1 of 1 references verified0 citation errors · 0 not checkable

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  • The retroviral mature CA core is pleomorphic and has been proposed to be a fullerene structure in which a hexameric lattice is closed by the incorporation of 12 pentameric Gag assemblies.

    “The retroviral mature CA core is pleomorphic and has been proposed to be a fullerene structure in which a hexameric lattice is closed by the incorporation of 12 pentameric Gag assemblies”
  • According to the fullerene model of the core, forming a closed structure from a hexameric lattice requires the incorporation of 12 pentamers.

    “According to the fullerene model of the core, forming a closed structure from a hexameric lattice requires the incorporation of 12 pentamers”
  • The cores are typically conical in HIV (5 pentamers at the tip and 7 at the base), tubular in M-PMV (6 pentamers at each end), and polyhedral in RSV and MLV (12 pentamers homogenously distributed).

    “The cores are typically conical in HIV (5 pentamers at the tip and 7 at the base), tubular in M-PMV (6 pentamers at each end), and polyhedral in RSV and MLV (12 pentamers homogenously distributed).”
  • CA can be induced to assemble in vitro into conical structures with some similarity to the viral core.

    “CA can be induced to assemble in vitro into conical structures with some similarity to the viral core [41].”

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Authors
Ganser, B. K., Li, S., Klishko, V. Y., Finch, J. T., & Sundquist, W. I.
Affiliations
MRC Laboratory of Molecular Biology (GB)
Corresponding author
  • Ganser, Barbie K.
  • Li, Su
  • Sundquist, Wesley I.
Venue
Science
Published
1999-01
Volume
283
Issue
5398
Pages
80-83
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2061714407
Cited by
671
References
1
Citations by year
2026: 13 · 2025: 31 · 2024: 24 · 2023: 28 · 2022: 17 · 2021: 30 · 2020: 32 · 2019: 26 · 2018: 20 · 2017: 18 · 2016: 31 · 2015: 30 · 2014: 27 · 2013: 41 · 2012: 34
FWCI
4.74
Type
journal article
Language
en
Open access
closed
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
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 › Advanced Electron Microscopy Techniques and Applications
Keywords
HIV-1 core, capsid protein, nucleocapsid protein, Euler's theorem, viral assembly
MeSH terms
Capsid, Mathematics, Microscopy, Electron, Models, Biological, Recombinant Fusion Proteins, RNA, Viral, Templates, Genetic, HIV-1, Gene Products, gag, Nucleocapsid

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