Cited by 293HIV Research and TreatmentT-cell and Retrovirus StudiesHIV/AIDS drug development and treatment

In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain

Open access
Campbell, Stephen, Rein, Alan·1999·Journal of Virology

Abstract

Human immunodeficiency virus type 1 (HIV-1) normally assembles into particles of 100 to 120 nm in diameter by budding through the plasma membrane of the cell. The Gag polyprotein is the only viral protein that is required for the formation of these particles. We have used an in vitro assembly system to examine the assembly properties of purified, recombinant HIV-1 Gag protein and of Gag missing the C-terminal p6 domain (Gag Deltap6). This system was used previously to show that the CA-NC fragment of HIV-1 Gag assembled into cylindrical particles. We now report that both HIV-1 Gag and Gag Deltap6 assemble into small, 25- to 30-nm-diameter spherical particles in vitro. The multimerization of Gag Deltap6 into units larger than dimers and the formation of spherical particles required nucleic acid. Removal of the nucleic acid with NaCl or nucleases resulted in the disruption of the multimerized complexes. We conclude from these results that (i) N-terminal extension of HIV-1 CA-NC to include the MA domain results in the formation of spherical, rather than cylindrical, particles; (ii) nucleic acid is required for the assembly and maintenance of HIV-1 Gag Deltap6 virus-like particles in vitro and possibly in vivo; (iii) a wide variety of RNAs or even short DNA oligonucleotides will support assembly; (iv) protein-protein interactions within the particle must be relatively weak; and (v) recombinant HIV-1 Gag Deltap6 and nucleic acid are not sufficient for the formation of normal-sized…

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Crossref · 10.1128/jvi.73.3.2270-2279.1999

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Authors
Campbell, S., & Rein, A.
Affiliations
Frederick National Laboratory for Cancer Research (US)
Venue
Journal of Virology
Published
1999-03
Volume
73
Issue
3
Pages
2270-2279
ISSN
  • 0022-538X (ISSN-L)
  • 1098-5514
OpenAlex
W2141194382
Cited by
293
References
59
Citations by year
2026: 5 · 2025: 2 · 2024: 8 · 2023: 3 · 2022: 8 · 2021: 9 · 2020: 5 · 2019: 10 · 2018: 12 · 2017: 15 · 2016: 14 · 2015: 6 · 2014: 13 · 2013: 12 · 2012: 18
FWCI
3.95
Type
journal article
Language
en
Open access
Locations
  • Journal of Virology (publishedVersion)
  • PubMed Central (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • U.S. Department of Health and Human Services
  • National Cancer Institute
Topics
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
  • Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
Keywords
HIV-1 Gag protein, viral assembly, virus-like particles, spherical particles, Gag multimerization, protein-protein interaction
MeSH terms
Escherichia coli, Microscopy, Electron, Recombinant Proteins, Ribonucleases, RNA, Viral, Sodium Chloride, HIV-1, Gene Products, gag, Virus Assembly

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