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

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In Vitro Assembly Properties of Human Immunodeficiency Virus Type 1 Gag Protein Lacking the p6 Domain

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

DOI 10.1128/jvi.73.3.2270-2279.1999PMC PMC104472

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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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Authors: Campbell, S., & Rein, A.
Affiliations: Frederick National Laboratory for Cancer Research (US)
ORCID: Rein, Alan
Venue: Journal of Virology
Publisher: American Society for Microbiology
Published: 1999-03
Volume: 73
Issue: 3
Pages: 2270-2279
ISSN: 0022-538X (ISSN-L)
1098-5514
DOI: 10.1128/jvi.73.3.2270-2279.1999
PMC: PMC104472
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: bronze
doi.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
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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In Vitro Assembly Properties of Human Immunodeficiency Virus Type 1 Gag Protein Lacking the p6 Domain

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