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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[6] Use of T7 RNA polymerase to direct expression of cloned genes
Studier, F. W., Rosenberg, A. H., Dunn, J. J., & Dubendorff, J. W. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)85008-c · Cited by 6,562
Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
Studier, F. W., & Moffatt, B. A. (1986) · Journal of Molecular Biology · doi:10.1016/0022-2836(86)90385-2 · Cited by 6,385
Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone
Adachi, A., Gendelman, H. E., Koenig, S., Folks, T. M., Willey, R. L., Rabson, A. B., & Martín, M. Á. (1986) · Journal of Virology · doi:10.1128/jvi.59.2.284-291.1986 · Cited by 2,805
Construction of a retrovirus packaging mutant and its use to produce helper-free defective retrovirus
Mann, R., Mulligan, R. C., & Baltimore, D. (1983) · Cell · doi:10.1016/0092-8674(83)90344-6 · Cited by 1,776
Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P. (1996) · Cell · doi:10.1016/s0092-8674(00)81823-1 · Cited by 706
Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release
Göttlinger, H. G., Dorfman, T., Sodroski, J. G., & Haseltine, W. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.8.3195 · Cited by 647
p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease
Huang, M., Orenstein, J. M., Martin, M. A., & Freed, E. O. (1995) · Journal of Virology · doi:10.1128/jvi.69.11.6810-6818.1995 · Cited by 486
Structure of the Amino-Terminal Core Domain of the HIV-1 Capsid Protein
Gitti, R. K., Lee, B. M., Walker, J., Summers, M. F., Yoo, S., & Sundquist, W. I. (1996) · Science · doi:10.1126/science.273.5272.231 · Cited by 459
Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1
Campbell, S., & Vogt, V. M. (1995) · Journal of Virology · doi:10.1128/jvi.69.10.6487-6497.1995 · Cited by 350
Self-citation
Proteolytic refolding of the HIV‐1 capsid protein amino‐terminus facilitates viral core assembly
von Schwedler, U. K., Stemmler, T. L., Klishko, V. Y., Li, S., Albertine, K. H., Davis, D. R., & Sundquist, W. I. (1998) · The EMBO Journal · doi:10.1093/emboj/17.6.1555 · Cited by 337

Show all 59 references

Research works printed but not linked: 1

Ausubel F. M. Current protocols in molecular biology 1994 4.4.4 4.4.7 John Wiley & Sons Inc. New York N.Y

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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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