Analysis of HIV particle formation using transient expression of subviral constructs in mammalian cells - PubMed (original) (raw)
Analysis of HIV particle formation using transient expression of subviral constructs in mammalian cells
K Mergener et al. Virology. 1992 Jan.
Abstract
Segments of the human immunodeficiency virus (HIV) type 1 gag and pol genes and mutants thereof were transiently expressed in mammalian cells. Expression was dependent on the presence of the rev responsive element in cis and the rev protein in trans and was readily detected by indirect immunofluorescence or Western blotting. Transfection of constructs encoding the entire gag and pol open reading frames yielded efficient release of particles banding at a density of 1.16 g of sucrose per milliliter and consisting mainly of processed gag proteins. In addition, these particles contained the p66/p51 heterodimer of reverse transcriptase (RT), had associated RT activity, and contained RNA. Electron micrographs revealed immature retrovirus-like particles budding primarily from the plasma membrane and extracellular particles with morphological characteristics of HIV. Particle production was independent of the pol open reading frame or an active HIV proteinase (PR) but without active PR, cell-associated and particle-associated proteins remained completely uncleaved and budding occurred primarily into intracellular vacuoles. A mutation preventing myristoylation of the viral polyproteins abolished particle release but did not interfere with polyprotein synthesis and did not prevent processing. Expression of gag and PR in the same reading frame yielded complete processing of polyproteins but no budding and led to increased cell toxicity. A mutation of the PR active site in this construct prevented cytotoxicity and restored particle release indicating that the observed phenotype was caused by the overexpression of PR. These particles were aberrant in size and morphology when analyzed on sucrose density gradients and by electron microscopy. Budding was arrested at an early stage and extracellular particles appeared to be released by a different mechanism. Only short C-terminal extensions were compatible with this release mechanism since expression of a similar mutant construct encoding the entire gag-pol open reading frame did not yield particles.
Similar articles
- Analysis of protein expression and virus-like particle formation in mammalian cell lines stably expressing HIV-1 gag and env gene products with or without active HIV proteinase.
Kräusslich HG, Ochsenbauer C, Traenckner AM, Mergener K, Fäcke M, Gelderblom HR, Bosch V. Kräusslich HG, et al. Virology. 1993 Feb;192(2):605-17. doi: 10.1006/viro.1993.1077. Virology. 1993. PMID: 8421902 - Overexpression of the HIV-1 gag-pol polyprotein results in intracellular activation of HIV-1 protease and inhibition of assembly and budding of virus-like particles.
Karacostas V, Wolffe EJ, Nagashima K, Gonda MA, Moss B. Karacostas V, et al. Virology. 1993 Apr;193(2):661-71. doi: 10.1006/viro.1993.1174. Virology. 1993. PMID: 7681610 - Studies on processing, particle formation, and immunogenicity of the HIV-1 gag gene product: a possible component of a HIV vaccine.
Wagner R, Fliessbach H, Wanner G, Motz M, Niedrig M, Deby G, von Brunn A, Wolf H. Wagner R, et al. Arch Virol. 1992;127(1-4):117-37. doi: 10.1007/BF01309579. Arch Virol. 1992. PMID: 1456888 - The packaging and maturation of the HIV-1 Pol proteins.
Hill M, Tachedjian G, Mak J. Hill M, et al. Curr HIV Res. 2005 Jan;3(1):73-85. doi: 10.2174/1570162052772942. Curr HIV Res. 2005. PMID: 15638725 Review. - The life-cycle of human immunodeficiency virus type 1.
Goto T, Nakai M, Ikuta K. Goto T, et al. Micron. 1998 Apr-Jun;29(2-3):123-38. doi: 10.1016/s0968-4328(98)00002-x. Micron. 1998. PMID: 9684349 Review.
Cited by
- HIV-1 Gag targeting to the plasma membrane reorganizes sphingomyelin-rich and cholesterol-rich lipid domains.
Tomishige N, Bin Nasim M, Murate M, Pollet B, Didier P, Godet J, Richert L, Sako Y, Mély Y, Kobayashi T. Tomishige N, et al. Nat Commun. 2023 Nov 21;14(1):7353. doi: 10.1038/s41467-023-42994-w. Nat Commun. 2023. PMID: 37990014 Free PMC article. - Perturbing HIV-1 Ribosomal Frameshifting Frequency Reveals a cis Preference for Gag-Pol Incorporation into Assembling Virions.
Benner BE, Bruce JW, Kentala JR, Murray M, Becker JT, Garcia-Miranda P, Ahlquist P, Butcher SE, Sherer NM. Benner BE, et al. J Virol. 2022 Jan 12;96(1):e0134921. doi: 10.1128/JVI.01349-21. Epub 2021 Oct 13. J Virol. 2022. PMID: 34643428 Free PMC article. - Identification of host proteins differentially associated with HIV-1 RNA splice variants.
Knoener R, Evans E 3rd, Becker JT, Scalf M, Benner B, Sherer NM, Smith LM. Knoener R, et al. Elife. 2021 Feb 25;10:e62470. doi: 10.7554/eLife.62470. Elife. 2021. PMID: 33629952 Free PMC article. - Biochemical and proteomic characterization of retrovirus Gag based microparticles carrying melanoma antigens.
Kurg R, Reinsalu O, Jagur S, Õunap K, Võsa L, Kasvandik S, Padari K, Gildemann K, Ustav M. Kurg R, et al. Sci Rep. 2016 Jul 11;6:29425. doi: 10.1038/srep29425. Sci Rep. 2016. PMID: 27403717 Free PMC article. - Live-cell observation of cytosolic HIV-1 assembly onset reveals RNA-interacting Gag oligomers.
Hendrix J, Baumgärtel V, Schrimpf W, Ivanchenko S, Digman MA, Gratton E, Kräusslich HG, Müller B, Lamb DC. Hendrix J, et al. J Cell Biol. 2015 Aug 17;210(4):629-46. doi: 10.1083/jcb.201504006. J Cell Biol. 2015. PMID: 26283800 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Other Literature Sources
Research Materials