ArticleJournal of virology2000
Role of Vif in stability of the human immunodeficiency virus type 1 core.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
32 citing papers in PubMed, 1 synthesis or guideline pooled it, 74 citations in OpenAlex.
- HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016Pooled it
- Requirements for nucleocapsid-mediated regulation of reverse transcription during the late steps of HIV-1 assembly.Scientific reports · 2016Article
- HIV-1 Capsid Stabilization Assay.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Identification and characterization of a new type of inhibitor against the human immunodeficiency virus type-1 nucleocapsid protein.Retrovirology · 2015Article
- Differential contribution of basic residues to HIV-1 nucleocapsid protein's nucleic acid chaperone function and retroviral replication.Nucleic acids research · 2014Article
- Human cytosolic extracts stabilize the HIV-1 core.Journal of virology · 2013Article
- Review
- A carboxy-terminally truncated human CPSF6 lacking residues encoded by exon 6 inhibits HIV-1 cDNA synthesis and promotes capsid disassembly.Journal of virology · 2013Article
- Inhibition of reverse transcriptase activity increases stability of the HIV-1 core.Journal of virology · 2013Article
- RING domain mutations uncouple TRIM5α restriction of HIV-1 from inhibition of reverse transcription and acceleration of uncoating.Journal of virology · 2012Article
- Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 Vif.Nucleic acids research · 2011Article
- Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase.Nucleic acids research · 2009Article
- Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors.Microbiology and molecular biology reviews : MMBR · 2009Review
- APOBEC3G inhibits elongation of HIV-1 reverse transcripts.PLoS pathogens · 2008Article
- The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G.Retrovirology · 2007Article
- Isolated HIV-1 core is active for reverse transcription.Retrovirology · 2007Article
- Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription.Nucleic acids research · 2007Article
- Simultaneous mutations in CA and Vif of Maedi-Visna virus cause attenuated replication in macrophages and reduced infectivity in vivo.Journal of virology · 2005Article
- A human immunodeficiency virus type 1 protease biosensor assay using bioluminescence resonance energy transfer.Journal of virological methods · 2005Article
- Vif is an auxiliary factor of the HIV-1 reverse transcriptase and facilitates abasic site bypass.The Biochemical journal · 2004Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Vif protein of human immunodeficiency virus type 1 (HIV-1) is important for virion infectivity. Previous studies have shown that vif-defective virions exhibit structural abnormalities in the virus core and are defective in the ability to complete proviral DNA synthesis in acutely infected cells. We developed novel assays to assess the relative stability of the core in HIV-1 virions. Using these assays, we examined the role of Vif in the stability of the HIV-1 core. The integrity of the core was examined following virion permeabilization or removal of the lipid envelope and treatment with various triggers, including S100 cytosol, deoxynucleoside triphosphates, detergents, NaCl, and buffers of different pH to mimic aspects of the uncoating and disassembly process which occurs after virus entry but preceding or during reverse transcription. vif mutant cores were more sensitive to disruption by all triggers tested than wild-type cores, as determined by endogenous reverse transcriptase (RT) assays, biochemical analyses, and electron microscopy. RT and the p7 nucleocapsid protein were released more readily from vif mutant virions than from wild-type virions, suggesting that the internal nucleocapsid is less stably packaged in the absence of Vif. Purified cores could be isolated from wild-type but not vif mutant virions by sedimentation through detergent-treated gradients. These results demonstrate that Vif increases the stability of virion cores. This may permit efficient viral DNA synthesis by preventing premature degradation or disassembly of viral nucleoprotein complexes during early events after virus entry.
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