ArticleJournal of virology2013
A carboxy-terminally truncated human CPSF6 lacking residues encoded by exon 6 inhibits HIV-1 cDNA synthesis and promotes capsid disassembly.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 51 citations in OpenAlex.
- Intragenic viral silencer element regulates HTLV-1 latency via RUNX complex recruitment.Nature microbiology · 2025Article
- CPSF6 promotes HIV-1 preintegration complex function.Journal of virology · 2025Article
- The nuclear localization signal of CPSF6 governs post-nuclear import steps of HIV-1 infection.PLoS pathogens · 2025Article
- HIV-1 usurps mixed-charge domain-dependent CPSF6 phase separation for higher-order capsid binding, nuclear entry and viral DNA integration.Nucleic acids research · 2024Article
- HIV-Tocky system to visualize proviral expression dynamics.Communications biology · 2024Article
- Cell Type-Dependent Escape of Capsid Inhibitors by Simian Immunodeficiency Virus SIVcpz.Journal of virology · 2020Article
- Human Immunodeficiency Virus 1 (HIV-1): Viral Latency, the Reservoir, and the Cure.The Yale journal of biology and medicine · 2020Review
- TNPO3-Mediated Nuclear Entry of the Rous Sarcoma Virus Gag Protein Is Independent of the Cargo-Binding Domain.Journal of virology · 2020Article
- Differential role for phosphorylation in alternative polyadenylation function versus nuclear import of SR-like protein CPSF6.Nucleic acids research · 2019Article
- HIV-1 nuclear import in macrophages is regulated by CPSF6-capsid interactions at the nuclear pore complex.eLife · 2019Article
- Nuclear pore heterogeneity influences HIV-1 infection and the antiviral activity of MX2.eLife · 2018Article
- Cellular and molecular mechanisms of HIV-1 integration targeting.Cellular and molecular life sciences : CMLS · 2018Review
- Truncated CPSF6 Forms Higher-Order Complexes That Bind and Disrupt HIV-1 Capsid.Journal of virology · 2018Article
- Capsid-Dependent Host Factors in HIV-1 Infection.Trends in microbiology · 2017Review
- Phosphorylation of the HIV-1 capsid by MELK triggers uncoating to promote viral cDNA synthesis.PLoS pathogens · 2017Article
- N-terminal half of transportin SR2 interacts with HIV integrase.The Journal of biological chemistry · 2017Article
- N-terminally truncated POM121C inhibits HIV-1 replication.PloS one · 2017Article
- Contributions of Charged Residues in Structurally Dynamic Capsid Surface Loops to Rous Sarcoma Virus Assembly.Journal of virology · 2016Article
- The Cleavage and Polyadenylation Specificity Factor 6 (CPSF6) Subunit of the Capsid-recruited Pre-messenger RNA Cleavage Factor I (CFIm) Complex Mediates HIV-1 Integration into Genes.The Journal of biological chemistry · 2016Article
- SUN2 Overexpression Deforms Nuclear Shape and Inhibits HIV.Journal of virology · 2016Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Since HIV-1 replication is modulated at multiple stages by host cell factors, identification and characterization of those host cell factors are expected to contribute to the development of novel anti-HIV therapeutics. Previous studies showed that a C-terminally truncated cytosolic form of cleavage and polyadenylation-specific factor 6 (CPSF6-358) inhibits HIV-1 infection through interference with HIV-1 trafficking to the nucleus. Here we identified and characterized a different configuration of C-terminally truncated human CPSF6 (hCPSF6-375) through cDNA expression cloning coupled with ganciclovir-mediated lethal selection. Notably, hCPSF6-375, but not mouse CPSF6-358 (mCPSF6-358) as previously reported, remarkably interfered with viral cDNA synthesis after HIV-1 infection. Moreover, we found that hCPSF6-375 aberrantly accelerated the disassembly of the viral capsid in target cells, while CPSF6-358 did not. Sequence comparison of CPSF6-375 and CPSF6-358 cDNAs showed a lack of exon 6 and additional coding sequence for 54 amino acid residues in the C terminus of hCPSF6-375. Mutational analyses revealed that the residues encoded by exon 6, but not the C-terminal 54 residues in hCPSF6-375, is responsible for impaired viral cDNA synthesis by hCPSF6-375. This is the first report demonstrating a novel mode of HIV-1 inhibition by truncated forms of CPSF6 that involves rapid capsid disassembly and inhibition of viral cDNA synthesis. These findings could facilitate an increased understanding of viral cDNA synthesis in light of the viral capsid disassembly.
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