ArticlePLoS pathogens2016
KIF5B and Nup358 Cooperatively Mediate the Nuclear Import of HIV-1 during Infection.
Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers, 1 of them a synthesis that pooled it.
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Who cites it
80 citing papers in PubMed, 1 synthesis or guideline pooled it, 123 citations in OpenAlex.
- Specialized DNA Structures Act as Genomic Beacons for Integration by Evolutionarily Diverse Retroviruses.Viruses · 2023Pooled it
- KIF18A knockdown enhances oxidative phosphorylation, suggesting a metabolic basis for antiviral activity against influenza A virus.Genes & genomics · 2026Article
- Proximity Ligation Assay: From a Foundational Principle to a Versatile Platform for Molecular and Translational Research.Biomolecules · 2025Review
- Microtubule remodeling by the innate immune factor Trim69 compromises dynein-dependent migration of HIV virion cores toward the nucleus.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- HIV capsids: orchestrators of innate immune evasion, pathogenesis and pandemicity.The Journal of general virology · 2025Review
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- Studying Retroviral Life Cycles Using Visible Viruses and Live Cell Imaging.Annual review of virology · 2024Review
- Review
- May I Help You with Your Coat? HIV-1 Capsid Uncoating and Reverse Transcription.International journal of molecular sciences · 2024Review
- Article
- The host cytoskeleton: a key regulator of early HIV-1 infection.The FEBS journal · 2024Review
- HIV-1 capsid shape, orientation, and entropic elasticity regulate translocation into the nuclear pore complex.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Characterization of Nuclear HIV-Induced Membraneless Organelles Through Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The nuclear pore protein NUP98 impedes LTR-driven basal gene expression of HIV-1, viral propagation, and infectivity.Frontiers in immunology · 2024Article
- Capsid-host interactions for HIV-1 ingress.Microbiology and molecular biology reviews : MMBR · 2023Review
- Emerging role of cyclophilin A in HIV-1 infection: from producer cell to the target cell nucleus.Journal of virology · 2023Review
- HIV Infection: Shaping the Complex, Dynamic, and Interconnected Network of the Cytoskeleton.International journal of molecular sciences · 2023Review
- HIV-1-induced nuclear invaginations mediated by VAP-A, ORP3, and Rab7 complex explain infection of activated T cells.Nature communications · 2023Article
- KIF16B Mediates Anterograde Transport and Modulates Lysosomal Degradation of the HIV-1 Envelope Glycoprotein.Journal of virology · 2023Article
20 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Following envelope mediated fusion, the HIV-1 core is released into the cytoplasm of the target cell and undergoes a series of trafficking and replicative steps that result in the nuclear import of the viral genome, which ultimately leads to the integration of the proviral DNA into the host cell genome. Previous studies have found that disruption of microtubules, or depletion of dynein or kinesin motors, perturb the normal uncoating and trafficking of the viral genome. Here, we show that the Kinesin-1 motor, KIF5B, induces a relocalization of the nuclear pore component Nup358 into the cytoplasm during HIV-1 infection. This relocalization of NUP358 is dependent on HIV-1 capsid, and NUP358 directly associates with viral cores following cytoplasmic translocation. This interaction between NUP358 and the HIV-1 core is dependent on multiple capsid binding surfaces, as this association is not observed following infection with capsid mutants in which a conserved hydrophobic binding pocket (N74D) or the cyclophilin A binding loop (P90A) is disrupted. KIF5B knockdown also prevents the nuclear entry and infection by HIV-1, but does not exert a similar effect on the N74D or P90A capsid mutants which do not rely on Nup358 for nuclear import. Finally, we observe that the relocalization of Nup358 in response to CA is dependent on cleavage protein and polyadenylation factor 6 (CPSF6), but independent of cyclophilin A. Collectively, these observations identify a previously unappreciated role for KIF5B in mediating the Nup358 dependent nuclear import of the viral genome during infection.
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