ArticleJournal of virology2010
The localization of APOBEC3H variants in HIV-1 virions determines their antiviral activity.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.
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Who cites it
40 citing papers in PubMed, 1 synthesis or guideline pooled it, 50 citations in OpenAlex.
- Multiple Inhibitory Factors Act in the Late Phase of HIV-1 Replication: a Systematic Review of the Literature.Microbiology and molecular biology reviews : MMBR · 2018Pooled it
- Mechanisms of APOBEC3 Packaging into HIV-1.Viruses · 2026Review
- Guardian ubiquitin E3 ligases target cancer-associated APOBEC3 deaminases for degradation to promote human genome integrity.Nature communications · 2026Article
- HIV-1 vif mediates ubiquitination of the proximal protomer in the APOBEC3H dimer to induce degradation.Nature communications · 2025Article
- Research on the influence of APOBEC family on the occurrence, diagnosis, and treatment of various tumors.Journal of cancer research and clinical oncology · 2023Review
- ISG15 deficiency restricts HIV-1 infection.PLoS pathogens · 2022Article
- APOBEC3B Potently Restricts HIV-2 but Not HIV-1 in a Vif-Dependent Manner.Journal of virology · 2021Article
- Human APOBEC3 Variations and Viral Infection.Viruses · 2021Review
- Examination of the APOBEC3 Barrier to Cross Species Transmission of Primate Lentiviruses.Viruses · 2021Review
- Polymorphisms in Human APOBEC3H Differentially Regulate Ubiquitination and Antiviral Activity.Viruses · 2020Article
- HIV protease cleaves the antiviral m6A reader protein YTHDF3 in the viral particle.PLoS pathogens · 2020Article
- The Role of RNA in HIV-1 Vif-Mediated Degradation of APOBEC3H.Journal of molecular biology · 2019Article
- Characterization of APOBEC3 variation in a population of HIV-1 infected individuals in northern South Africa.BMC medical genetics · 2019Article
- Structural basis of chimpanzee APOBEC3H dimerization stabilized by double-stranded RNA.Nucleic acids research · 2018Article
- IL-15 regulates susceptibility of CD4Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Understanding the Structure, Multimerization, Subcellular Localization and mC Selectivity of a Genomic Mutator and Anti-HIV Factor APOBEC3H.Scientific reports · 2018Article
- Deamination-independent restriction of LINE-1 retrotransposition by APOBEC3H.Scientific reports · 2017Article
- Biochemical Characterization of APOBEC3H Variants: Implications for Their HIV-1 Restriction Activity and mC Modification.Journal of molecular biology · 2016Article
- The DNA cytosine deaminase APOBEC3H haplotype I likely contributes to breast and lung cancer mutagenesis.Nature communications · 2016Article
- APOBEC3H polymorphisms and susceptibility to HIV-1 infection in an Indian population.Journal of human genetics · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Several members of the human APOBEC3 family of cytidine deaminases can potently restrict retroviruses such as HIV-1. The single-domain APOBEC3H (A3H) is encoded by four haplotypes, of which only A3H haplotype II-RDD (hapII-RDD) restricts HIV-1 efficiently. The goal of this study was to elucidate the mechanisms underlying the differences in antiviral activity among A3H haplotypes. The naturally occurring A3H hapI-GKE and hapII-RDD variants differ at three amino acid positions. A panel of six site-directed mutants containing combinations of the three variable residues was used to determine A3H protein expression, requirements of A3H virion incorporation, and A3H-Gag interactions. The catalytic activity of each A3H protein was assessed directly by using an Escherichia coli mutator assay. We found that the incorporation efficiencies of A3H variants into HIV-1 virions were comparable despite major differences in cellular expression. An assessment of the enzymes' catalytic activities showed that the deaminase activity of each A3H variant correlated with protein expression, suggesting similar enzymatic efficiencies. Surprisingly, virion incorporation experiments using Gag deletion mutants demonstrated that A3H haplotypes interacted with different Gag regions. A3H hapII-RDD associated with nucleocapsid in an RNA-dependent manner, whereas A3H hapI-GKE associated with the C-terminal part of matrix and the N-terminal capsid domain. Our results show that the A3H hapII-RDD interaction with nucleocapsid is critical for its antiviral activity and that the inability of A3H hapI-GKE to interact with nucleocapsid underlies its limited antiviral potential. Thus, the antiviral activity of A3H haplotypes is determined by its incorporation into the viral core, in proximity to the reverse transcription complex.
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Registered trials
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