ArticleNucleic acids research2013
Binding of RNA by APOBEC3G controls deamination-independent restriction of retroviruses.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 88 citations in OpenAlex.
- Article
- Article
- APOBEC-1 cofactors regulate APOBEC3-induced mutations in hepatitis B virus.Journal of virology · 2025Article
- APOBEC3-Related Editing and Non-Editing Determinants of HIV-1 and HTLV-1 Restriction.International journal of molecular sciences · 2025Review
- Review
- Article
- APOBEC3G protects the genome of human cultured cells and mice from radiation-induced damage.The FEBS journal · 2023Article
- APOBEC3B drives PKR-mediated translation shutdown and protects stress granules in response to viral infection.Nature communications · 2023Article
- Article
- Antiretroviral APOBEC3 cytidine deaminases alter HIV-1 provirus integration site profiles.Nature communications · 2023Article
- Structural basis for HIV-1 antagonism of host APOBEC3G via Cullin E3 ligase.Science advances · 2023Article
- Differential Activity of APOBEC3F, APOBEC3G, and APOBEC3H in the Restriction of HIV-2.Journal of molecular biology · 2022Article
- Divergence in Dimerization and Activity of Primate APOBEC3C.Journal of molecular biology · 2021Article
- APOBEC3A drives deaminase domain-independent chromosomal instability to promote pancreatic cancer metastasis.Nature cancer · 2021Article
- Tree Shrew Cells Transduced with Human CD4 and CCR5 Support Early Steps of HIV-1 Replication, but Viral Infectivity Is Restricted by APOBEC3.Journal of virology · 2021Article
- Review
- Deaminase-Independent Mode of Antiretroviral Action in Human and Mouse APOBEC3 Proteins.Microorganisms · 2020Review
- The Role of APOBECs in Viral Replication.Microorganisms · 2020Review
- Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G.Nature communications · 2020Article
- Flexibility in Nucleic Acid Binding Is Central to APOBEC3H Antiviral Activity.Journal of virology · 2019Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
APOBEC3G (A3G) is a host-encoded protein that potently restricts the infectivity of a broad range of retroviruses. This can occur by mechanisms dependent on catalytic activity, resulting in the mutagenic deamination of nascent viral cDNA, and/or by other means that are independent of its catalytic activity. It is not yet known to what extent deamination-independent processes contribute to the overall restriction, how they exactly work or how they are regulated. Here, we show that alanine substitution of either tryptophan 94 (W94A) or 127 (W127A) in the non-catalytic N-terminal domain of A3G severely impedes RNA binding and alleviates deamination-independent restriction while still maintaining DNA mutator activity. Substitution of both tryptophans (W94A/W127A) produces a more severe phenotype in which RNA binding and RNA-dependent protein oligomerization are completely abrogated. We further demonstrate that RNA binding is specifically required for crippling late reverse transcript accumulation, preventing proviral DNA integration and, consequently, restricting viral particle release. We did not find that deaminase activity made a significant contribution to the restriction of any of these processes. In summary, this work reveals that there is a direct correlation between A3G's capacity to bind RNA and its ability to inhibit retroviral infectivity in a deamination-independent manner.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.