ArticleNucleic acids research2010
Definition of the interacting interfaces of Apobec3G and HIV-1 Vif using MAPPIT mutagenesis analysis.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 51 citations in OpenAlex.
- Structural insights into RNA bridging between HIV-1 Vif and antiviral factor APOBEC3G.Nature communications · 2023Article
- Antiretroviral APOBEC3 cytidine deaminases alter HIV-1 provirus integration site profiles.Nature communications · 2023Article
- HIV-1 VIF and human APOBEC3G interaction directly observed through molecular specific labeling using a new dual promotor vector.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022Article
- ZBTB32 performs crosstalk with the glucocorticoid receptor and is crucial in glucocorticoid responses to starvation.iScience · 2021Article
- Examination of the APOBEC3 Barrier to Cross Species Transmission of Primate Lentiviruses.Viruses · 2021Review
- Characterization of an A3G-VifMolecular & cellular proteomics : MCP · 2021Article
- Structural perspectives on HIV-1 Vif and APOBEC3 restriction factor interactions.Protein science : a publication of the Protein Society · 2020Review
- Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G.Nature communications · 2020Article
- Retroviruses drive the rapid evolution of mammalianProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Straightforward Protein-Protein Interaction Interface Mapping via Random Mutagenesis and Mammalian Protein Protein Interaction Trap (MAPPIT).International journal of molecular sciences · 2019Review
- Structural Determinants of the APOBEC3G N-Terminal Domain for HIV-1 RNA Association.Frontiers in cellular and infection microbiology · 2019Article
- Simian Immunodeficiency Virus Vif and Human APOBEC3B Interactions Resemble Those between HIV-1 Vif and Human APOBEC3G.Journal of virology · 2018Article
- Identification of small molecule compounds targeting the interaction of HIV-1 Vif and human APOBEC3G by virtual screening and biological evaluation.Scientific reports · 2018Article
- Review
- Identification and characterization of loop7 motif and its role in regulating biological function of human APOBEC3G through molecular modeling and biological assay.Acta pharmaceutica Sinica. B · 2017Article
- Crystal structures of APOBEC3G N-domain alone and its complex with DNA.Nature communications · 2016Article
- Determinants of FIV and HIV Vif sensitivity of feline APOBEC3 restriction factors.Retrovirology · 2016Article
- Inhibition of APOBEC3G activity impedes double-stranded DNA repair.The FEBS journal · 2016Article
- RNA binding to APOBEC3G induces the disassembly of functional deaminase complexes by displacing single-stranded DNA substrates.Nucleic acids research · 2015Article
- Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G.Nature structural & molecular biology · 2015Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The host restriction factor Apobec3G is a cytidine deaminase that incorporates into HIV-1 virions and interferes with viral replication. The HIV-1 accessory protein Vif subverts Apobec3G by targeting it for proteasomal degradation. We propose a model in which Apobec3G N-terminal domains symmetrically interact via a head-to-head interface containing residues 122 RLYYFW 127. To validate this model and to characterize the Apobec3G-Apobec3G and the Apobec3G-Vif interactions, the mammalian protein-protein interaction trap two-hybrid technique was used. Mutations in the head-to-head interface abrogate the Apobec3G-Apobec3G interaction. All mutations that inhibit Apobec3G-Apobec3G binding also inhibit the Apobec3G-Vif interaction, indicating that the head-to head interface plays an important role in the interaction with Vif. Only the D128K, P129A and T32Q mutations specifically affect the Apobec3G-Vif association. In our model, D128, P129 and T32 cluster at the edge of the head-to-head interface, possibly forming a Vif binding site composed of two Apobec3G molecules. We propose that Vif either binds at the Apobec3G head-to-head interface or associates with an RNA-stabilized Apobec3G oligomer.
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