APOBEC3G Impairs the Multimerization of the HIV-1 Vif Protein in Living Cells

Batisse, Julien; Guerrero, Santiago; Bernacchi, Serena; Richert, Ludovic; Godet, Julien; Goldschmidt, Valérie; Mély, Yves; Marquet, Roland; Rocquigny, Hugues de; Paillart, Jean-Christophe

doi:10.1128/jvi.03494-12

Cited by 22 publications

(35 citation statements)

References 81 publications

(132 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The oligomerization of HIV-1 Vif into high-molecular-mass complexes is crucial for inducing Vif folding and binding onto HIV-1 genomic RNA, thereby enhancing HIV-1 Vif packaging into viral particles. A3G was found to be a regulator that strongly interferes with HIV-1 Vif multimerization to limit Vif function (55). It has also been proposed that CBF-␤ inhibits HIV-1 Vif oligomerization to promote the assembly of a well-ordered Vif-E3 complex (36).…”

Section: Discussionmentioning

confidence: 99%

“…3B) or other non-primate lentiviral Vifs (data not shown). Previous studies have shown that HIV-1 Vif forms oligomers or multimers in cells (53)(54)(55). The oligomerization of HIV-1 Vif into high-molecular-mass complexes is crucial for inducing Vif folding and binding onto HIV-1 genomic RNA, thereby enhancing HIV-1 Vif packaging into viral particles.…”

Section: Discussionmentioning

confidence: 99%

“…HIV-1 Vif was proposed to form multimers, which are necessary for the binding of Vif to viral RNA and packaging into virions. Disturbing HIV-1 Vif multimerization limited its function in the cells (53)(54)(55). Because CBF-␤ interacts with HIV-1 Vif to form a CUL5-based E3 ligase complex to induce APOBEC3 degradation (56), we questioned how HIV-1 Vif exerted its function in the multimeric form.…”

Section: Cbf-␤-kd 293t Cell Generationmentioning

confidence: 99%

See 2 more Smart Citations

Core-Binding Factor Subunit Beta Is Not Required for Non-Primate Lentiviral Vif-Mediated APOBEC3 Degradation

Zhu

Wang

et al. 2014

J Virol

View full text Add to dashboard Cite

Viral infectivity factor (Vif) is required for lentivirus fitness and pathogenicity, except in equine infectious anemia virus (EIAV).Vif enhances viral infectivity by a Cullin5-Elongin B/C E3 complex to inactivate the host restriction factor APOBEC3. Corebinding factor subunit beta (CBF-␤) is a cell factor that was recently shown to be important for the primate lentiviral Vif function. Non-primate lentiviral Vif also degrades APOBEC3 through the proteasome pathway. However, it is unclear whether CBF-␤ is required for the non-primate lentiviral Vif function. In this study, we demonstrated that the Vifs of non-primate lentiviruses, including feline immunodeficiency virus (FIV), bovine immunodeficiency virus (BIV), caprine arthritis encephalitis virus (CAEV), and maedi-visna virus (MVV), do not interact with CBF-␤. In addition, CBF-␤ did not promote the stability of FIV, BIV, CAEV, and MVV Vifs. Furthermore, CBF-␤ silencing or overexpression did not affect non-primate lentiviral Vif-mediated APOBEC3 degradation. Our results suggest that non-primate lentiviral Vif induces APOBEC3 degradation through a different mechanism than primate lentiviral Vif. IMPORTANCEThe APOBEC3 protein family members are host restriction factors that block retrovirus replication. Vif, an accessory protein of lentivirus, degrades APOBEC3 to rescue viral infectivity by forming Cullin5-Elongin B/C-based E3 complex. CBF-␤ was proved to be a novel regulator of primate lentiviral Vif function. In this study, we found that CBF-␤ knockdown or overexpression did not affect FIV Vif's function, which induced polyubiquitination and degradation of APOBEC3 by recruiting the E3 complex in a manner similar to that of HIV-1 Vif. We also showed that other non-primate lentiviral Vifs did not require CBF-␤ to degrade APOBEC3. CBF-␤ did not interact with non-primate lentiviral Vifs or promote their stability. These results suggest that a different mechanism exists for the Vif-APOBEC interaction and that non-primates are not suitable animal models for exploring pharmacological interventions that disrupt Vif-CBF-␤ interaction.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Cbf-␤-kd 293t Cell Generationmentioning

confidence: 99%

See 1 more Smart Citation

Core-Binding Factor Subunit Beta Is Not Required for Non-Primate Lentiviral Vif-Mediated APOBEC3 Degradation

Zhu

Wang

et al. 2014

J Virol

View full text Add to dashboard Cite

show abstract

“…164 motif critical for Vif oligomerization 33,34 and its interaction with the cellular kinase Hck 34,35 ; and (3) a domain (residues 172-192) important for binding with Pr55…”

Section: Pplpmentioning

confidence: 99%

“…18,34 We thus focused our analysis on the characterization of Vif domains regarding their capacity to self-assemble, their secondary structure, together with their RNA binding and chaperone activities.…”

Section: Rational Design Of Hiv-1 Vif Domains and Their Purificationmentioning

confidence: 99%

Characterization of RNA binding and chaperoning activities of HIV-1 Vif protein

Sleiman¹,

Bernacchi²,

Guerrero³

et al. 2014

RNA Biology

Self Cite

View full text Add to dashboard Cite

Spectral Phasor Applied to Spectrally‐Resolved Single Molecule Localization Microscopy

Manko,

Burton,

Mély

et al. 2024

ChemPhysChem

Self Cite

View full text Add to dashboard Cite

Spectrally‐resolved single‐molecule localization microscopy (srSMLM) has emerged as a powerful tool for exploring the spectral properties of single emitters in localization microscopy. By simultaneously capturing the spatial positions and spectroscopic signatures of individual fluorescent molecules, srSMLM opens up the possibility of investigating an additional dimension in super‐resolution imaging. However, appropriate and dedicated tools are required to fully capitalize on the spectral dimension. Here, we propose the application of the spectral phasor analysis as an effective method for summarizing and analyzing the spectral information obtained from srSMLM experiments. The spectral phasor condenses the complete spectrum of a single emitter into a two‐dimensional space, preserving key spectral characteristics for single‐molecule spectral exploration. We demonstrate the effectiveness of spectral phasor in efficiently classifying single Nile Red fluorescence emissions from largely overlapping cyanine fluorescence signals in dual‐color PAINT experiments. Additionally, we employed spectral phasor with srSMLM to reveal subtle alterations occurring in the membrane of Gram‐positive Enterococcus hirae in response to gramicidin exposure, a membrane‐perturbing antibiotic treatment. Spectral phasor provides a robust, model‐free analytic tool for the detailed analysis of the spectral component of srSMLM, enhancing the capabilities of multi‐color spectrally‐resolved single‐molecule imaging.

show abstract

APOBEC3G Impairs the Multimerization of the HIV-1 Vif Protein in Living Cells

Cited by 22 publications

References 81 publications

Core-Binding Factor Subunit Beta Is Not Required for Non-Primate Lentiviral Vif-Mediated APOBEC3 Degradation

Core-Binding Factor Subunit Beta Is Not Required for Non-Primate Lentiviral Vif-Mediated APOBEC3 Degradation

Characterization of RNA binding and chaperoning activities of HIV-1 Vif protein

Spectral Phasor Applied to Spectrally‐Resolved Single Molecule Localization Microscopy

Contact Info

Product

Resources

About