Evolutionarily Conserved Requirement for Core Binding Factor Beta in the Assembly of the Human Immunodeficiency Virus/Simian Immunodeficiency Virus Vif-Cullin 5-RING E3 Ubiquitin Ligase

Han, Xue; Liang, Weifang; Dai, Hua; Zhou, Xiao Hong; Du, Juan; Evans, Suzette M.; Gao, Qimeng; Wang, Hong; Viqueira, Rachel; Wei, Wei; Zhang, Wenyan; Yu, Xiao Fang

doi:10.1128/jvi.03833-13

Cited by 26 publications

(26 citation statements)

References 51 publications

(87 reference statements)

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“…Requirement for CBF-b in feline APOBEC3 degradation non-primate lentiviruses have either maintained an ancestral CBF-b-independent mechanism or have evolved to use another co-factor in the same way to degrade APOBEC3 proteins of their ancestral hosts. Interestingly, it has been recently reported that HIV-1 Vif can utilize CBF-b proteins from flies (Drosophila melanogaster) and worms (Saccoglossus kowalevskii) as the co-factor for human APOBEC3 degradation (Han et al, 2014). This further suggests that the usability of CBF-b is not dependent on the hosts and that primate lentiviral Vif has adapted to use CBF-b as an essential cofactor during its evolution.…”

mentioning

confidence: 74%

Vif determines the requirement for CBF-β in APOBEC3 degradation

Yoshikawa

Takeuchi

Yamada

et al. 2015

Journal of General Virology

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APOBEC3 (apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3) proteins are cellular DNA deaminases that restrict a broad spectrum of lentiviruses. This process is counteracted by Vif (viral infectivity factor) of lentiviruses, which binds APOBEC3s and promotes their degradation. CBF-b (core binding factor subunit b) is an essential co-factor for the function of human immunodeficiency virus type 1 Vif to degrade human APOBEC3s. However, the requirement for CBF-b in Vif-mediated degradation of other mammalian APOBEC3 proteins is less clear. Here, we determined the sequence of feline CBFB and performed phylogenetic analyses. These analyses revealed that mammalian CBFB is under purifying selection. Moreover, we demonstrated that CBF-b is dispensable for feline immunodeficiency virus Vif-mediated degradation of APOBEC3s of its host. These findings suggested that primate lentiviruses have adapted to use CBF-b, an evolutionary stable protein, to counteract APOBEC3 proteins of their hosts after diverging from other lentiviruses.

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mentioning

confidence: 74%

Vif determines the requirement for CBF-β in APOBEC3 degradation

Yoshikawa

Takeuchi

Yamada

et al. 2015

Journal of General Virology

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“…The N terminus of HIV-1 Vif, particularly the amino acids W5, V7, I9, W11, W21, W38, G84, E88, W89, L106, and I107 (Fig. 6A), was critical for CBF-␤ binding (30,56,(58)(59)(60)(61). These amino acids were almost conserved among primate lentiviral Vifs (Fig.…”

Section: Cbf-␤-kd 293t Cell Generationmentioning

confidence: 97%

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

Zhu

Wang

et al. 2014

J Virol

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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.

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“…While intrinsically disordered proteins can generally fold independently of chaperon assistance (44,45), recruitment of these molecular chaperoning factors can facilitate particular interactions. In support of this notion, recent biochemical and structural studies indicated that the disordered viral accessory Vif protein recruits cellular core-binding-factor-␤ (CBF-␤; a transcription cofactor known to form functional complexes with the RUNX family of transcription factors [46]), mainly as a molecular chaperon that increases Vif stability and solubility and induces a specific Vif-conformation mandatory for its interaction with cullin-5 and consequent Vif-E3 ligase assembly (47)(48)(49)(50)(51).…”

Section: Molecular Basis Underlying Flexible Exploitation Of Cellularmentioning

confidence: 94%

The Road Less Traveled: HIV's Use of Alternative Routes through Cellular Pathways

Marx

Alian

2015

J Virol

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Pathogens such as HIV-1, with their minimalist genomes, must navigate cellular networks and rely on hijacking and manipulating the host machinery for successful replication. Limited overlap of host factors identified as vital for pathogen replication may be explained by considering that pathogens target, rather than specific cellular factors, crucial cellular pathways by targeting different, functionally equivalent, protein-protein interactions within that pathway. The ability to utilize alternative routes through cellular pathways may be essential for pathogen survival when restricted and provide flexibility depending on the viral replication stage and the environment in the infected host. In this minireview, we evaluate evidence supporting this notion, discuss specific HIV-1 examples, and consider the molecular mechanisms which allow pathogens to flexibly exploit different routes.

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Evolutionarily Conserved Requirement for Core Binding Factor Beta in the Assembly of the Human Immunodeficiency Virus/Simian Immunodeficiency Virus Vif-Cullin 5-RING E3 Ubiquitin Ligase

Cited by 26 publications

References 51 publications

Vif determines the requirement for CBF-β in APOBEC3 degradation

Vif determines the requirement for CBF-β in APOBEC3 degradation

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

The Road Less Traveled: HIV's Use of Alternative Routes through Cellular Pathways

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