Evidence map›Paper›PMID 24810617›Full record

ArticlePloS one2014

Identification of HIV-1 Vif regions required for CBF-β interaction and APOBEC3 suppression.

Hong Wang, Bin Liu, Xin Liu, Zhaolong Li, Xiao-Fang Yu, Wenyan Zhang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
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  3. Characterization of an A3G-VifMolecular & cellular proteomics : MCP · 2021
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Hong WangInstitute of Virology and AIDS Research, First Hospital of Jilin University, Changchun, Jilin Province, China.
Bin LiuInstitute of Virology and AIDS Research, First Hospital of Jilin University, Changchun, Jilin Province, China; Department of Hand Surgery, First Hospital of Jilin University, Changchun, Jilin Province, China.
Xin LiuInstitute of Virology and AIDS Research, First Hospital of Jilin University, Changchun, Jilin Province, China.
Zhaolong LiInstitute of Virology and AIDS Research, First Hospital of Jilin University, Changchun, Jilin Province, China.
Xiao-Fang YuInstitute of Virology and AIDS Research, First Hospital of Jilin University, Changchun, Jilin Province, China; Department of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland, United States of America.
Wenyan ZhangInstitute of Virology and AIDS Research, First Hospital of Jilin University, Changchun, Jilin Province, China.
First Hospital of Jilin University · CNJilin University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human immunodeficiency virus type 1 (HIV-1) Vif requires core binding factor β (CBF-β) to degrade the host APOBEC3 restriction factors. Although a minimum domain and certain amino acids of HIV-1 Vif, including hydrophobic residues at the N-terminal, have been identified as critical sites for binding with CBF-β, other regions that potentially mediate this interaction need to be further investigated. Here, we mapped two new regions of HIV-1 Vif that are required for interaction with CBF-β by generating a series of single-site or multiple-site Vif mutants and testing their effect on the suppression of APOBEC3G (A3G) and APOBEC3F (A3F). A number of the mutants, including G84A/SIEW86-89AAAA (84/86-89), E88A/W89A (88/89), G84A, W89A, L106S and I107S in the 84GxSIEW89 and L102ADQLI107 regions, affected Vif function by disrupting CBF-β binding. These Vif mutants also had altered interactions with CUL5, since CBF-β is known to facilitate the binding of Vif to CUL5. We further showed that this effect was not due to misfolding or conformational changes in Vif, as the mutants still maintained their interactions with other factors such as ElonginB, A3G and A3F. Notably, G84D and D104A had stronger effects on the Vif-CUL5 interaction than on the Vif-CBF-β interaction, indicating that they mainly influenced the CUL5 interaction and implying that the interaction of Vif with CUL5 contributes to the binding of Vif to CBF-β. These new binding interfaces with CBF-β in HIV-1 Vif provide novel targets for the development of HIV-1 inhibitors.

Indexed as

APOBEC DeaminasesCore Binding Factor beta SubunitCullin ProteinsCytidine DeaminaseCytosine DeaminaseHIV-1HumansProtein BindingProtein Interaction Domains and Motifsvif Gene Products, Human Immunodeficiency VirusAPOBEC3 proteins, humanAPOBEC DeaminasesCore Binding Factor beta SubunitCUL5 protein, humanCullin ProteinsCytidine DeaminaseCytosine Deaminasevif Gene Products, Human Immunodeficiency Virus

Identifiers

PMID24810617
PMCPMC4014475
OpenAlexW2009685783

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LicenceCC BY
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Registered trials

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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.