Evidence map›Paper›PMID 24418540›Full record

ArticleVirology2014

Defining HIV-1 Vif residues that interact with CBFβ by site-directed mutagenesis.

Yusuke Matsui, Keisuke Shindo, Kayoko Nagata, Katsuhiro Io, Kohei Tada, Fumie Iwai, Masayuki Kobayashi, Norimitsu Kadowaki, Reuben S Harris, Akifumi Takaori-Kondo

Abstract read
In one paragraph

Article in Virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Improving HIV proteome annotation: new features of BioAfrica HIV Proteomics Resource.Database : the journal of biological databases and curation · 2016
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
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

10 authors.

Yusuke MatsuiDepartment of Hematology and Oncology, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, Japan.
Keisuke ShindoDepartment of Hematology and Oncology, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, Japan. Electronic address: shind009@kuhp.kyoto-u.ac.jp.
Kayoko NagataDepartment of Hematology and Oncology, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, Japan.
Katsuhiro IoDepartment of Hematology and Oncology, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, Japan.
Kohei TadaDepartment of Hematology and Oncology, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, Japan.
Fumie IwaiDepartment of Hematology and Oncology, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, Japan.
Masayuki KobayashiDepartment of Hematology and Oncology, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, Japan.
Norimitsu KadowakiDepartment of Hematology and Oncology, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, Japan.
Reuben S HarrisDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, MN 55455, United States; Institute for Molecular Virology, University of Minnesota, MN 55455, United States.
Akifumi Takaori-KondoDepartment of Hematology and Oncology, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, Japan.

Funding

Structural Characterization of APOBECS's Atomic interactionsP01GM091743 · NIGMS · UNIVERSITY OF MINNESOTA · PI KOTLER, MOSHE · 2011 to 2015
$10.1M
APOBEC proteins and uracil in retrovirus restrictionR01AI064046 · NIAID · UNIVERSITY OF MINNESOTA TWIN CITIES · PI HARRIS, REUBEN S · 2005 to 2014
$3.0M
NIAID NIH HHS R01 AI064046NIAID NIH HHS R01AI064046NIGMS NIH HHS P01 GM091743NIGMS NIH HHS P01GM091743
6 · The paper itself

Abstract

Vif is essential for HIV-1 replication in T cells and macrophages. Vif recruits a host ubiquitin ligase complex to promote proteasomal degradation of the APOBEC3 restriction factors by poly-ubiquitination. The cellular transcription cofactor CBFβ is required for Vif function by stabilizing the Vif protein and promoting recruitment of a cellular Cullin5-RING ubiquitin ligase complex. Interaction between Vif and CBFβ is a promising therapeutic target, but little is known about the interfacial residues. We now demonstrate that Vif conserved residues E88/W89 are crucial for CBFβ binding. Substitution of E88/W89 to alanines impaired binding to CBFβ, degradation of APOBEC3, and virus infectivity in the presence of APOBEC3 in single-cycle infection. In spreading infection, NL4-3 with Vif E88A/W89A mutation replicated comparably to wild-type virus in permissive CEM-SS cells, but not in multiple APOBEC3 expressing non-permissive CEM cells. These results support a model in which HIV-1 Vif residues E88/W89 may participate in binding CBFβ.

Indexed as

Amino Acid MotifsAmino Acid SequenceConserved SequenceCore Binding Factor beta SubunitCytidine DeaminaseHIV-1HIV InfectionsHumansMolecular Sequence DataMutagenesis, Site-DirectedProtein Bindingvif Gene Products, Human Immunodeficiency VirusCBFB protein, humanCore Binding Factor beta SubunitCytidine Deaminasevif Gene Products, Human Immunodeficiency VirusCBFβHIV-1Host factorsInteractionVif

Identifiers

PMID24418540
PMCPMC3936105

What OpenQuestion holds

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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.