Evidence map›Paper›PMID 37419875›Full record

ArticleNature communications2023

Structural insights into RNA bridging between HIV-1 Vif and antiviral factor APOBEC3G.

Takahide Kouno, Satoshi Shibata, Megumi Shigematsu, Jaekyung Hyun, Tae Gyun Kim, Hiroshi Matsuo, Matthias Wolf

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 20 citations in OpenAlex.

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  8. Fitness Landscapes of APOBEC3G Antagonism by HIV-1 Vif proteins.bioRxiv : the preprint server for biology · 2025
    Article
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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

7 authors at 3 institutions in 4 countries.

Takahide KounoMolecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, Onna-son, Okinawa, 904-0495, Japan. 1st.soluble.fla3g@gmail.com.ORCID 0000-0002-0075-5046
Satoshi ShibataMolecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, Onna-son, Okinawa, 904-0495, Japan.ORCID 0000-0002-6095-9796
Megumi ShigematsuComputational Medicine Center, Sidney Kimmel Medical College, Thomas Jefferson University, Philadelphia, PA, 19107, USA.ORCID 0000-0003-3265-5557
Jaekyung HyunMolecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, Onna-son, Okinawa, 904-0495, Japan.ORCID 0000-0003-2914-537X
Tae Gyun KimMolecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, Onna-son, Okinawa, 904-0495, Japan.
Hiroshi MatsuoCancer Innovation Laboratory, Frederick National Laboratory for Cancer Research, Frederick, MD, 21702, USA.ORCID 0000-0002-4559-6157
Matthias WolfMolecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, Onna-son, Okinawa, 904-0495, Japan. matthias.wolf@oist.jp.ORCID 0000-0001-8480-0918
Okinawa Institute of Science and Technology Graduate University · JPFrederick National Laboratory for Cancer Research · USThomas Jefferson University · US

Funding

WORK ORDER 126643 B539 EXPAND IC SUITE75N91019D00024 · NIAID · LEIDOS BIOMEDICAL RESEARCH, INC. · PI BRISCOE, LYNN · 2019 to 2025
$3932.6M
Structural studies of biomolecules related to cancer and HIV-AIDSZICBC011849 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MATSUO, HIROSHI · 2018 to 2024
$5.0M
Structurally dissecting APOBEC3's for HIV-1 restriction and beyondR01AI150478 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI SCHIFFER, CELIA A. · 2019 to 2024
$3.9M
Structurally dissecting APOBEC3's for HIV-1 restrictionR01GM118474 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI SCHIFFER, CELIA A. · 2016 to 2018
$1.8M
NCI NIH HHS 75N91019D00024NIAID NIH HHS R01 AI150478NIGMS NIH HHS R01 GM118474
6 · The paper itself

Abstract

Great effort has been devoted to discovering the basis of A3G-Vif interaction, the key event of HIV's counteraction mechanism to evade antiviral innate immune response. Here we show reconstitution of the A3G-Vif complex and subsequent A3G ubiquitination in vitro and report the cryo-EM structure of the A3G-Vif complex at 2.8 Å resolution using solubility-enhanced variants of A3G and Vif. We present an atomic model of the A3G-Vif interface, which assembles via known amino acid determinants. This assembly is not achieved by protein-protein interaction alone, but also involves RNA. The cryo-EM structure and in vitro ubiquitination assays identify an adenine/guanine base preference for the interaction and a unique Vif-ribose contact. This establishes the biological significance of an RNA ligand. Further assessment of interactions between A3G, Vif, and RNA ligands show that the A3G-Vif assembly and subsequent ubiquitination can be controlled by amino acid mutations at the interface or by polynucleotide modification, suggesting that a specific chemical moiety would be a promising pharmacophore to inhibit the A3G-Vif interaction.

Indexed as

HIV-1vif Gene Products, Human Immunodeficiency VirusAmino AcidsAntiviral AgentsAPOBEC-3G DeaminaseCytidine DeaminaseRNAAmino AcidsAntiviral AgentsAPOBEC-3G DeaminaseCytidine DeaminaseRNAvif Gene Products, Human Immunodeficiency Virus

Identifiers

PMID37419875
PMCPMC10328928
OpenAlexW4383499678

What OpenQuestion holds

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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.