Evidence map›Paper›PMID 34824224›Full record

ArticleNature communications2021

A structured RNA motif locks Argonaute2:miR-122 onto the 5' end of the HCV genome.

Luca F R Gebert, Mansun Law, Ian J MacRae

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
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  5. IGF2BP3 remodels the microRNA targeting landscape in MLL-AF4 leukemia.bioRxiv : the preprint server for biology · 2025
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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

3 authors at 1 institution in 1 country.

Luca F R GebertDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA.ORCID http://orcid.org/0000-0002-1830-119X
Mansun LawDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA, 92037, USA.ORCID http://orcid.org/0000-0002-8934-9756
Ian J MacRaeDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, 92037, USA. macrae@scripps.edu.ORCID http://orcid.org/0000-0002-5112-0294
Scripps Research Institute · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI PAUL David ADAMS, Gregory L Hura · 2017 to 2026
$28.6M
Structural and Mechanistic basis for RNA SilencingR35GM127090 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI IAN JOHN MACRAE · 2018 to 2026
$5.6M
Structure and function of Hepacivirus envelope glycoproteinR01AI123365 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI LAW, MANSUN, WILSON, IAN A · 2016 to 2020
$3.1M
NIAID NIH HHS R01 AI123365NIGMS NIH HHS P30 GM124169NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R35 GM127090
6 · The paper itself

Abstract

microRNAs (miRNAs) form regulatory networks in metazoans. Viruses engage miRNA networks in numerous ways, with Flaviviridae members exploiting direct interactions of their RNA genomes with host miRNAs. For hepatitis C virus (HCV), binding of liver-abundant miR-122 stabilizes the viral RNA and regulates viral translation. Here, we investigate the structural basis for these activities, taking into consideration that miRNAs function in complex with Argonaute (Ago) proteins. The crystal structure of the Ago2:miR-122:HCV complex reveals a structured RNA motif that traps Ago2 on the viral RNA, masking its 5' end from enzymatic attack. The trapped Ago2 can recruit host factor PCBP2, implicated in viral translation, while binding of a second Ago2:miR-122 competes with PCBP2, creating a potential molecular switch for translational control. Combined results reveal a viral RNA structure that modulates Ago2:miR-122 dynamics and repurposes host proteins to generate a functional analog of the mRNA cap-binding complex.

Indexed as

5' Untranslated RegionsArgonaute ProteinsBinding SitesCrystallography, X-RayExoribonucleasesGenome, ViralHepacivirusHumansMicroRNAsMicrotubule-Associated ProteinsNucleotide MotifsPhosphoric Monoester HydrolasesProtein ConformationRNA-Binding ProteinsRNA, Viral5' Untranslated RegionsAGO2 protein, humanArgonaute ProteinsExoribonucleasesMicroRNAsMicrotubule-Associated ProteinsMIRN122 microRNA, humanPCBP2 protein, humanPhosphoric Monoester HydrolasesRNA-Binding ProteinsRNA, ViralXRN1 protein, human

Identifiers

PMID34824224
PMCPMC8616905
OpenAlexW3215335769

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.