Evidence map›Paper›PMID 35018437›Full record

ArticleNucleic acids research2022

Selection and identification of an RNA aptamer that specifically binds the HIV-1 capsid lattice and inhibits viral replication.

Paige R Gruenke, Rachna Aneja, Sarah Welbourn, Obiaara B Ukah, Stefan G Sarafianos, Donald H Burke, Margaret J Lange

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
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  9. Role of Plant Virus Movement Proteins in Suppression of Host RNAi Defense.International journal of molecular sciences · 2023
    Review
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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 2 institutions in 1 country.

Paige R GruenkeDepartment of Biochemistry, University of Missouri, Columbia, MO 65211, USA.
Rachna AnejaDepartment of Molecular Microbiology & Immunology, School of Medicine, University of Missouri, Columbia, MO 65211, USA.
Sarah WelbournEmory Vaccine Center and Yerkes National Primate Research Center, Emory University, Atlanta, GA 30329, USA.
Obiaara B UkahDepartment of Molecular Microbiology & Immunology, School of Medicine, University of Missouri, Columbia, MO 65211, USA.
Stefan G SarafianosLaboratory of Biochemical Pharmacology, Department of Pediatrics, Emory University School of Medicine, Atlanta, GA 30322, USA.
Donald H BurkeDepartment of Biochemistry, University of Missouri, Columbia, MO 65211, USA.
Margaret J LangeDepartment of Molecular Microbiology & Immunology, School of Medicine, University of Missouri, Columbia, MO 65211, USA.
University of Missouri · USEmory University · US

Funding

Structural studies of HIV Capsid with host factors and Capsid-targeting antiviralsR01AI120860 · NIAID · UNIVERSITY OF MISSOURI-COLUMBIA · PI Stefan G Sarafianos, Zhengqiang Wang · 2015 to 2026
$6.0M
Molecular Interactions of HIV-1 with the Nuclear Pore ComplexR01AI148382 · NIAID · EMORY UNIVERSITY · PI MELIKIAN, GREGORY B, SARAFIANOS, STEFAN G · 2019 to 2022
$5.5M
RNA Aptamers that Differentiate Among HIV-1 Capsid Assembly StatesR21AI127195 · NIAID · UNIVERSITY OF MISSOURI-COLUMBIA · PI BURKE, DONALD H, LANGE, MARGARET J · 2016 to 2017
$422k
NIAID NIH HHS R01 AI120860NIAID NIH HHS R01 AI148382NIAID NIH HHS R21 AI127195
6 · The paper itself

Abstract

The HIV-1 capsid core participates in several replication processes. The mature capsid core is a lattice composed of capsid (CA) monomers thought to assemble first into CA dimers, then into ∼250 CA hexamers and 12 CA pentamers. CA assembly requires conformational flexibility of each unit, resulting in the presence of unique, solvent-accessible surfaces. Significant advances have improved our understanding of the roles of the capsid core in replication; however, the contributions of individual CA assembly forms remain unclear and there are limited tools available to evaluate these forms in vivo. Here, we have selected aptamers that bind CA lattice tubes. We describe aptamer CA15-2, which selectively binds CA lattice, but not CA monomer or CA hexamer, suggesting that it targets an interface present and accessible only on CA lattice. CA15-2 does not compete with PF74 for binding, indicating that it likely binds a non-overlapping site. Furthermore, CA15-2 inhibits HIV-1 replication when expressed in virus producer cells, but not target cells, suggesting that it binds a biologically-relevant site during virus production that is either not accessible during post-entry replication steps or is accessible but unaltered by aptamer binding. Importantly, CA15-2 represents the first aptamer that specifically recognizes the HIV-1 CA lattice.

Indexed as

Aptamers, NucleotideHIV-1CapsidCapsid ProteinsVirus ReplicationAptamers, NucleotideCapsid Proteins

Identifiers

PMID35018437
PMCPMC8860611
OpenAlexW4206837834

What Socratic holds

Textmetadata
LicenceCC BY-NC
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 Socratic graph.