Evidence map›Paper›PMID 34908151›Full record

ArticleNucleic acids research2022

Highly conserved s2m element of SARS-CoV-2 dimerizes via a kissing complex and interacts with host miRNA-1307-3p.

Joshua A Imperatore, Caylee L Cunningham, Kendy A Pellegrene, Robert G Brinson, John P Marino, Jeffrey D Evanseck, Mihaela Rita Mihailescu

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 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.5field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 45 citations in OpenAlex.

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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.

Joshua A ImperatoreDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA 15282, USA.
Caylee L CunninghamDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA 15282, USA.
Kendy A PellegreneDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA 15282, USA.
Robert G BrinsonInstitute for Bioscience and Biotechnology Research, National Institute of Standards and Technology and the University of Maryland, Rockville, MD 20850, USA.
John P MarinoInstitute for Bioscience and Biotechnology Research, National Institute of Standards and Technology and the University of Maryland, Rockville, MD 20850, USA.
Jeffrey D EvanseckDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA 15282, USA.
Mihaela Rita MihailescuDepartment of Chemistry and Biochemistry, Duquesne University, Pittsburgh, PA 15282, USA.ORCID 0000-0002-1162-7699
Duquesne University · USNational Institute of Standards and Technology · US

Funding

Major Research Instrumentation 1726824National Science Foundation 2029124
6 · The paper itself

Abstract

The ongoing COVID-19 pandemic highlights the necessity for a more fundamental understanding of the coronavirus life cycle. The causative agent of the disease, SARS-CoV-2, is being studied extensively from a structural standpoint in order to gain insight into key molecular mechanisms required for its survival. Contained within the untranslated regions of the SARS-CoV-2 genome are various conserved stem-loop elements that are believed to function in RNA replication, viral protein translation, and discontinuous transcription. While the majority of these regions are variable in sequence, a 41-nucleotide s2m element within the genome 3' untranslated region is highly conserved among coronaviruses and three other viral families. In this study, we demonstrate that the SARS-CoV-2 s2m element dimerizes by forming an intermediate homodimeric kissing complex structure that is subsequently converted to a thermodynamically stable duplex conformation. This process is aided by the viral nucleocapsid protein, potentially indicating a role in mediating genome dimerization. Furthermore, we demonstrate that the s2m element interacts with multiple copies of host cellular microRNA (miRNA) 1307-3p. Taken together, our results highlight the potential significance of the dimer structures formed by the s2m element in key biological processes and implicate the motif as a possible therapeutic drug target for COVID-19 and other coronavirus-related diseases.

Indexed as

3' Untranslated RegionsBase SequenceBinding SitesConserved SequenceCOVID-19DimerizationGenome, ViralHost-Pathogen InteractionsHumansMicroRNAsNucleic Acid ConformationNucleotide MotifsProton Magnetic Resonance SpectroscopyRNA, ViralSARS-CoV-23' Untranslated RegionsMicroRNAsMIRN1307 microRNA, humanRNA, Viral

Identifiers

PMID34908151
PMCPMC8789046
OpenAlexW4200364738

What OpenQuestion 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 OpenQuestion graph.