Evidence map›Paper›PMID 35077748›Full record

ArticleInternational journal of biological macromolecules2022

Insights into the specificity for the interaction of the promiscuous SARS-CoV-2 nucleocapsid protein N-terminal domain with deoxyribonucleic acids.

Icaro Putinhon Caruso, Vitor Dos Santos Almeida, Mariana Juliani do Amaral, Guilherme Caldas de Andrade, Gabriela Rocha de Araújo, Talita Stelling de Araújo, Jéssica Moreira de Azevedo, Glauce Moreno Barbosa, Leonardo Bartkevihi, Peter Reis Bezerra and 17 more

Open access · greenAbstract read
In one paragraph

Article in International journal of biological macromolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  5. SARS-CoV-2 nucleocapsid protein directly prevents cGAS-DNA recognition through competitive binding.Proceedings of the National Academy of Sciences of the United States of America · 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

27 authors at 4 institutions in 1 country.

Icaro Putinhon CarusoInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Multiuser Center for Biomolecular Innovation (CMIB), Department of Physics, São Paulo State University (UNESP), São José do Rio Preto, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil. Electronic address: icaro.caruso@unesp.br.
Vitor Dos Santos AlmeidaNational Center of Nuclear Magnetic Resonance (CNRMN), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Mariana Juliani do AmaralFaculty of Pharmacy, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Protein Advanced Biochemistry (PAB), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Guilherme Caldas de AndradeInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; National Center of Nuclear Magnetic Resonance (CNRMN), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Gabriela Rocha de AraújoInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; National Center of Nuclear Magnetic Resonance (CNRMN), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Talita Stelling de AraújoInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Protein Advanced Biochemistry (PAB), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Jéssica Moreira de AzevedoInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Protein Advanced Biochemistry (PAB), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Glauce Moreno BarbosaInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; National Center of Nuclear Magnetic Resonance (CNRMN), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Leonardo BartkevihiInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; National Center of Nuclear Magnetic Resonance (CNRMN), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Peter Reis BezerraInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; National Center of Nuclear Magnetic Resonance (CNRMN), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Katia Maria Dos Santos CabralInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Protein Advanced Biochemistry (PAB), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Isabella Otênio de LourençoMultiuser Center for Biomolecular Innovation (CMIB), Department of Physics, São Paulo State University (UNESP), São José do Rio Preto, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Clara L F Malizia-MottaDepartment of Biochemistry, Institute of Chemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Aline de Luna MarquesInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Multidisciplinary Center for Research in Biology (NUMPEX), Campus Duque de Caxias Federal University of Rio de Janeiro, Duque de Caxias, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Nathane Cunha Mebus-AntunesInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Thais Cristtina Neves-MartinsInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Jéssica Maróstica de SáMultiuser Center for Biomolecular Innovation (CMIB), Department of Physics, São Paulo State University (UNESP), São José do Rio Preto, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Karoline SanchesMultiuser Center for Biomolecular Innovation (CMIB), Department of Physics, São Paulo State University (UNESP), São José do Rio Preto, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Marcos Caique Santana-SilvaInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Multidisciplinary Center for Research in Biology (NUMPEX), Campus Duque de Caxias Federal University of Rio de Janeiro, Duque de Caxias, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Ariana Azevedo VasconcelosInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; National Center of Nuclear Magnetic Resonance (CNRMN), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Marcius da Silva AlmeidaInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Protein Advanced Biochemistry (PAB), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Gisele Cardoso de AmorimInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Multidisciplinary Center for Research in Biology (NUMPEX), Campus Duque de Caxias Federal University of Rio de Janeiro, Duque de Caxias, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Cristiane Dinis AnobomNational Center of Nuclear Magnetic Resonance (CNRMN), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Department of Biochemistry, Institute of Chemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Andrea T Da PoianInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Francisco Gomes-NetoNational Center of Nuclear Magnetic Resonance (CNRMN), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Laboratory of Toxinology, Oswaldo Cruz Foundation (FIOCRUZ), Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Anderson S PinheiroDepartment of Biochemistry, Institute of Chemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil.
Fabio C L AlmeidaInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; National Center of Nuclear Magnetic Resonance (CNRMN), CENABIO, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil; Rio BioNMR Network, Rio de Janeiro, Brazil. Electronic address: falmeida@bioqmed.ufrj.br.
Universidade Federal do Rio de Janeiro · BRNational Education and Research Network · BRUniversidade Estadual Paulista (Unesp) · BRFundação Oswaldo Cruz · BR

Funding

TRD3 NMRbox: Bayesian AnalyticsP41GM111135 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI HOCH, JEFFREY C · 2015 to 2024
$14.0M
NIGMS NIH HHS P41 GM111135
6 · The paper itself

Abstract

The SARS-CoV-2 nucleocapsid protein (N) is a multifunctional promiscuous nucleic acid-binding protein, which plays a major role in nucleocapsid assembly and discontinuous RNA transcription, facilitating the template switch of transcriptional regulatory sequences (TRS). Here, we dissect the structural features of the N protein N-terminal domain (N-NTD) and N-NTD plus the SR-rich motif (N-NTD-SR) upon binding to single and double-stranded TRS DNA, as well as their activities for dsTRS melting and TRS-induced liquid-liquid phase separation (LLPS). Our study gives insights on the specificity for N-NTD(-SR) interaction with TRS. We observed an approximation of the triple-thymidine (TTT) motif of the TRS to β-sheet II, giving rise to an orientation difference of ~25° between dsTRS and non-specific sequence (dsNS). It led to a local unfavorable energetic contribution that might trigger the melting activity. The thermodynamic parameters of binding of ssTRSs and dsTRS suggested that the duplex dissociation of the dsTRS in the binding cleft is entropically favorable. We showed a preference for TRS in the formation of liquid condensates when compared to NS. Moreover, our results on DNA binding may serve as a starting point for the design of inhibitors, including aptamers, against N, a possible therapeutic target essential for the virus infectivity.

Indexed as

Protein Interaction Domains and MotifsBinding SitesCOVID-19DNAGene Expression Regulation, ViralHost-Pathogen InteractionsHumansHydrogen BondingModels, MolecularNucleic AcidsNucleocapsid ProteinsProtein BindingRNASARS-CoV-2Spectrum AnalysisStructure-Activity RelationshipDNANucleic AcidsNucleocapsid ProteinsRNABinding specificityDNA/RNA binding proteinSARS-CoV-2 nucleocapsid protein

Identifiers

PMID35077748
PMCPMC8783401
OpenAlexW4207059657

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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.