Evidence map›Paper›PMID 35328409›Full record

ArticleInternational journal of molecular sciences2022

SARS-CoV-2 Membrane Protein: From Genomic Data to Structural New Insights.

Catarina Marques-Pereira, Manuel N Pires, Raquel P Gouveia, Nádia N Pereira, Ana B Caniceiro, Nícia Rosário-Ferreira, Irina S Moreira

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2022. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. SARS-CoV-2 and the DNA damage response.The Journal of general virology · 2023
    Review
  12. Article
  13. Article
  14. Review
  15. Toll-like Receptor Mediation in SARS-CoV-2: A Therapeutic Approach.International journal of molecular sciences · 2022
    Review
  16. Review
  17. Review
  18. Article
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.

Catarina Marques-PereiraCNC-Center for Neuroscience and Cell Biology, University of Coimbra, 3004-535 Coimbra, Portugal.ORCID 0000-0001-6840-8991
Manuel N PiresCNC-Center for Neuroscience and Cell Biology, University of Coimbra, 3004-535 Coimbra, Portugal.
Raquel P GouveiaCNC-Center for Neuroscience and Cell Biology, University of Coimbra, 3004-535 Coimbra, Portugal.ORCID 0000-0001-5092-4373
Nádia N PereiraCNC-Center for Neuroscience and Cell Biology, University of Coimbra, 3004-535 Coimbra, Portugal.
Ana B CaniceiroCNC-Center for Neuroscience and Cell Biology, University of Coimbra, 3004-535 Coimbra, Portugal.
Nícia Rosário-FerreiraCNC-Center for Neuroscience and Cell Biology, University of Coimbra, 3004-535 Coimbra, Portugal.ORCID 0000-0002-7225-9287
Irina S MoreiraDepartment of Life Sciences, University of Coimbra, Calçada Martim de Freitas, 3000-456 Coimbra, Portugal.ORCID 0000-0003-2970-5250

Funding

Fundação para a Ciência e Tecnologia DSAIPA/DS/0118/2020Fundação para a Ciência e Tecnologia POCI-01-0145-FEDER-031356Fundação para a Ciência e Tecnologia UIDB/04539/2020
6 · The paper itself

Abstract

Severe Acute Respiratory Syndrome CoronaVirus-2 (SARS-CoV-2) is composed of four structural proteins and several accessory non-structural proteins. SARS-CoV-2's most abundant structural protein, Membrane (M) protein, has a pivotal role both during viral infection cycle and host interferon antagonism. This is a highly conserved viral protein, thus an interesting and suitable target for drug discovery. In this paper, we explain the structural nature of M protein homodimer. To do so, we developed and applied a detailed and robust in silico workflow to predict M protein dimeric structure, membrane orientation, and interface characterization. Single Nucleotide Polymorphisms (SNPs) in M protein were retrieved from over 1.2 M SARS-CoV-2 genomes and proteins from the Global Initiative on Sharing All Influenza Data (GISAID) database, 91 of which were located at the predicted dimer interface. Among those, we identified SNPs in Variants of Concern (VOC) and Variants of Interest (VOI). Binding free energy differences were evaluated for dimer interfacial SNPs to infer mutant protein stabilities. A few high-prevalent mutated residues were found to be especially relevant in VOC and VOI. This realization may be a game-changer to structure-driven formulation of new therapeutics for SARS-CoV-2.

Indexed as

MutationPolymorphism, Single NucleotideBinding SitesCoronavirus M ProteinsCOVID-19Genome, ViralHumansMolecular Dynamics SimulationProtein BindingProtein DomainsProtein MultimerizationSARS-CoV-2Coronavirus M Proteinsmembrane protein, SARS-CoV-2genomicsproteomicsSARS-CoV-2

Identifiers

PMID35328409
PMCPMC8948900

What OpenQuestion holds

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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.