Evidence map›Paper›PMID 32785274›Full record

ArticlePloS one2020

Structural insight into the role of novel SARS-CoV-2 E protein: A potential target for vaccine development and other therapeutic strategies.

Manish Sarkar, Soham Saha

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.4field-weighted citation impact, top 6% 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

51 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Computational and structural biotechnology journal · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Lung fibrosis: Post-COVID-19 complications and evidences.International immunopharmacology · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Comparing the Cytokine Storms of COVID-19 and Pandemic Influenza.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2022
    Article
  18. Review
  19. Review
  20. Molecular and structural insights of β-boswellic acid and glycyrrhizic acid as potent SARS-CoV-2 Envelope protein inhibitors.Phytomedicine plus : international journal of phytotherapy and phytopharmacology · 2022
    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

2 authors at 2 institutions in 2 countries.

Manish SarkarDepartment of Biochemistry, Bose Institute, Kolkata, India.
Soham SahaLaboratory for Perception and Memory, Institut Pasteur, Paris, France.ORCID 0000-0003-1173-1397
Bose Institute · INCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The outbreak of COVID-19 across the world has posed unprecedented and global challenges on multiple fronts. Most of the vaccine and drug development has focused on the spike proteins and viral RNA-polymerases and main protease for viral replication. Using the bioinformatics and structural modelling approach, we modelled the structure of the envelope (E)-protein of novel SARS-CoV-2. The E-protein of this virus shares sequence similarity with that of SARS- CoV-1, and is highly conserved in the N-terminus regions. Incidentally, compared to spike proteins, E proteins demonstrate lower disparity and mutability among the isolated sequences. Using homology modelling, we found that the most favorable structure could function as a gated ion channel conducting H+ ions. Combining pocket estimation and docking with water, we determined that GLU 8 and ASN 15 in the N-terminal region were in close proximity to form H-bonds which was further validated by insertion of the E protein in an ERGIC-mimic membrane. Additionally, two distinct "core" structures were visible, the hydrophobic core and the central core, which may regulate the opening/closing of the channel. We propose this as a mechanism of viral ion channeling activity which plays a critical role in viral infection and pathogenesis. In addition, it provides a structural basis and additional avenues for vaccine development and generating therapeutic interventions against the virus.

Indexed as

BetacoronavirusComputer SimulationCoronavirus Envelope ProteinsCoronavirus InfectionsCOVID-19COVID-19 VaccinesHumansHydrogenHydrogen BondingMagnetic Resonance SpectroscopyModels, MolecularPandemicsPneumonia, ViralPoint MutationProtein ConformationSARS-CoV-2Coronavirus Envelope ProteinsCOVID-19 Vaccinesenvelope protein, SARS-CoV-2HydrogenVaccines, AttenuatedVaccines, InactivatedViral Envelope ProteinsViral VaccinesWater

Identifiers

PMID32785274
PMCPMC7423102
OpenAlexW3048538582

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.