Evidence map›Paper›PMID 28900197›Full record

ArticleScientific reports2017

Structural insights into the Middle East respiratory syndrome coronavirus 4a protein and its dsRNA binding mechanism.

Maria Batool, Masaud Shah, Mahesh Chandra Patra, Dhanusha Yesudhas, Sangdun Choi

Registry-linked trialOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT04934111 (A Clinical Trial to Assess the Safety and Immunogenicity of LNP-nCOV saRNA-02, a Self-amplifying Ribonucleic Acid), which is not on this map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.9field-weighted citation impact, top 10% 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.

NCT04934111 phase1unknown statusnot on this mapstarted 2021, after this paper: background citation

A Clinical Trial to Assess the Safety and Immunogenicity of LNP-nCOV saRNA-02, a Self-amplifying Ribonucleic Acid (saRNA) Vaccine, in SARS-CoV-2 Seronegative and Seropositive Uganda Population

TypeinterventionalSponsorMRC/UVRI and LSHTM Uganda Research UnitRan2021 to 2022Enrolled42ConditionsCOVID-19ArmsLNP-nCOV saRNA-02 Vaccine
3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Innate Inhibiting Proteins Enhance Expression and Immunogenicity of Self-Amplifying RNA.Molecular therapy : the journal of the American Society of Gene Therapy · 2021
    Article
  8. Review
  9. Article
  10. Article
  11. Overview of lethal human coronaviruses.Signal transduction and targeted therapy · 2020
    Review
  12. Article
  13. Article
  14. MERS coronavirus outbreak: Implications for emerging viral infections.Diagnostic microbiology and infectious disease · 2019
    Review
  15. Review
  16. Review
  17. Prospects for a MERS-CoV spike vaccine.Expert review of vaccines · 2018
    Review
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

5 authors at 1 institution in 1 country.

Maria BatoolDepartment of Molecular Science and Technology, Ajou University, Suwon, 16499, South Korea.
Masaud ShahDepartment of Molecular Science and Technology, Ajou University, Suwon, 16499, South Korea.
Mahesh Chandra PatraDepartment of Molecular Science and Technology, Ajou University, Suwon, 16499, South Korea.
Dhanusha YesudhasDepartment of Molecular Science and Technology, Ajou University, Suwon, 16499, South Korea.
Sangdun ChoiDepartment of Molecular Science and Technology, Ajou University, Suwon, 16499, South Korea. sangdunchoi@ajou.ac.kr.
Ajou University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Middle East respiratory syndrome coronavirus (MERS-CoV) has evolved to navigate through the sophisticated network of a host's immune system. The immune evasion mechanism including type 1 interferon and protein kinase R-mediated antiviral stress responses has been recently attributed to the involvement of MERS-CoV protein 4a (p4a) that masks the viral dsRNA. However, the structural mechanism of how p4a recognizes and establishes contacts with dsRNA is not well explained. In this study, we report a dynamic mechanism deployed by p4a to engage the viral dsRNA and make it unavailable to the host immune system. Multiple variants of p4a-dsRNA were created and investigated through extensive molecular dynamics procedures to highlight crucial interfacial residues that may be used as potential pharmacophores for future drug development. The structural analysis revealed that p4a exhibits a typical αβββα fold structure, as found in other dsRNA-binding proteins. The α1 helix and the β1-β2 loop play a crucial role in recognizing and establishing contacts with the minor grooves of dsRNA. Further, mutational and binding free energy analyses suggested that in addition to K63 and K67, two other residues, K27 and W45, might also be crucial for p4a-dsRNA stability.

Indexed as

Amino Acid SequenceCoronavirus InfectionsHydrogen BondingMiddle East Respiratory Syndrome CoronavirusModels, MolecularMolecular ConformationMutagenesisProtein BindingRNA, Double-StrandedRNA, ViralStructure-Activity RelationshipViral ProteinsRNA, Double-StrandedRNA, ViralViral Proteins

Identifiers

PMID28900197
PMCPMC5596018
OpenAlexW2752563075

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.