Evidence map›Paper›PMID 33986405›Full record

ArticleScientific reports2021

Repurposing potential of posaconazole and grazoprevir as inhibitors of SARS-CoV-2 helicase.

Syed Hani Abidi, Nahlah Makki Almansour, Daulet Amerzhanov, Khaled S Allemailem, Wardah Rafaqat, Mahmoud A A Ibrahim, Philip la Fleur, Martin Lukac, Syed Ali

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.4field-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.

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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. 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

9 authors at 5 institutions in 4 countries.

Syed Hani AbidiDepartment of Biological and Biomedical Sciences, Aga Khan University, Karachi, Pakistan.
Nahlah Makki AlmansourDepartment of Biology, College of Science, University of Hafr Al Batin, Hafr Al Batin, Saudi Arabia.
Daulet AmerzhanovNazarbayev University School of Medicine, Nazarbayev University, Astana, Kazakhstan.
Khaled S AllemailemDepartment of Medical Laboratories, College of Applied Medical Sciences, Qassim University, Buraydah, Saudi Arabia.
Wardah RafaqatMedical College, Aga Khan University, Karachi, Pakistan.
Mahmoud A A IbrahimComputational Chemistry Laboratory, Chemistry Department, Faculty of Science, Minia University, Minia, 61519, Egypt.
Philip la FleurNazarbayev University School of Medicine, Nazarbayev University, Astana, Kazakhstan.
Martin LukacDepartment of Computer Science, School of Engineering and Digital Sciences, Nazarbayev University, Astana, Kazakhstan.
Syed AliNazarbayev University School of Medicine, Nazarbayev University, Astana, Kazakhstan. syed.ali@nu.edu.kz.
Nazarbayev University · KZAga Khan University · PKMinia University · EGQassim University · SAUniversity of Hafr Al-Batin · SA

Funding

Phylodynamic Analysis of HIV Transmission Clusters in Kazakhstan for Targeted InterventionsR03DA052179 · NIDA · YALE UNIVERSITY · PI ALI, SYED, VERMUND, STEN H. · 2020 to 2021
$145k
Nazarbayev University 110119FD4516NIDA NIH HHS R03 DA052179NIDA NIH HHS R03DA052179Science and Technology Development Fund 5480
6 · The paper itself

Abstract

As the Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2) pandemic engulfs millions worldwide, the quest for vaccines or drugs against the virus continues. The helicase protein of SARS-CoV-2 represents an attractive target for drug discovery since inhibition of helicase activity can suppress viral replication. Using in silico approaches, we have identified drugs that interact with SARS-CoV-2 helicase based on the presence of amino acid arrangements matching binding sites of drugs in previously annotated protein structures. The drugs exhibiting an RMSD of ≤ 3.0 Å were further analyzed using molecular docking, molecular dynamics (MD) simulation, and post-MD analyses. Using these approaches, we found 12 drugs that showed strong interactions with SARS-CoV-2 helicase amino acids. The analyses were performed using the recently available SARS-CoV-2 helicase structure (PDB ID: 5RL6). Based on the MM-GBSA approach, out of the 12 drugs, two drugs, namely posaconazole and grazoprevir, showed the most favorable binding energy, - 54.8 and - 49.1 kcal/mol, respectively. Furthermore, of the amino acids found conserved among all human coronaviruses, 10/11 and 10/12 were targeted by, respectively, grazoprevir and posaconazole. These residues are part of the crucial DEAD-like helicase C and DEXXQc_Upf1-like/ DEAD-like helicase domains. Strong interactions of posaconazole and grazoprevir with conserved amino acids indicate that the drugs can be potent against SARS-CoV-2. Since the amino acids are conserved among the human coronaviruses, the virus is unlikely to develop resistance mutations against these drugs. Since these drugs are already in use, they may be immediately repurposed for SARS-CoV-2 therapy.

Indexed as

Drug RepositioningAmidesAntiviral AgentsCarbamatesCOVID-19 Drug TreatmentCyclopropanesEnzyme InhibitorsHumansLactams, MacrocyclicMolecular Docking SimulationMolecular Dynamics SimulationProtein DomainsQuinoxalinesRNA HelicasesSARS-CoV-2SulfonamidesAmidesAntiviral AgentsCarbamatesCyclopropanesEnzyme InhibitorsgrazoprevirLactams, MacrocyclicposaconazoleQuinoxalinesRNA HelicasesSulfonamidesTriazolesViral Proteins

Identifiers

PMID33986405
PMCPMC8119689
OpenAlexW3163058366

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.