Evidence map›Paper›PMID 34128351›Full record

ArticlePharmacology research & perspectives2021

p-cymene impairs SARS-CoV-2 and Influenza A (H1N1) viral replication: In silico predicted interaction with SARS-CoV-2 nucleocapsid protein and H1N1 nucleoprotein.

Athanasios Panagiotopoulos, Melpomeni Tseliou, Ioannis Karakasiliotis, Danai-Maria Kotzampasi, Vangelis Daskalakis, Nikolaos Kesesidis, George Notas, Christos Lionis, Marilena Kampa, Stergios Pirintsos and 2 more

Open access · goldAbstract read
In one paragraph

Article in Pharmacology research & perspectives, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
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  3. International journal of molecular sciences · 2024
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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

12 authors at 3 institutions in 2 countries.

Athanasios PanagiotopoulosLaboratory of Experimental Endocrinology, School of Medicine, University of Crete, Heraklion, Greece.
Melpomeni TseliouLaboratory of Clinical Virology, School of Medicine, University of Crete, Heraklion, Greece.
Ioannis KarakasiliotisLaboratory of Biology, School of Medicine, Democritus University of Thrace, Alexandroupolis, Greece.
Danai-Maria KotzampasiLaboratory of Experimental Endocrinology, School of Medicine, University of Crete, Heraklion, Greece.
Vangelis DaskalakisDepartment of Chemical Engineering, Cyprus University of Technology, Limassol, Cyprus.ORCID 0000-0001-8870-0850
Nikolaos KesesidisLaboratory of Biology, School of Medicine, Democritus University of Thrace, Alexandroupolis, Greece.
George NotasLaboratory of Experimental Endocrinology, School of Medicine, University of Crete, Heraklion, Greece.
Christos LionisClinic of Social and Family Medicine, School of Medicine, University of Crete, Heraklion, Greece.
Marilena KampaLaboratory of Experimental Endocrinology, School of Medicine, University of Crete, Heraklion, Greece.ORCID 0000-0002-6324-9570
Stergios PirintsosNature Crete Pharmaceuticals, Heraklion, Greece.
George SourvinosLaboratory of Clinical Virology, School of Medicine, University of Crete, Heraklion, Greece.
Elias CastanasLaboratory of Experimental Endocrinology, School of Medicine, University of Crete, Heraklion, Greece.ORCID 0000-0002-8370-1835
University of Crete · GRDemocritus University of Thrace · GRCyprus University of Technology · CY

Funding

EU-Horizon 2020European Social Fund- ESF MIS-5000432Galenica SAHellenic Foundation for Research and Innovation (H.F.R.I.) 3725
6 · The paper itself

Abstract

Therapeutic regimens for the COVID-19 pandemics remain unmet. In this line, repurposing of existing drugs against known or predicted SARS-CoV-2 protein actions have been advanced, while natural products have also been tested. Here, we propose that p-cymene, a natural monoterpene, can act as a potential novel agent for the treatment of SARS-CoV-2-induced COVID-19 and other RNA-virus-induced diseases (influenza, rabies, Ebola). We show by extensive molecular simulations that SARS-CoV-2 C-terminal structured domain contains a nuclear localization signal (NLS), like SARS-CoV, on which p-cymene binds with low micromolar affinity, impairing nuclear translocation of this protein and inhibiting viral replication, as verified by preliminary in vitro experiments. A similar mechanism may occur in other RNA-viruses (influenza, rabies and Ebola), also verified in vitro for influenza, by interaction of p-cymene with viral nucleoproteins, and structural modification of their NLS site, weakening its interaction with importin A. This common mechanism of action renders therefore p-cymene as a possible antiviral, alone, or in combination with other agents, in a broad spectrum of RNA viruses, from SARS-CoV-2 to influenza A infections.

Indexed as

AnimalsAntiviral AgentsCell NucleusChlorocebus aethiopsCymenesDogsHumansInfluenza A Virus, H1N1 SubtypeMadin Darby Canine Kidney CellsModels, MolecularMolecular Dynamics SimulationNuclear Localization SignalsNucleocapsid ProteinsProtein ConformationProtein DomainsProtein Transport4-cymeneAntiviral AgentsCymenesNuclear Localization SignalsNucleocapsid ProteinsEbolaimportin Ainfluenza Anucleocapsid proteinnucleoproteinp-cymenerabiesSARS-CoV-2

Identifiers

PMID34128351
PMCPMC8204097
OpenAlexW3171634274

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.