Evidence map›Paper›PMID 36432196›Full record

ArticleMolecules (Basel, Switzerland)2022

Neuropeptides, New Ligands of SARS-CoV-2 Nucleoprotein, a Potential Link between Replication, Inflammation and Neurotransmission.

Julien Henri, Laetitia Minder, Kevin Mohanasundaram, Sébastien Dilly, Anne Goupil-Lamy, Carmelo Di Primo, Anny Slama Schwok

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Review
  3. Potential Anti-SARS-CoV-2 Molecular Strategies.Molecules (Basel, Switzerland) · 2023
    Article
  4. 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 at 3 institutions in 1 country.

Julien HenriLaboratoire de Biologie Computationnelle et Quantitative, Institut de Biologie Paris-Seine, UMR-CNRS 7238, Sorbonne Université, F-75005 Paris, France.ORCID 0000-0003-0772-8881
Laetitia MinderInstitut Européen de Chimie et Biologie (IECB), CNRS, INSERM UAR 3033, US001, Univ. Bordeaux, F-33000 Bordeaux, France.
Kevin MohanasundaramSaint Antoine Hospital, Centre de Recherche Saint Antoine, Sorbonne Université, Biology and Cancer Therapeutics, INSERM U938, F-75231 Paris, France.
Sébastien DillySaint Antoine Hospital, Centre de Recherche Saint Antoine, Sorbonne Université, Biology and Cancer Therapeutics, INSERM U938, F-75231 Paris, France.
Anne Goupil-LamyBiovia, Dassault Systèmes, 10 Rue Marcel Dassault, CS40501, CEDEX, F-78946 Vélizy-Villacoublay, France.
Carmelo Di PrimoCNRS, INSERM, ARNA, UMR 5320, U1212, IECB, Univ. Bordeaux, F-33000 Bordeaux, France.ORCID 0000-0002-0509-8399
Anny Slama SchwokSaint Antoine Hospital, Centre de Recherche Saint Antoine, Sorbonne Université, Biology and Cancer Therapeutics, INSERM U938, F-75231 Paris, France.ORCID 0000-0002-2703-9728
Centre National de la Recherche Scientifique · FRInserm · FRDassault Systèmes (France) · FR

Funding

The CovNucleovir from the faculty of Medicine of Sorbonne University CoVNucleovirThe Sorbonne University Foundation CoVNucleovir
6 · The paper itself

Abstract

This work identifies new ligands of the nucleoprotein N of SARS-CoV-2 by in silico screening, which used a new model of N, built from an Alphafold model refined by molecular dynamic simulations. The ligands were neuropeptides, such as substance P (1-7) and enkephalin, bound at a large site of the C-terminal or associated with the N-terminal β-sheet. The BA4 and BA5 Omicron variants of N also exhibited a large site as in wt N, and an increased flexibility of the BA5 variant, enabling substance P binding. The binding sites of some ligands deduced from modeling in wt N were assessed by mutation studies in surface plasmon resonance experiments. Dynamic light scattering showed that the ligands impeded RNA binding to N, which likely inhibited replication. We suggest that the physiological role of these neuropeptides in neurotransmission, pain and vasodilation for cholecystokinin and substance P could be altered by binding to N. We speculate that N may link between viral replication and multiple pathways leading to long COVID-19 symptoms. Therefore, N may constitute a "danger hub" that needs to be inhibited, even at high cost for the host. Antivirals targeted to N may therefore reduce the risk of brain fog and stroke, and improve patients' health.

Indexed as

COVID-19NeuropeptidesHumansInflammationLigandsNucleoproteinsPost-Acute COVID-19 SyndromeSARS-CoV-2Substance PSynaptic TransmissionLigandsNeuropeptidesNucleoproteinsSubstance Palphafold model and molecular dynamicsbrain fogmetabolismneuroinflammationneuropeptidesneurotransmissionnucleocapsid or nucleoproteinSARS-CoV-2structure-based drug discovery

Identifiers

PMID36432196
PMCPMC9698730
OpenAlexW4309718269

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.