Evidence map›Paper›PMID 32251731›Full record

ArticleInternational journal of antimicrobial agents2020

Structural and molecular modelling studies reveal a new mechanism of action of chloroquine and hydroxychloroquine against SARS-CoV-2 infection.

Jacques Fantini, Coralie Di Scala, Henri Chahinian, Nouara Yahi

Open access · greenAbstract read
In one paragraph

Article in International journal of antimicrobial agents, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 321 papers, 4 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
321citing papers in PubMed, 4 pooled it
13.7field-weighted citation impact, top 1% 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

321 citing papers in PubMed, 4 syntheses or guidelines pooled it, 576 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Pooled it
  4. Pooled it
  5. Trial
  6. Trial
  7. Trial
  8. Article
  9. Review
  10. Article
  11. Host Glycan-Lectin Interplay in SARS-CoV-2 Infection.International journal of molecular sciences · 2026
    Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Review
  19. Article
  20. Article

261 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Jacques FantiniINSERM UMR_S 1072, Marseille, France; Department of Biology, Aix-Marseille Université, Marseille, France. Electronic address: jacques.fantini@univ-amu.fr.
Coralie Di ScalaINMED, INSERM U1249, Parc Scientifique de Luminy, Marseille, France.
Henri ChahinianINSERM UMR_S 1072, Marseille, France; Department of Biology, Aix-Marseille Université, Marseille, France.
Nouara YahiINSERM UMR_S 1072, Marseille, France; Department of Biology, Aix-Marseille Université, Marseille, France.
Inserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The recent emergence of the novel pathogenic SARS-coronavirus 2 (SARS-CoV-2) is responsible for a worldwide pandemic. Given the global health emergency, drug repositioning is the most reliable option to design an efficient therapy for infected patients without delay. The first step of the viral replication cycle [i.e. attachment to the surface of respiratory cells, mediated by the spike (S) viral protein] offers several potential therapeutic targets. The S protein uses the angiotension-converting enzyme-2 (ACE-2) receptor for entry, but also sialic acids linked to host cell surface gangliosides. Using a combination of structural and molecular modelling approaches, this study showed that chloroquine (CLQ), one of the drugs currently under investigation for SARS-CoV-2 treatment, binds sialic acids and gangliosides with high affinity. A new type of ganglioside-binding domain at the tip of the N-terminal domain of the SARS-CoV-2 S protein was identified. This domain (111-158), which is fully conserved among clinical isolates worldwide, may improve attachment of the virus to lipid rafts and facilitate contact with the ACE-2 receptor. This study showed that, in the presence of CLQ [or its more active derivative, hydroxychloroquine (CLQ-OH)], the viral S protein is no longer able to bind gangliosides. The identification of this new mechanism of action of CLQ and CLQ-OH supports the use of these repositioned drugs to cure patients infected with SARS-CoV-2. The in-silico approaches used in this study might also be used to assess the efficiency of a broad range of repositioned and/or innovative drug candidates before clinical evaluation.

Indexed as

Amino Acid SequenceBetacoronavirusChloroquineCoronavirus InfectionsCOVID-19HumansHydroxychloroquineModels, MolecularMolecular Targeted TherapyPandemicsPneumonia, ViralProtein Structure, QuaternaryProtein Structure, TertiarySARS-CoV-2Sequence Analysis, ProteinSpike Glycoprotein, CoronavirusChloroquineHydroxychloroquineSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ChloroquineCoronavirusGangliosidePandemicSARS-CoV-2Spike

Identifiers

PMID32251731
PMCPMC7128678
OpenAlexW3015186638

What OpenQuestion holds

Textmetadata
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.