Evidence map›Paper›PMID 33946304›Full record

ArticleViruses2021

Inhibitors of Protein Glycosylation Are Active against the Coronavirus Severe Acute Respiratory Syndrome Coronavirus SARS-CoV-2.

Sreejith Rajasekharan, Rafaela Milan Bonotto, Lais Nascimento Alves, Yvette Kazungu, Monica Poggianella, Pamela Martinez-Orellana, Natasa Skoko, Sulena Polez, Alessandro Marcello

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

30 citing papers in PubMed, 54 citations in OpenAlex.

  1. Trial
  2. Molecules (Basel, Switzerland) · 2026
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  10. ACS central science · 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

9 authors at 1 institution in 1 country.

Sreejith RajasekharanLaboratory of Molecular Virology, International Centre for Genetic Engineering and Biotechnology (ICGEB) Padriciano, 99-34149 Trieste, Italy.
Rafaela Milan BonottoLaboratory of Molecular Virology, International Centre for Genetic Engineering and Biotechnology (ICGEB) Padriciano, 99-34149 Trieste, Italy.
Lais Nascimento AlvesLaboratory of Molecular Virology, International Centre for Genetic Engineering and Biotechnology (ICGEB) Padriciano, 99-34149 Trieste, Italy.
Yvette KazunguLaboratory of Molecular Virology, International Centre for Genetic Engineering and Biotechnology (ICGEB) Padriciano, 99-34149 Trieste, Italy.
Monica PoggianellaLaboratory of Molecular Virology, International Centre for Genetic Engineering and Biotechnology (ICGEB) Padriciano, 99-34149 Trieste, Italy.
Pamela Martinez-OrellanaLaboratory of Molecular Virology, International Centre for Genetic Engineering and Biotechnology (ICGEB) Padriciano, 99-34149 Trieste, Italy.
Natasa SkokoBiotechnology Development, International Centre for Genetic Engineering and Biotechnology (ICGEB) Padriciano, 99-34149 Trieste, Italy.
Sulena PolezBiotechnology Development, International Centre for Genetic Engineering and Biotechnology (ICGEB) Padriciano, 99-34149 Trieste, Italy.
Alessandro MarcelloLaboratory of Molecular Virology, International Centre for Genetic Engineering and Biotechnology (ICGEB) Padriciano, 99-34149 Trieste, Italy.ORCID 0000-0002-8903-8202
International Centre for Genetic Engineering and Biotechnology · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Repurposing clinically available drugs to treat the new coronavirus disease 2019 (COVID-19) is an urgent need in the course of the Severe Acute Respiratory Syndrome coronavirus (SARS-CoV-2) pandemic, as very few treatment options are available. The iminosugar Miglustat is a well-characterized drug for the treatment of rare genetic lysosome storage diseases, such as Gaucher and Niemann-Pick type C, and has also been described to be active against a variety of enveloped viruses. The activity of Miglustat is here demonstrated in the micromolar range for SARS-CoV-2 in vitro. The drug acts at the post-entry level and leads to a marked decrease of viral proteins and release of infectious viruses. The mechanism resides in the inhibitory activity toward α-glucosidases that are involved in the early stages of glycoprotein N-linked oligosaccharide processing in the endoplasmic reticulum, leading to a marked decrease of the viral Spike protein. Indeed, the antiviral potential of protein glycosylation inhibitors against SARS-CoV-2 is further highlighted by the low-micromolar activity of the investigational drug Celgosivir. These data point to a relevant role of this approach for the treatment of COVID-19.

Indexed as

Drug Repositioning1-DeoxynojirimycinA549 CellsAnimalsAntiviral AgentsChlorocebus aethiopsCOVID-19 Drug TreatmentGlycoside Hydrolase InhibitorsGlycosylationHEK293 CellsHumansIndolizidinesIndolizinesSARS-CoV-2Spike Glycoprotein, CoronavirusVero Cells1-DeoxynojirimycinAntiviral AgentscelgosivirGlycoside Hydrolase InhibitorsIndolizidinesIndolizinesmiglustatSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2antiviralCelgosivircoronavirusCOVID-19inhibitorMiglustatSARS-CoV-2spike

Identifiers

PMID33946304
PMCPMC8144969
OpenAlexW3158999144

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.