Evidence map›Paper›PMID 22072773›Full record

ArticleJournal of virology2012

Ex vivo and in vivo inhibition of human rhinovirus replication by a new pseudosubstrate of viral 2A protease.

Nisrine Falah, Sébastien Violot, Didier Décimo, Fatma Berri, Marie-Laure Foucault-Grunenwald, Théophile Ohlmann, Isabelle Schuffenecker, Florence Morfin, Bruno Lina, Béatrice Riteau and 1 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

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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

11 authors at 5 institutions in 1 country.

Nisrine FalahVirPath, EMR 4610, Virologie et Pathologie Humaine, Université Lyon 1, Université de Lyon, Faculté de Médecine Lyon-Est, Secteur Laennec, Lyon, France.
Sébastien Violot
Didier Décimo
Fatma Berri
Marie-Laure Foucault-Grunenwald
Théophile Ohlmann
Isabelle Schuffenecker
Florence Morfin
Bruno Lina
Béatrice Riteau
Jean-Claude Cortay
Université Claude Bernard Lyon 1 · FRHospices Civils de Lyon · FRVirologie et Pathologies Humaines · FRInserm · FRStructural and Molecular Basis of Infectious Systems · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human rhinoviruses (HRVs) remain a significant public health problem as they are the major cause of both upper and lower respiratory tract infections. Unfortunately, to date no vaccine or antiviral against these pathogens is available. Here, using a high-throughput yeast two-hybrid screening, we identified a 6-amino-acid hit peptide, LVLQTM, which acted as a pseudosubstrate of the viral 2A cysteine protease (2A(pro)) and inhibited its activity. This peptide was chemically modified with a reactive electrophilic fluoromethylketone group to form a covalent linkage with the nucleophilic active-site thiol of the enzyme. Ex vivo and in vivo experiments showed that thus converted, LVLQTM was a strong inhibitor of HRV replication in both A549 cells and mice. To our knowledge, this is the first report validating a compound against HRV infection in a mouse model.

Indexed as

Down-RegulationVirus ReplicationAmino Acid SequenceAnimalsCysteine EndopeptidasesFemaleHumansMiceMice, Inbred BALB CMolecular Sequence DataPeptidesPicornaviridae InfectionsProtein BindingRhinovirusSequence AlignmentSubstrate SpecificityCysteine EndopeptidasesPeptidespicornain 2A, PicornavirusViral Proteins

Identifiers

PMID22072773
PMCPMC3255852
OpenAlexW2087199210

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.