Evidence map›Paper›PMID 35765101›Full record

ArticleBMC pharmacology & toxicology2022

Identification of 2-(4-N,N-Dimethylaminophenyl)-5-methyl-1-phenethyl-1H-benzimidazole targeting HIV-1 CA capsid protein and inhibiting HIV-1 replication in cellulo.

Guzmán Alvarez, Lisa van Pul, Xavier Robert, Zoraima Artía, Ad C van Nuenen, Mathieu Long, Natalia Sierra, Williams Porcal, Neeltje A Kootstra, Christophe Guillon

Open access · goldAbstract read
In one paragraph

Article in BMC pharmacology & toxicology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 62% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

10 authors at 5 institutions in 3 countries.

Guzmán Alvarez *Laboratorio de Moléculas Bioactivas, Departamento de Ciencias Biológicas, CENUR Litoral Norte, Universidad de La República, 60000, Paysandú, Uruguay. guzmanalvarezlqo@gmail.com.
Lisa van Pul *Department of Experimental Immunology, Amsterdam UMC, Amsterdam Infection & Immunity Institute, University of Amsterdam, 1105 AZ, Amsterdam, the Netherlands.
Xavier RobertRetroviruses and Structural Biochemistry, UMR5086, Université de Lyon, CNRS, MMSB, 69367, Lyon, France.
Zoraima ArtíaLaboratorio de Moléculas Bioactivas, Departamento de Ciencias Biológicas, CENUR Litoral Norte, Universidad de La República, 60000, Paysandú, Uruguay.
Ad C van NuenenDepartment of Experimental Immunology, Amsterdam UMC, Amsterdam Infection & Immunity Institute, University of Amsterdam, 1105 AZ, Amsterdam, the Netherlands.
Mathieu LongRetroviruses and Structural Biochemistry, UMR5086, Université de Lyon, CNRS, MMSB, 69367, Lyon, France.
Natalia SierraLaboratorio de Moléculas Bioactivas, Departamento de Ciencias Biológicas, CENUR Litoral Norte, Universidad de La República, 60000, Paysandú, Uruguay.
Williams PorcalDepartamento de Química Orgánica, Facultad de Química, Universidad de La República, 11800, Montevideo, Uruguay.
Neeltje A KootstraDepartment of Experimental Immunology, Amsterdam UMC, Amsterdam Infection & Immunity Institute, University of Amsterdam, 1105 AZ, Amsterdam, the Netherlands. n.a.kootstra@amsterdamumc.nl.
Christophe GuillonRetroviruses and Structural Biochemistry, UMR5086, Université de Lyon, CNRS, MMSB, 69367, Lyon, France. christophe.guillon@ibcp.fr.
Universidad de la República · UYUniversité Claude Bernard Lyon 1 · FRUniversity of Amsterdam · NLAmsterdam University Medical Centers · NLCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The capsid (CA) subunit of the HIV-1 Gag polyprotein is involved in several steps of the viral cycle, from the assembly of new viral particles to the protection of the viral genome until it enters into the nucleus of newly infected cells. As such, it represents an interesting therapeutic target to tackle HIV infection. In this study, we screened hundreds of compounds with a low cost of synthesis for their ability to interfere with Gag assembly in vitro. Representatives of the most promising families of compounds were then tested for their ability to inhibit HIV-1 replication in cellulo. From these molecules, a hit compound from the benzimidazole family with high metabolic stability and low toxicity, 2-(4-N,N-dimethylaminophenyl)-5-methyl-1-phenethyl-1H-benzimidazole (696), appeared to block HIV-1 replication with an IC50 of 3 µM. Quantitative PCR experiments demonstrated that 696 does not block HIV-1 infection before the end of reverse transcription, and molecular docking confirmed that 696 is likely to bind at the interface between two monomers of CA and interfere with capsid oligomerization. Altogether, 696 represents a promising lead molecule for the development of a new series of HIV-1 inhibitors.

Indexed as

HIV-1HIV InfectionsBenzimidazolesCapsid ProteinsHumansMolecular Docking SimulationVirus ReplicationBenzimidazolesCapsid ProteinsBenzimidazoleCACapsidHIV-1Inhibitorp24

Identifiers

PMID35765101
PMCPMC9241302
OpenAlexW4283705397

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.