Evidence map›Paper›PMID 30700731›Full record

ArticleScientific reports2019

Quantitative monitoring of the cytoplasmic release of NCp7 proteins from individual HIV-1 viral cores during the early steps of infection.

Sarwat Zgheib, Iryna Lysova, Eleonore Réal, Oleksii Dukhno, Romain Vauchelles, Manuel Pires, Halina Anton, Yves Mély

Abstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Article
  2. Studying SARS-CoV-2 with Fluorescence Microscopy.International journal of molecular sciences · 2021
    Review
  3. Review
  4. Review
  5. 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

8 authors.

Sarwat ZgheibLaboratory of Bioimaging and Pathologies, UMR 7021 CNRS, Faculty of Pharmacy, Université de Strasbourg, 67401, Illkirch, France.
Iryna LysovaLaboratory of Bioimaging and Pathologies, UMR 7021 CNRS, Faculty of Pharmacy, Université de Strasbourg, 67401, Illkirch, France.
Eleonore RéalLaboratory of Bioimaging and Pathologies, UMR 7021 CNRS, Faculty of Pharmacy, Université de Strasbourg, 67401, Illkirch, France.
Oleksii DukhnoLaboratory of Bioimaging and Pathologies, UMR 7021 CNRS, Faculty of Pharmacy, Université de Strasbourg, 67401, Illkirch, France.
Romain VauchellesLaboratory of Bioimaging and Pathologies, UMR 7021 CNRS, Faculty of Pharmacy, Université de Strasbourg, 67401, Illkirch, France.
Manuel PiresLaboratory of Bioimaging and Pathologies, UMR 7021 CNRS, Faculty of Pharmacy, Université de Strasbourg, 67401, Illkirch, France.
Halina AntonLaboratory of Bioimaging and Pathologies, UMR 7021 CNRS, Faculty of Pharmacy, Université de Strasbourg, 67401, Illkirch, France. halina.anton@unistra.fr.ORCID 0000-0003-1304-8671
Yves MélyLaboratory of Bioimaging and Pathologies, UMR 7021 CNRS, Faculty of Pharmacy, Université de Strasbourg, 67401, Illkirch, France. yves.mely@unistra.fr.ORCID 0000-0001-7328-8269

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorescence microscopy imaging of individual HIV-1 viruses necessitates a specific labeling of viral structures that minimally perturbs the infection process. Herein, we used HIV-1 pseudoviruses containing NCp7 fused to a tetracystein (TC) tag, labeled by a biarsenical fluorescein derivative (FlAsH) to quantitatively monitor the NCp7 protein concentration in the viral cores during the early stages of infection. Single particle imaging of individual pseudoviruses with defined ratios of TC-tagged to non tagged NCp7 proteins, together with theoretical modeling of energy transfer between FlAsH dyes, showed that the high packaging of TC-tagged proteins in the viral cores causes a strong fluorescence quenching of FlAsH and that the fluorescence intensity of individual viral complexes is an appropriate parameter to monitor changes in the amount of NCp7 molecules within the viral particles during infection. Interestingly, we observed a dramatic fluorescence increase of individual FlAsH-labeled pseudoviruses containing 100% TC-tagged NCp7 proteins in infected cells at 8 and 16 h post-infection. This effect was significantly lower for pseudoviruses expressing TC-tagged integrase. Therefore, this fluorescence increase is likely related to the cytoplasmic viral transformation and the release of NCp7 molecules from the viral complexes. This loss of quenching effect is largely reduced when reverse transcriptase is inhibited, showing that NCp7 release is connected to viral DNA synthesis. A spatial analysis further revealed that NCp7-TC release is more pronounced in the perinuclear space, where capsid disassembly is thought to be completed. Quantification of NCp7-TC content based on fluorescence quenching presented in this study evidences for the first time the cytoplasmic release of NCp7 during the remodeling of HIV-1 viral particles on their journey toward the nucleus. The developed approach can be applied to quantify dye concentrations in a wide range of nano-objects by fluorescence microscopy techniques.

Indexed as

Virus AssemblyCytoplasmFluoresceingag Gene Products, Human Immunodeficiency VirusHeLa CellsHIV-1HIV InfectionsHumansMicroscopy, FluorescenceRecombinant Fusion ProteinsFluoresceingag Gene Products, Human Immunodeficiency VirusNCP7 protein, Human immunodeficiency virus 1Recombinant Fusion Proteins

Identifiers

PMID30700731
PMCPMC6353972

What Socratic 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 Socratic graph.