Evidence map›Paper›PMID 23325686›Full record

ArticleJournal of virology2013

Comparative proteomic analysis of HIV-1 particles reveals a role for Ezrin and EHD4 in the Nef-dependent increase of virus infectivity.

Christelle Brégnard, Alessia Zamborlini, Marjorie Leduc, Philippe Chafey, Luc Camoin, Ali Saïb, Serge Benichou, Olivier Danos, Stéphane Basmaciogullari

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 11% 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

31 citing papers in PubMed, 1 synthesis or guideline pooled it, 40 citations in OpenAlex.

  1. Pooled it
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  5. Functional 20S Proteasomes in Retroviruses: Evidence in Favor.International journal of molecular sciences · 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 5 institutions in 2 countries.

Christelle BrégnardHôpital Necker-Enfants Malades, Université Paris Descartes, Sorbonne Paris Cité, Paris, France.
Alessia Zamborlini
Marjorie Leduc
Philippe Chafey
Luc Camoin
Ali Saïb
Serge Benichou
Olivier Danos
Stéphane Basmaciogullari
Université Paris Cité · FRDélégation Paris 7 · FRInstitut Cochin · FRHôpital Necker-Enfants Malades · FRInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nef is a human immunodeficiency virus type 1 (HIV-1) auxiliary protein that plays an important role in virus replication and the onset of acquired immunodeficiency. Although known functions of Nef might explain its contribution to HIV-1-associated pathogenesis, how Nef increases virus infectivity is still an open question. In vitro, Nef-deleted viruses have a defect that prevents efficient completion of early steps of replication. We have previously shown that this restriction is not due to the absence of Nef in viral particles. Rather, a loss of function in virus-producing cells accounts for the lower infectivity of nef-deleted viruses compared to wild-type (WT) viruses. Here we used DiGE and iTRAQ to identify differences between the proteomes of WT and nef-deleted viruses. We observe that glucosidase II is enriched in WT virions, whereas Ezrin, ALG-2, CD81, and EHD4 are enriched in nef-deleted virions. Functional analysis shows that glucosidase II, ALG-2, and CD81 have no or only Nef-independent effect on infectivity. In contrast, Ezrin and EHD4 are involved in the ability of Nef to increase virus infectivity (referred to thereafter as Nef potency). Indeed, simultaneous Ezrin and EHD4 depletion in SupT1 and 293T virus-producing cells result in an ∼30 and ∼70% decrease of Nef potency, respectively. Finally, while Ezrin behaves as an inhibitory factor counteracted by Nef, EHD4 should be considered as a cofactors required by Nef to increase virus infectivity.

Indexed as

alpha-GlucosidasesBlotting, WesternCytoskeletal ProteinsDNA-Binding ProteinsElectrophoresisEzrinGene SilencingHEK293 CellsHIV-1Humansnef Gene Products, Human Immunodeficiency VirusNuclear ProteinsProteomicsRNA, Small InterferingTetraspanin 28Ultracentrifugation4-nitrophenyl-alpha-glucosidasealpha-GlucosidasesCD81 protein, humanCytoskeletal ProteinsDNA-Binding ProteinsEHD4 protein, humanEzrinnef Gene Products, Human Immunodeficiency Virusnef protein, Human immunodeficiency virus 1Nuclear ProteinsRNA, Small InterferingTetraspanin 28

Identifiers

PMID23325686
PMCPMC3624205
OpenAlexW2040311458

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.