Evidence map›Paper›PMID 26031340›Full record

ArticleTraffic (Copenhagen, Denmark)2015

Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets.

Nestor G Iglesias, Juan A Mondotte, Laura A Byk, Federico A De Maio, Marcelo M Samsa, Cecilia Alvarez, Andrea V Gamarnik

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
10.3field-weighted citation impact, top 2% 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

46 citing papers in PubMed, 73 citations in OpenAlex.

  1. Review
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  7. Arfs on the Golgi: four conductors, one orchestra.Frontiers in molecular biosciences · 2025
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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

7 authors at 2 institutions in 1 country.

Nestor G IglesiasFundación Instituto Leloir-CONICET, Avenida Patricias Argentinas 435, Buenos Aires, 1405, Argentina.
Juan A MondotteFundación Instituto Leloir-CONICET, Avenida Patricias Argentinas 435, Buenos Aires, 1405, Argentina.
Laura A BykFundación Instituto Leloir-CONICET, Avenida Patricias Argentinas 435, Buenos Aires, 1405, Argentina.
Federico A De MaioFundación Instituto Leloir-CONICET, Avenida Patricias Argentinas 435, Buenos Aires, 1405, Argentina.
Marcelo M SamsaFundación Instituto Leloir-CONICET, Avenida Patricias Argentinas 435, Buenos Aires, 1405, Argentina.
Cecilia AlvarezCentro de Investigaciones en Bioquímica Clínica e Inmunología-CONICET, Departamento de Bioquímica Clínica, Facultad de Ciencias Químicas, UNC, 5000, Córdoba, Argentina.
Andrea V GamarnikFundación Instituto Leloir-CONICET, Avenida Patricias Argentinas 435, Buenos Aires, 1405, Argentina.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARFundación Instituto Leloir · AR

Funding

MECHANISMS OF DENGUE VIRUS GENOME ENCAPSIDATION AND UNCOATINGR01AI095175 · NIAID · FUNDACION INSTITUTO LELOIR · PI GAMARNIK, ANDREA · 2011 to 2020
$1.0M
NIAID NIH HHS R01 AI095175NIAID NIH HHS R01.AI095175-01PHS HHS PICT 2010-1141
6 · The paper itself

Abstract

Dengue viruses cause the most important human viral disease transmitted by mosquitoes. In recent years, a great deal has been learned about molecular details of dengue virus genome replication; however, little is known about genome encapsidation and the functions of the viral capsid protein. During infection, dengue virus capsid progressively accumulates around lipid droplets (LDs) by an unknown mechanism. Here, we examined the process by which the viral capsid is transported from the endoplasmic reticulum (ER) membrane, where the protein is synthesized, to LDs. Using different methods of intervention, we found that the GBF1-Arf1/Arf4-COPI pathway is necessary for capsid transport to LDs, while the process is independent of both COPII components and Golgi integrity. The transport was sensitive to Brefeldin A, while a drug resistant form of GBF1 was sufficient to restore capsid subcellular distribution in infected cells. The mechanism by which LDs gain or lose proteins is still an open question. Our results support a model in which the virus uses a non-canonical function of the COPI system for capsid accumulation on LDs, providing new ideas for antiviral strategies.

Indexed as

ADP-Ribosylation Factor 1Capsid ProteinsCell Line, TumorCoat Protein Complex IDengue VirusEndoplasmic ReticulumGuanine Nucleotide Exchange FactorsHumansLipid DropletsProtein TransportADP-Ribosylation Factor 1Capsid ProteinsCoat Protein Complex IGBF1 protein, humanGuanine Nucleotide Exchange Factorscapsid proteinCOPIdengue virusflavivirusGBF1lipid droplets

Identifiers

PMID26031340
PMCPMC4543523
OpenAlexW1880359614

What OpenQuestion holds

Textmetadata
LicenceTDM
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.