Evidence map›Paper›PMID 24643062›Full record

ArticlePloS one2014

Caveolin-1 in lipid rafts interacts with dengue virus NS3 during polyprotein processing and replication in HMEC-1 cells.

Julio García Cordero, Moisés León Juárez, Jorge A González-Y-Merchand, Leticia Cedillo Barrón, Benito Gutiérrez Castañeda

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

29 citing papers in PubMed, 48 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

5 authors at 3 institutions in 1 country.

Julio García CorderoDepartamento de Biomedicina Molecular, Centro de Investigación y Estudios Avanzados del IPN, México City, México; Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas IPN, México City, México.
Moisés León JuárezDepartamento de Biomedicina Molecular, Centro de Investigación y Estudios Avanzados del IPN, México City, México.
Jorge A González-Y-MerchandDepartamento de Microbiología, Escuela Nacional de Ciencias Biológicas IPN, México City, México.
Leticia Cedillo BarrónDepartamento de Biomedicina Molecular, Centro de Investigación y Estudios Avanzados del IPN, México City, México.
Benito Gutiérrez CastañedaLaboratorio de Inmunología, Facultad de Estudios Superiores Iztacala Universidad Autónoma de México, Tlalnepantla Estado de México, México.
Center for Research and Advanced Studies of the National Polytechnic Institute · MXInstituto Politécnico Nacional · MXAutonomous University of Tlaxcala · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipid rafts are ordered microdomains within cellular membranes that are rich in cholesterol and sphingolipids. Caveolin (Cav-1) and flotillin (Flt-1) are markers of lipid rafts, which serve as an organizing center for biological phenomena and cellular signaling. Lipid rafts involvement in dengue virus (DENV) processing, replication, and assembly remains poorly characterized. Here, we investigated the role of lipid rafts after DENV endocytosis in human microvascular endothelial cells (HMEC-1). The non-structural viral proteins NS3 and NS2B, but not NS5, were associated with detergent-resistant membranes. In sucrose gradients, both NS3 and NS2B proteins appeared in Cav-1 and Flt-1 rich fractions. Additionally, double immunofluorescence staining of DENV-infected HMEC-1 cells showed that NS3 and NS2B, but not NS5, colocalized with Cav-1 and Flt-1. Furthermore, in HMEC-1cells transfected with NS3 protease, shown a strong overlap between NS3 and Cav-1, similar to that in DENV-infected cells. In contrast, double-stranded viral RNA (dsRNA) overlapped weakly with Cav-1 and Flt-1. Given these results, we investigated whether Cav-1 directly interacted with NS3. Cav-1 and NS3 co-immunoprecipitated, indicating that they resided within the same complex. Furthermore, when cellular cholesterol was depleted by methyl-beta cyclodextrin treatment after DENV entrance, lipid rafts were disrupted, NS3 protein level was reduced, besides Cav-1 and NS3 were displaced to fractions 9 and 10 in sucrose gradient analysis, and we observed a dramatically reduction of DENV particles release. These data demonstrate the essential role of caveolar cholesterol-rich lipid raft microdomains in DENV polyprotein processing and replication during the late stages of the DENV life cycle.

Indexed as

Caveolin 1Cell LineDEAD-box RNA HelicasesDengue VirusDetergentsEndothelial CellsHost-Pathogen InteractionsHumansMembrane MicrodomainsMembrane ProteinsNucleoside-TriphosphataseProtein BindingRNA HelicasesSerine EndopeptidasesViral Nonstructural ProteinsViral ProteasesCAV1 protein, humanCaveolin 1DEAD-box RNA HelicasesDetergentsflotillinsMembrane ProteinsNS2B protein, flavivirusNS3 protein, flavivirusNucleoside-TriphosphataseRNA HelicasesSerine EndopeptidasesViral Nonstructural ProteinsViral Proteases

Identifiers

PMID24643062
PMCPMC3958351
OpenAlexW2147882701

What OpenQuestion 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 OpenQuestion graph.