Evidence map›Paper›PMID 30813555›Full record

ArticleViruses2019

Lipid Exchange Factors at Membrane Contact Sites in African Swine Fever Virus Infection.

Inmaculada Galindo, Miguel Ángel Cuesta-Geijo, Ana Del Puerto, Eva Soriano, Covadonga Alonso

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 14 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 1 institution in 1 country.

Inmaculada GalindoDepartment Biotecnología, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA), Ctra. de la Coruña km 7.5, 28040 Madrid, Spain. galindo@inia.es.
Miguel Ángel Cuesta-GeijoDepartment Biotecnología, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA), Ctra. de la Coruña km 7.5, 28040 Madrid, Spain. cuesta.miguelangel@inia.es.
Ana Del PuertoDepartment Biotecnología, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA), Ctra. de la Coruña km 7.5, 28040 Madrid, Spain. delpuerto.ana@inia.es.
Eva SorianoDepartment Biotecnología, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA), Ctra. de la Coruña km 7.5, 28040 Madrid, Spain. e.sorianojerez@pgr.reading.ac.uk.ORCID 0000-0003-3125-1833
Covadonga AlonsoDepartment Biotecnología, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA), Ctra. de la Coruña km 7.5, 28040 Madrid, Spain. calonso@inia.es.ORCID 0000-0002-0862-6177
Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

African swine fever (ASF) is a hemorrhagic fever of wild and domestic pigs with a high rate of mortality. Originally endemic in Africa, this disease is currently disseminating in Europe and China, causing a large socioeconomic impact. ASF is caused by a DNA virus, African swine fever virus (ASFV). There is no vaccine available against ASFV, limiting the options for disease control. ASFV reorganizes intracellular membranes to generate viral factories (VFs) in order to amplify its genome. However, little is known about the process involved in the formation of these viral replication organelles. Membrane contact sites (MCSs) allow nonvesicular lipids and ion exchange between organelles. Lipid exchange to form VFs apparently requires a number of proteins at MCSs, such as the oxysterol-binding protein (OSBP), the acyl-coenzyme A binding domain containing 3 (ACBD3) and the phosphatidylinositol-phosphate-4-kinase III beta (PI4Kβ). Itraconazole (ITZ) is an antifungal agent that targets sterol-transport molecules such as OSBP and OSBP-related protein 4 (ORP4). 25-Hydroxycholesterol (25-HC) inhibits lipid transport by high affinity binding OSBP. In this work, we analyzed the antiviral function of ITZ and 25-HC against ASFV in Vero cell cultures using the cell-adapted Ba71V isolate. ITZ and 25-HC decreased significantly ASFV replication. Our study revealed OSBP distribution in cytoplasmic membranes in uninfected Vero cells and to the periphery of VFs in infected cells. In addition, we showed that OSBP and OSBP-related proteins, PI4Kβ and ACBD3 were recruited to VFs in the context ASFV infection.

Indexed as

Host Microbial InteractionsLipid MetabolismVirus AttachmentAdaptor Proteins, Signal TransducingAfrican Swine FeverAfrican Swine Fever VirusAnimalsAntiviral AgentsChlorocebus aethiopsGenome, ViralHeLa CellsHumansHydroxycholesterolsItraconazoleMembrane ProteinsMinor Histocompatibility Antigens25-hydroxycholesterolACBD3 protein, humanAdaptor Proteins, Signal TransducingAntiviral AgentsHydroxycholesterolsItraconazoleMembrane ProteinsMinor Histocompatibility AntigensOxysterol Binding Proteinsphosphatidylinositol phosphate 4-kinasePhosphotransferases (Alcohol Group Acceptor)Receptors, Steroid25-HCACBD3African swine fever virusitraconazolelipidsmembrane contact sitesOSBPPI4Kβsterol transportviral factory

Identifiers

PMID30813555
PMCPMC6466349
OpenAlexW2916879035

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.