Evidence map›Paper›PMID 32132240›Full record

ArticleJournal of virology2020

Palmitoylated Cysteines in Chikungunya Virus nsP1 Are Critical for Targeting to Cholesterol-Rich Plasma Membrane Microdomains with Functional Consequences for Viral Genome Replication.

William Bakhache, Aymeric Neyret, Eric Bernard, Andres Merits, Laurence Briant

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

25 citing papers in PubMed, 32 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 2 institutions in 2 countries.

William BakhacheIRIM, University of Montpellier, CNRS UMR9004, Montpellier, France.
Aymeric NeyretIRIM, University of Montpellier, CNRS UMR9004, Montpellier, France.
Eric BernardIRIM, University of Montpellier, CNRS UMR9004, Montpellier, France.
Andres MeritsInstitute of Technology, University of Tartu, Tartu, Estonia.ORCID 0000-0001-8193-0071
Laurence BriantIRIM, University of Montpellier, CNRS UMR9004, Montpellier, France laurence.briant@irim.cnrs.fr.
Centre National de la Recherche Scientifique · FRUniversity of Tartu · EE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In mammalian cells, alphavirus replication complexes are anchored to the plasma membrane. This interaction with lipid bilayers is mediated through the viral methyl/guanylyltransferase nsP1 and reinforced by palmitoylation of cysteine residue(s) in the C-terminal region of this protein. Lipid content of membranes supporting nsP1 anchoring remains poorly studied. Here, we explore the membrane binding capacity of nsP1 with regard to cholesterol. Using the medically important chikungunya virus (CHIKV) as a model, we report that nsP1 cosegregates with cholesterol-rich detergent-resistant membrane microdomains (DRMs), also called lipid rafts. In search for the critical factor for cholesterol partitioning, we identify nsP1 palmitoylated cysteines as major players in this process. In cells infected with CHIKV or transfected with CHIKV

Indexed as

AnimalsCell LineCell MembraneChikungunya FeverChikungunya virusChlorocebus aethiopsCholesterolCysteineEndosomesHEK293 CellsHeLa CellsHumansLipoylationMembrane MicrodomainsSindbis VirusVero CellsCholesterolCysteinensP1 protein, Sindbis virusViral Nonstructural Proteinsalphaviruschikungunya viruscholesterolmethyl/guanylyltransferaseplasma membranereplication complexes

Identifiers

PMID32132240
PMCPMC7199415
OpenAlexW3010155983

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.