Evidence map›Paper›PMID 22573858›Full record

ArticleJournal of virology2012

Ebolavirus requires acid sphingomyelinase activity and plasma membrane sphingomyelin for infection.

Mary E Miller, Shramika Adhikary, Andrey A Kolokoltsov, Robert A Davey

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

90 citing papers in PubMed, 144 citations in OpenAlex.

  1. Article
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  11. Article
  12. Review
  13. Review
  14. Entry inhibitors as arenavirus antivirals.Frontiers in microbiology · 2024
    Review
  15. Review
  16. The Implication of Sphingolipids in Viral Infections.International journal of molecular sciences · 2023
    Review
  17. Article
  18. HIV and SIV Envelope Glycoproteins Interact with Glycolipids and Lipids.International journal of molecular sciences · 2023
    Article
  19. Review
  20. Article

30 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Mary E MillerDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, USA.
Shramika Adhikary
Andrey A Kolokoltsov
Robert A Davey
The University of Texas Medical Branch at Galveston · US

Funding

WRCE Nonhuman Primate CoreU54AI057156 · NIAID · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI WALKER, DAVID H · 2003 to 2013
$102.6M
Receptor Trafficking in Entry of Murine Leukemia VirusesR01AI063513 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI DAVEY, ROBERT A · 2006 to 2011
$1.5M
NIAID NIH HHS 2 U54 AI057156-06NIAID NIH HHS 5R01AI063513-02NIAID NIH HHS R01 AI063513NIAID NIH HHS U54 AI057156
6 · The paper itself

Abstract

Acid sphingomyelinase (ASMase) converts the lipid sphingomyelin (SM) to phosphocholine and ceramide and has optimum activity at acidic pH. Normally, ASMase is located in lysosomes and endosomes, but membrane damage or the interaction with some bacterial and viral pathogens can trigger its recruitment to the plasma membrane. Rhinovirus and measles viruses each require ASMase activity during early stages of infection. Both sphingomyelin and ceramide are important components of lipid rafts and are potent signaling molecules. Each plays roles in mediating macropinocytosis, which has been shown to be important for ebolavirus (EBOV) infection. Here, we investigated the role of ASMase and its substrate, SM, in EBOV infection. The work was performed at biosafety level 4 with wild-type virus with specificity and mechanistic analysis performed using virus pseudotypes and virus-like particles. We found that virus particles strongly associate with the SM-rich regions of the cell membrane and depletion of SM reduces EBOV infection. ASM-specific drugs and multiple small interfering RNAs strongly inhibit the infection by EBOV and EBOV glycoprotein pseudotyped viruses but not by the pseudotypes bearing the glycoprotein of vesicular stomatitis virus. Interestingly, the binding of virus-like particles to cells is strongly associated with surface-localized ASMase as well as SM-enriched sites. Our work suggests that ASMase activity and SM presence are necessary for efficient infection of cells by EBOV. The inhibition of this pathway may provide new avenues for drug treatment.

Indexed as

AnimalsCell MembraneChlorocebus aethiopsEbolavirusHEK293 CellsHeLa CellsHeterocyclic Compounds, 4 or More RingsHumansLysosomesMembrane MicrodomainsMembrane ProteinsRNA InterferenceRNA, Small InterferingSphingomyelin PhosphodiesteraseSphingomyelinsVero CellsHeterocyclic Compounds, 4 or More RingsMembrane ProteinsRNA, Small InterferingSMPD1 protein, humanSphingomyelin PhosphodiesteraseSphingomyelinsvacuolin-1

Identifiers

PMID22573858
PMCPMC3416309
OpenAlexW2152354057

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.