Evidence map›Paper›PMID 27875299›Full record

ArticleThe Journal of biological chemistry2016

Lipids Cooperate with the Reovirus Membrane Penetration Peptide to Facilitate Particle Uncoating.

Anthony J Snyder, Pranav Danthi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.7field-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

20 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Cell Killing by Reovirus: Mechanisms and Consequences.Current topics in microbiology and immunology · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Large nanodiscs going viral.Current opinion in structural biology · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. The Orchestra of Reovirus Cell Entry.Current clinical microbiology reports · 2017
    Article
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

2 authors at 1 institution in 1 country.

Anthony J SnyderFrom the Department of Biology, Indiana University, Bloomington, Indiana 47405.
Pranav DanthiFrom the Department of Biology, Indiana University, Bloomington, Indiana 47405 pdanthi@indiana.edu.
Indiana University Bloomington · US

Funding

Regulating the Detection of Reovirus InfectionR01AI110637 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI Pranav Danthi · 2014 to 2026
$4.5M
NIAID NIH HHS R01 AI110637
6 · The paper itself

Abstract

Virus-host interactions play a role in many stages of the viral lifecycle, including entry. Reovirus, a model system for studying the entry mechanisms of nonenveloped viruses, undergoes a series of regulated structural transitions that culminate in delivery of the viral genetic material. Lipids can trigger one of these conformational changes, infectious subviral particle (ISVP)-to-ISVP* conversion. ISVP* formation releases two virally encoded peptides, myristoylated μ1N (myr-μ1N) and Φ. Among these, myr-μ1N is sufficient to form pores within membranes. Released myr-μ1N can also promote ISVP* formation in trans Using thermal inactivation as a readout for ISVP-to-ISVP* conversion, we demonstrate that lipids render ISVPs less thermostable in a virus concentration-dependent manner. Under conditions in which neither lipids alone nor myr-μ1N alone promotes ISVP-to-ISVP* conversion, myr-μ1N induces particle uncoating when lipids are present. These data suggest that the pore-forming activity and the ISVP*-promoting activity of myr-μ1N are linked. Lipid-associated myr-μ1N interacts with ISVPs and triggers efficient ISVP* formation. The cooperativity between a reovirus component and lipids reveals a distinct virus-host interaction in which membranes can facilitate nonenveloped virus entry.

Indexed as

Amino Acid SequenceAnimalsCapsid ProteinsCell MembraneCell Membrane PermeabilityCell-Penetrating PeptidesCells, CulturedLiposomesMembrane LipidsMiceModels, BiologicalMyristic AcidsProtein ConformationProtein Processing, Post-TranslationalReoviridaeReoviridae InfectionsCapsid ProteinsCell-Penetrating PeptidesLiposomesMembrane LipidsMyristic Acidsconformational changekineticsmembranephospholipid vesiclereovirusvirus entry

Identifiers

PMID27875299
PMCPMC5207185
OpenAlexW2551044271

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.