Evidence map›Paper›PMID 28802158›Full record

ArticleVirology2017

Lipidation increases antiviral activities of coronavirus fusion-inhibiting peptides.

Jung-Eun Park, Tom Gallagher

Open access · bronzeAbstract read
In one paragraph

Article in Virology, 2017. 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
1.3field-weighted citation impact, top 21% 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, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Lipid and Lipidation in Membrane Fusion.The Journal of membrane biology · 2022
    Review
  10. Leveraging the therapeutic, biological, and self-assembling potential of peptides for the treatment of viral infections.Journal of controlled release : official journal of the Controlled Release Society · 2022
    Review
  11. Article
  12. Review
  13. Coronavirus Entry Inhibitors.Advances in experimental medicine and biology · 2022
    Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Evaluating MERS-CoV Entry Pathways.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  19. Article
  20. 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.

Jung-Eun ParkDepartment of Microbiology and Immunology, Loyola University Chicago, Maywood, IL 60153, USA.
Tom GallagherDepartment of Microbiology and Immunology, Loyola University Chicago, Maywood, IL 60153, USA. Electronic address: tgallag@luc.edu.
Loyola University Chicago · US

Funding

SARS-CoV Proteins in Heterologous Viral InfectionP01AI060699 · NIAID · UNIVERSITY OF IOWA · PI PERLMAN, STANLEY · 2004 to 2021
$21.5M
NIAID NIH HHS P01 AI060699
6 · The paper itself

Abstract

Coronaviruses (CoVs) can cause life-threatening respiratory diseases. Their infectious entry requires viral spike (S) proteins, which attach to cell receptors, undergo proteolytic cleavage, and then refold in a process that catalyzes virus-cell membrane fusion. Fusion-inhibiting peptides bind to S proteins, interfere with refolding, and prevent infection. Here we conjugated fusion-inhibiting peptides to various lipids, expecting this to secure peptides onto cell membranes and thereby increase antiviral potencies. Cholesterol or palmitate adducts increased antiviral potencies up to 1000-fold. Antiviral effects were evident after S proteolytic cleavage, implying that lipid conjugates affixed the peptides at sites of protease-triggered fusion activation. Unlike lipid-free peptides, the lipopeptides suppressed CoV S protein-directed virus entry taking place within endosomes. Cell imaging revealed intracellular peptide aggregates, consistent with their endocytosis into compartments where CoV entry takes place. These findings suggest that lipidations localize antiviral peptides to protease-rich sites of CoV fusion, thereby protecting cells from diverse CoVs.

Indexed as

AnimalsAntiviral AgentsChlorocebus aethiopsCoronavirusEndosomesLipopeptidesVero CellsVirus InternalizationAntiviral AgentsLipopeptidesAntiviral agentsCoronavirusFusion-inhibiting peptideLipopeptideProteolytic activationVirus-cell fusionVirus entry

Identifiers

PMID28802158
PMCPMC7112077
OpenAlexW2743954445

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.