Evidence map›Paper›PMID 21454542›Full record

ArticleThe Journal of biological chemistry2011

Inhibition of Ebola virus entry by a C-peptide targeted to endosomes.

Emily Happy Miller, Joseph S Harrison, Sheli R Radoshitzky, Chelsea D Higgins, Xiaoli Chi, Lian Dong, Jens H Kuhn, Sina Bavari, Jonathan R Lai, Kartik Chandran

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. A Review: The Antiviral Activity of Cyclic Peptides.International journal of peptide research and therapeutics · 2023
    Review
  7. Article
  8. 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
  9. Ebola Virus Entry Inhibitors.Advances in experimental medicine and biology · 2022
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

10 authors at 3 institutions in 1 country.

Emily Happy MillerDepartment of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Joseph S Harrison
Sheli R Radoshitzky
Chelsea D Higgins
Xiaoli Chi
Lian Dong
Jens H Kuhn
Sina Bavari
Jonathan R Lai
Kartik Chandran
Albert Einstein College of Medicine · USUnited States Army Medical Research Institute of Infectious Diseases · USTunnell Consulting

Funding

MOLECULAR BIOPHYSICS TRAINING GRANTT32GM008572 · NIGMS · YESHIVA UNIVERSITY · PI BRENOWITZ, MICHAEL D. · 1995 to 2009
$3.0M
Mechanisms of Ebolavirus and Marburgvirus Entry into CellsR01AI088027 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI CHANDRAN, KARTIK · 2010 to 2014
$2.0M
Targeting Viral Envelope Glycoproteins with Synthetic AntibodiesR01AI090249 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI LAI, JONATHAN R. · 2010 to 2014
$2.0M
NIAID NIH HHS R01 AI088027NIAID NIH HHS R01 AI090249NIGMS NIH HHS T32 GM008572NIGMS NIH HHS T32-GM008572
6 · The paper itself

Abstract

Ebola virus (EboV) and Marburg virus (MarV) (filoviruses) are the causative agents of severe hemorrhagic fever. Infection begins with uptake of particles into cellular endosomes, where the viral envelope glycoprotein (GP) catalyzes fusion between the viral and host cell membranes. This fusion event is thought to involve conformational rearrangements of the transmembrane subunit (GP2) of the envelope spike that ultimately result in formation of a six-helix bundle by the N- and C-terminal heptad repeat (NHR and CHR, respectively) regions of GP2. Infection by other viruses employing similar viral entry mechanisms (such as HIV-1 and severe acute respiratory syndrome coronavirus) can be inhibited with synthetic peptides corresponding to the native CHR sequence ("C-peptides"). However, previously reported EboV C-peptides have shown weak or insignificant antiviral activity. To determine whether the activity of a C-peptide could be improved by increasing its intracellular concentration, we prepared an EboV C-peptide conjugated to the arginine-rich sequence from HIV-1 Tat, which is known to accumulate in endosomes. We found that this peptide specifically inhibited viral entry mediated by filovirus GP proteins and infection by authentic filoviruses. We determined that antiviral activity was dependent on both the Tat sequence and the native EboV CHR sequence. Mechanistic studies suggested that the peptide acts by blocking a membrane fusion intermediate.

Indexed as

AnimalsAntiviral AgentsChlorocebus aethiopsEbolavirusEndosomesHIV-1HumansPeptidestat Gene Products, Human Immunodeficiency VirusVero CellsVirus InternalizationAntiviral AgentsPeptidestat Gene Products, Human Immunodeficiency Virus

Identifiers

PMID21454542
PMCPMC3091195
OpenAlexW2043332877

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.