Evidence map›Paper›PMID 36007601›Full record

ArticleAntiviral research2022

Ligand-based design of peptide entry inhibitors targeting the endosomal receptor binding site of filoviruses.

Leah Liu Wang, Leslie Estrada, Joshua Wiggins, Manu Anantpadma, J J Patten, Robert A Davey, Shi-Hua Xiang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Antiviral research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

7 authors at 2 institutions in 1 country.

Leah Liu WangSchool of Veterinary Medicine and Biomedical Sciences, USA; Nebraska Center for Virology, University of Nebraska-Lincoln, Lincoln, NE, 68583, USA.
Leslie EstradaSchool of Veterinary Medicine and Biomedical Sciences, USA; Nebraska Center for Virology, University of Nebraska-Lincoln, Lincoln, NE, 68583, USA.
Joshua WigginsNebraska Center for Virology, University of Nebraska-Lincoln, Lincoln, NE, 68583, USA; School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE, 68583, USA.
Manu AnantpadmaDepartment of Microbiology & National Emerging Infectious Diseases Laboratories, Boston University School of Medicine, Boston, MA, 02115, USA.
J J PattenDepartment of Microbiology & National Emerging Infectious Diseases Laboratories, Boston University School of Medicine, Boston, MA, 02115, USA.
Robert A DaveyDepartment of Microbiology & National Emerging Infectious Diseases Laboratories, Boston University School of Medicine, Boston, MA, 02115, USA.
Shi-Hua XiangSchool of Veterinary Medicine and Biomedical Sciences, USA; Nebraska Center for Virology, University of Nebraska-Lincoln, Lincoln, NE, 68583, USA. Electronic address: sxiang2@unl.edu.
University of Nebraska–Lincoln · USBoston University · US

Funding

Antiviral Lead Identification to Treat Filovirus InfectionsR01AI128364 · NIAID · PURDUE UNIVERSITY · PI DAVEY, ROBERT A, DAVISSON, VINCENT JO · 2019 to 2022
$2.6M
Structure-Based Design of Peptide Entry Inhibitors against Ebola Virus InfectionR21AI151483 · NIAID · UNIVERSITY OF NEBRASKA LINCOLN · PI XIANG, SHI-HUA · 2021 to 2022
$468k
NIAID NIH HHS R01 AI128364NIAID NIH HHS R21 AI151483
6 · The paper itself

Abstract

Filoviruses enter cells through macropinocytosis and trafficking into the endosomes in which they bind to the receptor Niemann-Pick C1 protein (NPC1) for membrane fusion and entry into the cytoplasm. The endosomal receptor-binding is critical step for filovirus entry. Designing inhibitors to block receptor binding will prevent viral entry. Using available binding structural information from the co-crystal structures of the viral GP with the receptor NPC1 or with monoclonal antibodies, we have conducted structure-based design of peptide inhibitors to target the receptor binding site (RBS). The designed peptides were tested for their inhibition activity against pseudo-typed or replication-competent viruses in a cell-based assay. The results indicate that these peptides exhibited strong activities against both Ebola and Marburg virus infection. It is expected that these peptides can be further developed for therapeutic use to treat filovirus infection and combat the outbreaks.

Indexed as

FiloviridaeReceptors, VirusViral Fusion Protein InhibitorsBinding SitesCarrier ProteinsCell LineEbolavirusEndosomesHemorrhagic Fever, EbolaHumansIntracellular Signaling Peptides and ProteinsLigandsMembrane GlycoproteinsNiemann-Pick C1 ProteinVirus InternalizationCarrier ProteinsIntracellular Signaling Peptides and ProteinsLigandsMembrane GlycoproteinsNiemann-Pick C1 ProteinReceptors, VirusViral Fusion Protein InhibitorsEbola virus (EBOV)FilovirusMarburg virus (MARV)Niemann-pick C1 receptor binding site (RBS)Peptide entry inhibitorStructure based design

Identifiers

PMID36007601
PMCPMC13622972
OpenAlexW4292622684

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.