ArticlePLoS pathogens2012
The ebola virus interferon antagonist VP24 directly binds STAT1 and has a novel, pyramidal fold.
Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 83 papers.
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.
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.
Who cites it
83 citing papers in PubMed, 148 citations in OpenAlex.
- A short history of Auto-Rickshaw.Acta crystallographica. Section D, Structural biology · 2026Review
- Review
- Article
- Article
- Jamaican fruit bats' competence for Ebola but not Marburg virus is driven by intrinsic differences.Nature communications · 2025Article
- Structural basis for Ebola virus nucleocapsid assembly and function regulated by VP24.Nature communications · 2025Article
- Review
- Intracellular Ebola virus nucleocapsid assembly revealed by in situ cryo-electron tomography.Cell · 2024Article
- Molecular determinants of cross-species transmission in emerging viral infections.Microbiology and molecular biology reviews : MMBR · 2024Review
- The Role of Ebola Virus VP24 Nuclear Trafficking Signals in Infectious Particle Production.bioRxiv : the preprint server for biology · 2024Article
- Review
- Natural killer cells and their exosomes in viral infections and related therapeutic approaches: where are we?Cell communication and signaling : CCS · 2023Review
- Article
- Molecular mechanisms and cellular functions of liquid-liquid phase separation during antiviral immune responses.Frontiers in immunology · 2023Review
- Immune correlates of protection for SARS-CoV-2, Ebola and Nipah virus infection.Frontiers in immunology · 2023Review
- African swine fever virus pA104R protein acts as a suppressor of type I interferon signaling.Frontiers in microbiology · 2023Article
- African Swine Fever Virus pI215L Inhibits Type I Interferon Signaling by Targeting Interferon Regulatory Factor 9 for Autophagic Degradation.Journal of virology · 2022Article
- Identification of promising anti-EBOV inhibitors:Royal Society open science · 2022Article
- TRIM25 and ZAP target the Ebola virus ribonucleoprotein complex to mediate interferon-induced restriction.PLoS pathogens · 2022Article
- Article
23 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Ebolaviruses cause hemorrhagic fever with up to 90% lethality and in fatal cases, are characterized by early suppression of the host innate immune system. One of the proteins likely responsible for this effect is VP24. VP24 is known to antagonize interferon signaling by binding host karyopherin α proteins, thereby preventing them from transporting the tyrosine-phosphorylated transcription factor STAT1 to the nucleus. Here, we report that VP24 binds STAT1 directly, suggesting that VP24 can suppress at least two distinct branches of the interferon pathway. Here, we also report the first crystal structures of VP24, derived from different species of ebolavirus that are pathogenic (Sudan) and nonpathogenic to humans (Reston). These structures reveal that VP24 has a novel, pyramidal fold. A site on a particular face of the pyramid exhibits reduced solvent exchange when in complex with STAT1. This site is above two highly conserved pockets in VP24 that contain key residues previously implicated in virulence. These crystal structures and accompanying biochemical analysis map differences between pathogenic and nonpathogenic viruses, offer templates for drug design, and provide the three-dimensional framework necessary for biological dissection of the many functions of VP24 in the virus life cycle.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.