ArticleNature communications2025
A protein-proximity screen reveals Ebola virus co-opts the mRNA decapping complex through the scaffold protein EDC4.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Self-adjuvanting Ebola virus-like particles that incorporate a cellular interferon-inducing domain.Research square · 2026Article
- Ebola virus disease: A persistent challenge in global health security.Open veterinary journal · 2026Review
- 25 Years of Ebola Virus VP35 Research.Journal of molecular biology · 2025Review
- Ebola virus VP35 NNLNS motif modulates viral RNA synthesis and MIB2-mediated signaling.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
- Update of
Authors and funding
13 authors.
Funding
Abstract
The interaction of host and Ebola virus (EBOV) proteins is required for establishing infection. In this study, we use proximity-dependent biotinylation to identify cellular proteins that bind to EBOV proteins encoded by six of the seven viral genes. Hits are computationally mapped onto a human protein-protein interactome and annotated with viral proteins, confirming known EBOV-host protein interactions and revealing previously undescribed interactions and processes. This approach efficiently arranges proteins into functional complexes associated with single viral proteins. Focused characterization of interactions between EBOV VP35 and the mRNA decapping complex shows that VP35 binds the scaffold protein EDC4 through the C-terminal subdomain, with both proteins colocalizing in EBOV-infected cells. siRNA depletion of EDC4, DCP2, and EDC3 reduces virus replication by inhibiting early viral RNA synthesis. Overall, the analytical approach efficiently identifies EBOV protein interactions with cellular protein complexes, providing a deeper understanding of replication mechanisms for therapeutic intervention.
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.