ArticleVeterinary research2025
ASFV pS183L protein negatively regulates RLR-mediated antiviral signalling by blocking MDA5 oligomerisation.
Article in Veterinary research, 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.
- Transcriptomic and Metabolomic Profiling Identifies a Core Gene-Metabolite Axis Driving African Swine Fever Virus Replication in the Soft Tick Ornithodoros lahorensis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- African swine fever virus pE199L, as a mitophagy receptor, suppresses antiviral innate immunity to promote viral replication.Autophagy · 2026Article
- African swine fever virus pC147L inhibits retinoic acid-inducible gene I-like receptors pathway via targeting MAVS-TRAF6 complex.Veterinary research · 2026Article
- Host-pathogen interactions in African swine fever: From viral entry to systemic disease progression.Cell insight · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors.
Funding
Abstract
The retinoic acid-inducible gene I (RIG-I)-like receptors (RLRs) are major sensors against viral infection, but their roles in DNA virus infection largely remain unknown. This study found that a previously uncharacterised protein, pS183L, negatively regulates RLR signalling by suppressing MDA5 oligomerisation. Specifically, we showed that the overexpression of pS183L suppresses MDA5 but not cGAS-STING or RIG-I-induced IFN-β activation. Consistently, pS183L inhibited high molecular weight poly (I:C) activated IFN-β production. Furthermore, we demonstrated that pS183L interacts with CARDs and the MDA5 Helicase domain, consequently blocking MDA5 oligomerisation and the MDA5-MAVS interaction. Taken together, we concluded that pS183L blocks MDA5 oligomerisation through protein-protein interaction and thus disrupts MDA5-mediated IFN-β signalling.
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.