ArticleNature communications2026
A phage-encoded sponge protein suppresses bacterial TIR-Caspase immune signaling.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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.
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Who cites it
1 citing paper in PubMed.
- Phage RyR-domain proteins degrade ADPR-based immune signals and fuel NADbioRxiv : the preprint server for biology · 2026Article
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Authors and funding
14 authors.
Funding
Abstract
Triggering immune response through generation of signal molecules is a common immune strategy across all domains of life. In the bacterial type IV Thoeris anti-phage system, a Toll/interleukin-1 receptor (TIR)-domain protein produces adenosine 5'-diphosphate-cyclo[N7:1"]-ribose (N7-cADPR) as the immune signal to activate a Caspase-like effector. Here, we identified an inhibitor of type IV Thoeris through a phage mating assay that allows a sensitive phage to acquire anti-defense genes from related resistant phages. The inhibitor (hereafter TadIV-1) functions as a sponge that sequesters the N7-cADPR signal to inhibit Caspase activation. Structural analyses of TadIV-1 indicate a distinctive signal binding mechanism, wherein the binding pocket comprises its N-terminal flexible loop. In addition, phages lacking TadIV-1 can escape type IV Thoeris sensing through mutation in the capsid vertex protein. Collectively, this work expands the phage anti-defense arsenal with a unique immune signal sequestration mechanism and provides insights into phage invasion recognition mechanism of type IV Thoeris.
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