ArticlePLoS biology2015
Signal transduction by a fungal NOD-like receptor based on propagation of a prion amyloid fold.
Article in PLoS biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 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
41 citing papers in PubMed, 90 citations in OpenAlex.
- NOD-Like Receptor Genes Undergo Diversity-Enhancing Evolution in a Fungal Species Complex.Genome biology and evolution · 2026Article
- Regulated cell death in fungi from a comparative immunology perspective.Cell death and differentiation · 2026Review
- Characterization of an amyloid-based antiphage defence system in Escherichia coli.Nature microbiology · 2025Article
- Reconstructing NOD-like receptor alleles with high internal conservation inMicrobial genomics · 2025Article
- Identification of metabolism related biomarkers in obesity based on adipose bioinformatics and machine learning.Journal of translational medicine · 2024Article
- What are the 100 most cited fungal genera?Studies in mycology · 2024Article
- het-B allorecognition in Podospora anserina is determined by pseudo-allelic interaction of genes encoding a HET and lectin fold domain protein and a PII-like protein.PLoS genetics · 2024Article
- A Story Between s and S: [Het-s] Prion of the FungusMycobiology · 2024Review
- Emergence of the fungal immune system.iScience · 2023Review
- Exploring a diverse world of effector domains and amyloid signaling motifs in fungal NLR proteins.PLoS computational biology · 2022Article
- The host exocyst complex is targeted by a conserved bacterial type-III effector that promotes virulence.The Plant cell · 2022Article
- Innate immunity in fungi: Is regulated cell death involved?PLoS pathogens · 2022Article
- Fungal gasdermin-like proteins are controlled by proteolytic cleavage.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The expanding scope of amyloid signalling.Prion · 2021Article
- The Hunt for Ancient Prions: Archaeal Prion-Like Domains Form Amyloid-Based Epigenetic Elements.Molecular biology and evolution · 2021Article
- Searching for universal model of amyloid signaling motifs using probabilistic context-free grammars.BMC bioinformatics · 2021Article
- Article
- Structural and molecular basis of cross-seeding barriers in amyloids.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective.Frontiers in molecular neuroscience · 2021Review
- Structural Insights into the Plant Immune Receptors PRRs and NLRs.Plant physiology · 2020Review
Corrections and comments
- Commented on by
Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the fungus Podospora anserina, the [Het-s] prion induces programmed cell death by activating the HET-S pore-forming protein. The HET-s β-solenoid prion fold serves as a template for converting the HET-S prion-forming domain into the same fold. This conversion, in turn, activates the HET-S pore-forming domain. The gene immediately adjacent to het-S encodes NWD2, a Nod-like receptor (NLR) with an N-terminal motif similar to the elementary repeat unit of the β-solenoid fold. NLRs are immune receptors controlling cell death and host defense processes in animals, plants and fungi. We have proposed that, analogously to [Het-s], NWD2 can activate the HET-S pore-forming protein by converting its prion-forming region into the β-solenoid fold. Here, we analyze the ability of NWD2 to induce formation of the β-solenoid prion fold. We show that artificial NWD2 variants induce formation of the [Het-s] prion, specifically in presence of their cognate ligands. The N-terminal motif is responsible for this prion induction, and mutations predicted to affect the β-solenoid fold abolish templating activity. In vitro, the N-terminal motif assembles into infectious prion amyloids that display a structure resembling the β-solenoid fold. In vivo, the assembled form of the NWD2 N-terminal region activates the HET-S pore-forming protein. This study documenting the role of the β-solenoid fold in fungal NLR function further highlights the general importance of amyloid and prion-like signaling in immunity-related cell fate pathways.
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.