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Signal Transduction by a Fungal NOD-Like Receptor Based on Propagation of a Prion Amyloid Fold
| dc.contributor.author | DASKALOV, Asen | |
| dc.contributor.author | HABENSTEIN, Birgit | |
| dc.contributor.author | MARTINEZ, Denis | |
| dc.contributor.author | DEBETS, Alfons J. M. | |
| dc.contributor.author | SABATE, Raimon | |
| dc.contributor.author | LOQUET, Antoine | |
| dc.contributor.author | SAUPE, Sven J. | |
| dc.date.accessioned | 2020-09-03T08:02:14Z | |
| dc.date.available | 2020-09-03T08:02:14Z | |
| dc.date.issued | 2015 | |
| dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/10995 | |
| dc.description.abstractEn | In the fungus Podospora anserina, the [Het-s] prion induces programmed cell death by activating the HET-S pore-forming protein. The HET-s beta-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 beta-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 beta-solenoid fold. Here, we analyze the ability of NWD2 to induce formation of the beta-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 beta-solenoid fold abolish templating activity. In vitro, the N-terminal motif assembles into infectious prion amyloids that display a structure resembling the beta-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 beta-solenoid fold in fungal NLR function further highlights the general importance of amyloid and prion-like signaling in immunity-related cell fate pathways. | |
| dc.language.iso | en | |
| dc.title.en | Signal Transduction by a Fungal NOD-Like Receptor Based on Propagation of a Prion Amyloid Fold | |
| dc.type | Article de revue | |
| dc.identifier.doi | 10.1371/journal.pbio.1002059 | |
| dc.subject.hal | Chimie/Matériaux | |
| bordeaux.journal | PLoS biology | |
| bordeaux.page | e1002059-e1002059 | |
| bordeaux.volume | 13 | |
| bordeaux.hal.laboratories | Institut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248 | * |
| bordeaux.hal.laboratories | Institut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248) | |
| bordeaux.issue | 2 | |
| bordeaux.institution | Université de Bordeaux | |
| bordeaux.institution | Bordeaux INP | |
| bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=PLoS%20biology&rft.date=2015&rft.volume=13&rft.issue=2&rft.spage=e1002059-e1002059&rft.epage=e1002059-e1002059&rft.au=DASKALOV,%20Asen&HABENSTEIN,%20Birgit&MARTINEZ,%20Denis&DEBETS,%20Alfons%20J.%20M.&SABATE,%20Raimon&rft.genre=article |
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