Citation

BibTex format

@article{Madhuprakash:2024:10.1126/sciadv.adr2594,
author = {Madhuprakash, J and Toghani, A and Contreras, MP and Posbeyikian, A and Richardson, J and Kourelis, J and Bozkurt, TO and Webster, MW and Kamoun, S},
doi = {10.1126/sciadv.adr2594},
journal = {Science Advances},
title = {A disease resistance protein triggers oligomerization of its NLR helper into a hexameric resistosome to mediate innate immunity},
url = {http://dx.doi.org/10.1126/sciadv.adr2594},
volume = {10},
year = {2024}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - NRCs are essential helper NLR (nucleotide-binding domain and leucine-rich repeat) proteins that execute immune responses triggered by sensor NLRs. The resting state of NbNRC2 was recently shown to be a homodimer, but the sensor-activated state remains unclear. Using cryo-EM, we determined the structure of sensor-activated NbNRC2, which forms a hexameric inflammasome-like resistosome. Mutagenesis of the oligomerization interface abolished immune signaling, confirming the functional significance of the NbNRC2 resistosome. Comparative structural analyses between the resting state homodimer and sensor-activated homohexamer revealed substantial rearrangements, providing insights into NLR activation mechanisms. Furthermore, structural comparisons between NbNRC2 hexamer and previously reported CC-NLR pentameric assemblies revealed features allowing an additional protomer integration. Using the NbNRC2 hexamer structure, we assessed the recently released AlphaFold 3 for predicting activated CC-NLR oligomers, revealing high-confidence modeling of NbNRC2 and other CC-NLR amino-terminal α1 helices, a region proven difficult to resolve structurally. Overall, our work sheds light on NLR activation mechanisms and expands understanding of NLR structural diversity.
AU - Madhuprakash,J
AU - Toghani,A
AU - Contreras,MP
AU - Posbeyikian,A
AU - Richardson,J
AU - Kourelis,J
AU - Bozkurt,TO
AU - Webster,MW
AU - Kamoun,S
DO - 10.1126/sciadv.adr2594
PY - 2024///
SN - 2375-2548
TI - A disease resistance protein triggers oligomerization of its NLR helper into a hexameric resistosome to mediate innate immunity
T2 - Science Advances
UR - http://dx.doi.org/10.1126/sciadv.adr2594
UR - http://hdl.handle.net/10044/1/115682
VL - 10
ER -

General enquiries


 For any enquiries about the Fungal Science Network at Imperial, please contact:

fungalnetwork@imperial.ac.uk