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Peer-reviewedCC BYScience Advances

A potato late blight pathogen effector interacts with ENTH-domain protein TOL9a and an activated helper NLR to suppress immunity

  • Jogi Madhuprakash1,2
  • AmirAli Toghani2
  • Hsuan Pai2
  • Madia Harvey2
  • Adam R. Bentham3
  • Benjamin A. Seager2
  • Enoch Lok Him Yuen4
  • Juan Carlos De la Concepción2
  • David M. Lawson3
  • Clare E. M. Stevenson3
  • Angel Vergara Cruces2
  • Lida Derevnina2
4 more authors
  • Tolga O. Bozkurt4
  • Mark James Banfield3
  • Sophien Kamoun2
  • Mauricio P. Contreras2
4 affiliations
  1. 1Department of Plant Sciences, School of Life Sciences, University of Hyderabad, Gachibowli, Hyderabad, India
  2. 2The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK
  3. 3Department of Biochemistry and Metabolism, John Innes Centre, Norwich Research Park, Norwich, UK
  4. 4Department of Life Sciences, Imperial College, London, UK
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Abstract

Pathogens counteract central nodes of NLR immune receptor networks to suppress immunity. However, the mechanisms by which pathogens hijack helper NLR pathways are poorly understood. Here, we show that an effector from the potato late blight pathogen Phytophthora infestans bridges the host protein NbTOL9a, a putative member of the host ESCRT pathway, to a helper NLR to suppress immunity. In this work, we solved the crystal structure of the RXLR-LWY effector AVRcap1b in complex with the ENTH domain of NbTOL9a. The structure revealed that unlike other RXLR-LWY effectors, AVRcap1b has a novel L-shaped fold that defines a new structural family of effectors in the Phytophthora genus. Moreover, we defined the AVRcap1b/NbTOL9a binding interface and designed effector mutants that don’t bind NbTOL9a, impairing immune suppression. This indicates that ENTH binding is required for full virulence activity of this effector. Lastly, we show that AVRcap1b associates specifically with activated NbNRC2 independently of NbTOL9a binding. This suggests that the effector functions as a bridge that interconnects NbNRC2 with the NbTOL9a pathway. These results illustrate an unprecedented pathogen mechanism to hijack helper NLR pathways and suppress immunity.

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Cite

BibTeXRIS
BibTeX
@article{madhuprakash2026potato,
  title = {{A potato late blight pathogen effector interacts with ENTH-domain protein TOL9a and an activated helper NLR to suppress immunity}},
  author = {Jogi Madhuprakash and AmirAli Toghani and Hsuan Pai and Madia Harvey and Adam R. Bentham and Benjamin A. Seager and Enoch Lok Him Yuen and Juan Carlos De la Concepción and David M. Lawson and Clare E. M. Stevenson and Angel Vergara Cruces and Lida Derevnina and Tolga O. Bozkurt and Mark James Banfield and Sophien Kamoun and Mauricio P. Contreras},
  journal = {Science Advances},
  year = {2026},
  month = jun,
  doi = {10.1126/sciadv.aea4500},
  url = {https://doi.org/10.1126/sciadv.aea4500},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - A potato late blight pathogen effector interacts with ENTH-domain protein TOL9a and an activated helper NLR to suppress immunity
AU  - Jogi Madhuprakash
AU  - AmirAli Toghani
AU  - Hsuan Pai
AU  - Madia Harvey
AU  - Adam R. Bentham
AU  - Benjamin A. Seager
AU  - Enoch Lok Him Yuen
AU  - Juan Carlos De la Concepción
AU  - David M. Lawson
AU  - Clare E. M. Stevenson
AU  - Angel Vergara Cruces
AU  - Lida Derevnina
AU  - Tolga O. Bozkurt
AU  - Mark James Banfield
AU  - Sophien Kamoun
AU  - Mauricio P. Contreras
PY  - 2026
DA  - 2026/06/05
JO  - Science Advances
DO  - 10.1126/sciadv.aea4500
UR  - https://doi.org/10.1126/sciadv.aea4500
AB  - Pathogens counteract central nodes of NLR immune receptor networks to suppress immunity. However, the mechanisms by which pathogens hijack helper NLR pathways are poorly understood. Here, we show that an effector from the potato late blight pathogen Phytophthora infestans bridges the host protein NbTOL9a, a putative member of the host ESCRT pathway, to a helper NLR to suppress immunity. In this work, we solved the crystal structure of the RXLR-LWY effector AVRcap1b in complex with the ENTH domain of NbTOL9a. The structure revealed that unlike other RXLR-LWY effectors, AVRcap1b has a novel L-shaped fold that defines a new structural family of effectors in the Phytophthora genus. Moreover, we defined the AVRcap1b/NbTOL9a binding interface and designed effector mutants that don’t bind NbTOL9a, impairing immune suppression. This indicates that ENTH binding is required for full virulence activity of this effector. Lastly, we show that AVRcap1b associates specifically with activated NbNRC2 independently of NbTOL9a binding. This suggests that the effector functions as a bridge that interconnects NbNRC2 with the NbTOL9a pathway. These results illustrate an unprecedented pathogen mechanism to hijack helper NLR pathways and suppress immunity.
SN  - 2375-2548
ER  -