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Peer-reviewedCC BYScience

Molecular mimicry of a pathogen virulence target by a plant immune receptor

  • Diana Gómez De La Cruz1,2,3
  • Thomas W. Ingram4,5,2
  • Rafał Zdrzałek6,5,2
  • Jodie Taylor1,2,3
  • Aleksandra Wawryk-Khamdavong1,2,7,3,8
  • Kinga Bachowska1
  • Mark James Banfield6
  • Nicholas J. Talbot1
  • Matthew Moscou9,4,1,10
10 affiliations
  1. 1The Sainsbury Laboratory, University of East Anglia, Norwich, UK
  2. 2Norwich, UK
  3. 3The Sainsbury Laboratory, University of East Anglia
  4. 4Department of Plant Pathology, University of Minnesota, St. Paul, MN, USA
  5. 5Department of Biochemistry and Metabolism, John Innes Centre
  6. 6Department of Biochemistry and Metabolism, John Innes Centre, Norwich, UK
  7. 7St. Paul, Minnesota, USA
  8. 8USDA-ARS Cereal Disease Laboratory, University of Minnesota
  9. 9Center for Precision Plant Genomics, University of Minnesota, St. Paul, MN, USA
  10. 10USDA-ARS Cereal Disease Laboratory, St. Paul, MN, USA
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Abstract

Plants and animals respond to pathogen attack by mounting innate immune responses that require intracellular nucleotide binding leucine-rich repeat (NLR) proteins. These immune receptors detect pathogen infection by sensing virulence effector proteins. However, the mechanisms by which receptors evolve new recognition specificities remain poorly understood. Here we report that a plant NLR has evolved the capacity to bind to a pathogen effector by acting as a molecular mimic of a virulence target of the effector, thereby triggering an immune response. The barley NLR Mildew Locus A 3 (MLA3) confers resistance to the blast fungus Magnaporthe oryzae by recognizing the effector Pwl2. Using structural analysis, we show that MLA3 has acquired the capacity to bind and respond to Pwl2 through molecular mimicry of the effector host target HIPP43. We demonstrate that the amino acids at the binding interface of MLA3 and Pwl2 are highly conserved in interface of HIPP43 with Pwl2, and are required to trigger an immune response. We used this discovery to bioengineer SR50—an MLA ortholog in rye that confers resistance to wheat stem rust—by introducing the Pwl2 binding interface of MLA3. This chimeric receptor has dual recognition activities, binding and responding to effectors from two major cereal pathogens. Collectively, these results provide evidence that plant immune receptors have evolved sophisticated mimicry strategies to counteract pathogen attack.

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Cite

BibTeXRIS
BibTeX
@article{cruz2026molecular,
  title = {{Molecular mimicry of a pathogen virulence target by a plant immune receptor}},
  author = {Diana Gómez De La Cruz and Thomas W. Ingram and Rafał Zdrzałek and Jodie Taylor and Aleksandra Wawryk-Khamdavong and Kinga Bachowska and Mark James Banfield and Nicholas J. Talbot and Matthew Moscou},
  journal = {Science},
  year = {2026},
  month = jun,
  doi = {10.1126/science.aef9946},
  url = {https://doi.org/10.1126/science.aef9946},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Molecular mimicry of a pathogen virulence target by a plant immune receptor
AU  - Diana Gómez De La Cruz
AU  - Thomas W. Ingram
AU  - Rafał Zdrzałek
AU  - Jodie Taylor
AU  - Aleksandra Wawryk-Khamdavong
AU  - Kinga Bachowska
AU  - Mark James Banfield
AU  - Nicholas J. Talbot
AU  - Matthew Moscou
PY  - 2026
DA  - 2026/06/04
JO  - Science
DO  - 10.1126/science.aef9946
UR  - https://doi.org/10.1126/science.aef9946
AB  - Plants and animals respond to pathogen attack by mounting innate immune responses that require intracellular nucleotide binding leucine-rich repeat (NLR) proteins. These immune receptors detect pathogen infection by sensing virulence effector proteins. However, the mechanisms by which receptors evolve new recognition specificities remain poorly understood. Here we report that a plant NLR has evolved the capacity to bind to a pathogen effector by acting as a molecular mimic of a virulence target of the effector, thereby triggering an immune response. The barley NLR Mildew Locus A 3 (MLA3) confers resistance to the blast fungus Magnaporthe oryzae by recognizing the effector Pwl2. Using structural analysis, we show that MLA3 has acquired the capacity to bind and respond to Pwl2 through molecular mimicry of the effector host target HIPP43. We demonstrate that the amino acids at the binding interface of MLA3 and Pwl2 are highly conserved in interface of HIPP43 with Pwl2, and are required to trigger an immune response. We used this discovery to bioengineer SR50—an MLA ortholog in rye that confers resistance to wheat stem rust—by introducing the Pwl2 binding interface of MLA3. This chimeric receptor has dual recognition activities, binding and responding to effectors from two major cereal pathogens. Collectively, these results provide evidence that plant immune receptors have evolved sophisticated mimicry strategies to counteract pathogen attack.
SN  - 0036-8075
SN  - 0193-4511
SN  - 1095-9203
ER  -