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The synthetic NLR RGA5HMA5 requires multiple interfaces within and outside the integrated domain for effector recognition

Author

Listed:
  • Xin Zhang

    (China Agricultural University
    China Agricultural University)

  • Yang Liu

    (China Agricultural University
    China Agricultural University)

  • Guixin Yuan

    (China Agricultural University
    China Agricultural University)

  • Shiwei Wang

    (China Agricultural University
    China Agricultural University)

  • Dongli Wang

    (China Agricultural University
    China Agricultural University)

  • Tongtong Zhu

    (China Agricultural University
    China Agricultural University)

  • Xuefeng Wu

    (China Agricultural University
    China Agricultural University)

  • Mengqi Ma

    (China Agricultural University
    China Agricultural University)

  • Liwei Guo

    (China Agricultural University
    Yunnan Agricultural University)

  • Hailong Guo

    (China Agricultural University)

  • Vijai Bhadauria

    (China Agricultural University)

  • Junfeng Liu

    (China Agricultural University
    China Agricultural University)

  • You-Liang Peng

    (China Agricultural University
    China Agricultural University)

Abstract

Some plant sensor nucleotide-binding leucine-rich repeat (NLR) receptors detect pathogen effectors through their integrated domains (IDs). Rice RGA5 sensor NLR recognizes its corresponding effectors AVR-Pia and AVR1-CO39 from the blast fungus Magnaporthe oryzae through direct binding to its heavy metal-associated (HMA) ID to trigger the RGA4 helper NLR-dependent resistance in rice. Here, we report a mutant of RGA5 named RGA5HMA5 that confers complete resistance in transgenic rice plants to the M. oryzae strains expressing the noncorresponding effector AVR-PikD. RGA5HMA5 carries three engineered interfaces, two of which lie in the HMA ID and the other in the C-terminal Lys-rich stretch tailing the ID. However, RGA5 variants having one or two of the three interfaces, including replacing all the Lys residues with Glu residues in the Lys-rich stretch, failed to activate RGA4-dependent cell death of rice protoplasts. Altogether, this work demonstrates that sensor NLRs require a concerted action of multiple surfaces within and outside the IDs to both recognize effectors and activate helper NLR-mediated resistance, and has implications in structure-guided designing of sensor NLRs.

Suggested Citation

  • Xin Zhang & Yang Liu & Guixin Yuan & Shiwei Wang & Dongli Wang & Tongtong Zhu & Xuefeng Wu & Mengqi Ma & Liwei Guo & Hailong Guo & Vijai Bhadauria & Junfeng Liu & You-Liang Peng, 2024. "The synthetic NLR RGA5HMA5 requires multiple interfaces within and outside the integrated domain for effector recognition," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-45380-2
    DOI: 10.1038/s41467-024-45380-2
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    References listed on IDEAS

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    1. Karine de Guillen & Diana Ortiz-Vallejo & Jérome Gracy & Elisabeth Fournier & Thomas Kroj & André Padilla, 2015. "Structure Analysis Uncovers a Highly Diverse but Structurally Conserved Effector Family in Phytopathogenic Fungi," PLOS Pathogens, Public Library of Science, vol. 11(10), pages 1-27, October.
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