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  • Review Article
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Plant pattern recognition receptors: from evolutionary insight to engineering

Nature Reviews Genetics volume 26, pages 268–278 (2025)Cite this article

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Abstract

The plant immune system relies on germline-encoded pattern recognition receptors (PRRs) that sense foreign and plant-derived molecular patterns, and signal health threats. Genomic and pangenomic data sets provide valuable insights into the evolution of PRRs and their molecular triggers, which is furthering our understanding of plant–pathogen co-evolution and convergent evolution. Moreover, in silico and in vivo methods of PRR identification have accelerated the characterization of receptor–ligand complexes, and advances in protein structure prediction algorithms are revealing novel PRR sensor functions. Harnessing these recent advances to engineer PRRs presents an opportunity to enhance plant disease resistance against a broad spectrum of pathogens, enabling more sustainable agricultural practices. This Review summarizes both established and innovative approaches to leverage genomic data and translate resulting evolutionary insights into engineering PRR recognition specificities.

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Fig. 1: The innate plant immune response.
Fig. 2: Synteny analysis of characterized LRR ligand–receptor pairs and their corresponding receptor locus within the family of the Fabaceae, Solanaceae and the order of the Brassicales.
Fig. 3: PRR–ligand co-evolution.
Fig. 4: Engineering PRR-based disease resistance.

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Data availability

Detailed methods and results of the synteny analysis depicted in Fig. 2 can be found within the Supplementary information.

References

  1. Food and Agriculture Organization of the United Nations. International year of plant health 2020. FAO https://www.fao.org/plant-health-2020/about/en (2020).

  2. Kourelis, J. et al. The helper NLR immune protein NRC3 mediates the hypersensitive cell death caused by the cell-surface receptor Cf-4. PLoS Genet. 18, e1010414 (2022).

    CAS  PubMed  PubMed Central  Google Scholar 

  3. Tian, H. et al. Activation of TIR signalling boosts pattern-triggered immunity. Nature 598, 500–503 (2021).

    CAS  PubMed  Google Scholar 

  4. Yuan, M. et al. Pattern-recognition receptors are required for NLR-mediated plant immunity. Nature 592, 105–109 (2021).

    CAS  PubMed  PubMed Central  Google Scholar 

  5. Ngou, B. P. M., Ahn, H. K., Ding, P. & Jones, J. D. G. Mutual potentiation of plant immunity by cell-surface and intracellular receptors. Nature 592, 110–115 (2021).

    CAS  PubMed  Google Scholar 

  6. Pruitt, R. N. et al. The EDS1–PAD4–ADR1 node mediates Arabidopsis pattern-triggered immunity. Nature 598, 495–499 (2021).

    CAS  PubMed  Google Scholar 

  7. Snoeck, S., Garcia, A. G. & Steinbrenner, A. D. Plant receptor-like proteins (RLPs): structural features enabling versatile immune recognition. Physiol. Mol. Plant Pathol. 125, 102004 (2023).

    CAS  Google Scholar 

  8. Pok, B., Ngou, M., Ding, P. & Jones, J. D. G. Thirty years of resistance: zig-zag through the plant immune system. Plant Cell 34, 1447–1478 (2022).

    Google Scholar 

  9. Boutrot, F. & Zipfel, C. Function, discovery, and exploitation of plant pattern recognition receptors for broad-spectrum disease resistance. Annu. Rev. Phytopathol. 55, 257–286 (2017).

    CAS  PubMed  Google Scholar 

  10. Felix, G., Duran, J. D., Volko, S. & Boller, T. Plants have a sensitive perception system for the most conserved domain of bacterial flagellin. Plant J. 18, 265–276 (1999).

    CAS  PubMed  Google Scholar 

  11. Kunze, G. et al. The N terminus of bacterial elongation factor Tu elicits innate immunity in Arabidopsis plants. Plant Cell 16, 3496–3507 (2004).

    CAS  PubMed  PubMed Central  Google Scholar 

  12. Toruño, T. Y., Stergiopoulos, I. & Coaker, G. Plant-pathogen effectors: cellular probes interfering with plant defenses in spatial and temporal manners. Annu. Rev. Phytopathol. 54, 419 (2016).

    PubMed  PubMed Central  Google Scholar 

  13. Buscaill, P. & van der Hoorn, R. A. L. Defeated by the nines: nine extracellular strategies to avoid microbe-associated molecular patterns recognition in plants. Plant Cell 33, 2116 (2021).

    PubMed  PubMed Central  Google Scholar 

  14. Snoeck, S., Guayazán-Palacios, N. & Steinbrenner, A. D. Molecular tug-of-war: plant immune recognition of herbivory. Plant Cell 34, 1497–1513 (2022).

    PubMed  PubMed Central  Google Scholar 

  15. Ngou, B. P. M., Heal, R., Wyler, M., Schmid, M. W. & Jones, J. D. G. Concerted expansion and contraction of immune receptor gene repertoires in plant genomes. Nat. Plants 8, 1146–1152 (2022). This study reports evidence for correlation between numbers of NLR-encoding and PRR-encoding genes across plant lineages and provides a comprehensive overview of PRR repertoires and evolution.

    CAS  PubMed  PubMed Central  Google Scholar 

  16. Liu, Q. et al. Curation, nomenclature, and topological classification of receptor-like kinases from 528 plant species for novel domain discovery and functional inference. Mol. Plant 17, 658–671 (2024).

    CAS  PubMed  Google Scholar 

  17. Yin, Z., Liu, J. & Dou, D. RLKdb: a comprehensively curated database of plant receptor-like kinase families. Mol. Plant 17, 513–515 (2024).

    CAS  PubMed  Google Scholar 

  18. Snoeck, S. et al. Leveraging coevolutionary insights and AI-based structural modeling to unravel receptor–peptide ligand-binding mechanisms. Proc. Natl Acad. Sci. USA 121, e2400862121 (2024). This publication was, to our knowledge, the first to use protein structure prediction to directly derive ligand–receptor interfaces.

    CAS  PubMed  PubMed Central  Google Scholar 

  19. Zhang, L. et al. Distinct immune sensor systems for fungal endopolygalacturonases in closely related Brassicaceae. Nat. Plants 7, 1254–1263 (2021).

    CAS  PubMed  Google Scholar 

  20. Yang, Y. et al. Convergent evolution of plant pattern recognition receptors sensing cysteine-rich patterns from three microbial kingdoms. Nat. Commun. 14, 1–12 (2023).

    Google Scholar 

  21. Torres Ascurra, Y. C. et al. Functional diversification of a wild potato immune receptor at its center of origin. Science 381, 891–897 (2023). This study reports the identification of the long elusive receptor for Pep-13 and Pep-25 and the evolutionary diversification of this receptor in potato.

    CAS  PubMed  Google Scholar 

  22. Chen, Z. et al. Convergent evolution of immune receptors underpins distinct elicitin recognition in closely related Solanaceous plants. Plant Cell 35, 1186–1201 (2023).

    PubMed  PubMed Central  Google Scholar 

  23. Helft, L. et al. LRR conservation mapping to predict functional sites within protein leucine-rich repeat domains. PLoS One 6, e21614 (2011).

    CAS  PubMed  PubMed Central  Google Scholar 

  24. Snoeck, S. et al. Evolutionary gain and loss of a plant pattern-recognition receptor for HAMP recognition. eLife 11, e81050 (2022).

    CAS  PubMed  PubMed Central  Google Scholar 

  25. Albert, I., Hua, C., Nürnberger, T., Pruitt, R. N. & Zhang, L. Surface sensor systems in plant immunity. Plant Physiol. 182, 1582–1596 (2020).

    CAS  PubMed  Google Scholar 

  26. Shi, Q., Febres, V. J., Jones, J. B. & Moore, G. A. A survey of FLS2 genes from multiple citrus species identifies candidates for enhancing disease resistance to Xanthomonas citri ssp. citri. Hortic. Res. 3, 16022 (2016).

    PubMed  PubMed Central  Google Scholar 

  27. Trdá, L. et al. The grapevine flagellin receptor VvFLS2 differentially recognizes flagellin-derived epitopes from the endophytic growth-promoting bacterium Burkholderia phytofirmans and plant pathogenic bacteria. N. Phytol. 201, 1371–1384 (2014).

    Google Scholar 

  28. Takai, R., Isogai, A., Takayama, S. & Che, F. S. Analysis of flagellin perception mediated by flg22 receptor OsFLS2 in rice. Mol. Plant Microbe Interact. 21, 1635–1642 (2008).

    CAS  PubMed  Google Scholar 

  29. Hann, D. R. & Rathjen, J. P. Early events in the pathogenicity of Pseudomonas syringae on Nicotiana benthamiana. Plant J. 49, 607–618 (2007).

    CAS  PubMed  Google Scholar 

  30. Robatzek, S. et al. Molecular identification and characterization of the tomato flagellin receptor LeFLS2, an orthologue of Arabidopsis FLS2 exhibiting characteristically different perception specificities. Plant Mol. Biol. 64, 539–547 (2007).

    CAS  PubMed  Google Scholar 

  31. Dunning, F. M., Sun, W., Jansen, K. L., Helft, L. & Bent, A. F. Identification and mutational analysis of Arabidopsis FLS2 leucine-rich repeat domain residues that contribute to flagellin perception. Plant Cell 19, 3297–3313 (2007).

    CAS  PubMed  PubMed Central  Google Scholar 

  32. Kim, W. et al. Perception of unrelated microbe-associated molecular patterns triggers conserved yet variable physiological and transcriptional changes in Brassica rapa ssp. pekinensis. Hortic. Res. 7, 186 (2020).

    CAS  PubMed  PubMed Central  Google Scholar 

  33. Boller, T. & Felix, G. A renaissance of elicitors: perception of microbe-associated molecular patterns and danger signals by pattern-recognition receptors. Annu. Rev. Plant Biol. 60, 379–407 (2009).

    CAS  PubMed  Google Scholar 

  34. Fritz-Laylin, L. K., Krishnamurthy, N., Tör, M., Sjölander, K. V. & Jones, J. D. G. Phylogenomic analysis of the receptor-like proteins of rice and Arabidopsis. Plant Physiol. 138, 611–623 (2005).

    CAS  PubMed  PubMed Central  Google Scholar 

  35. Tang, P. et al. Disease resistance signature of the leucine-rich repeat receptor-like kinase genes in four plant species. Plant Sci. 179, 399–406 (2010).

    CAS  Google Scholar 

  36. Jamieson, P. A., Shan, L. & He, P. Plant cell surface molecular cypher: receptor-like proteins and their roles in immunity and development. Plant Sci. 274, 242–251 (2018).

    CAS  PubMed  PubMed Central  Google Scholar 

  37. Ngou, B. P. M., Wyler, M., Schmid, M. W., Kadota, Y. & Shirasu, K. Evolutionary trajectory of pattern recognition receptors in plants. Nat. Commun. 15, 1–22 (2024).

    Google Scholar 

  38. Rhodes, J. et al. Perception of a conserved family of plant signalling peptides by the receptor kinase HSL3. eLife 11, e74687 (2022).

    CAS  PubMed  PubMed Central  Google Scholar 

  39. Krogh, A., Brown, M., Mian, I. S., Sjölander, K. & Haussler, D. Hidden Markov models in computational biology. Applications to protein modeling. J. Mol. Biol. 235, 1501–1531 (1994).

    CAS  PubMed  Google Scholar 

  40. Stringlis, I. A. & Pieterse, C. M. J. Evolutionary ‘hide and seek’ between bacterial flagellin and the plant immune system. Cell Host Microbe 29, 548–550 (2021).

    CAS  PubMed  Google Scholar 

  41. Brunner, F. et al. Pep‐13, a plant defense‐inducing pathogen‐associated pattern from Phytophthora transglutaminases. EMBO J. 21, 6681–6688 (2002).

    CAS  PubMed  PubMed Central  Google Scholar 

  42. Panchy, N., Lehti-Shiu, M. & Shiu, S. H. Evolution of gene duplication in plants. Plant Physiol. 171, 2294–2316 (2016).

    CAS  PubMed  PubMed Central  Google Scholar 

  43. Fliegmann, J. & Felix, G. Immunity: flagellin seen from all sides. Nat. Plants 2, 1–2 (2016).

    Google Scholar 

  44. Fürst, U. et al. Perception of Agrobacterium tumefaciens flagellin by FLS2XL confers resistance to crown gall disease. Nat. Plants 6, 22–27 (2020).

    PubMed  Google Scholar 

  45. Wei, Y. et al. An immune receptor complex evolved in soybean to perceive a polymorphic bacterial flagellin. Nat. Commun. 11, 3763 (2020).

    CAS  PubMed  PubMed Central  Google Scholar 

  46. Chen, Y. et al. GmFLS2 contributes to soybean resistance to Ralstonia solanacearum. N. Phytol. 240, 17–22 (2023).

    CAS  Google Scholar 

  47. Parys, K. et al. Signatures of antagonistic pleiotropy in a bacterial flagellin epitope. Cell Host Microbe 29, 620–634.e9 (2021).

    CAS  PubMed  Google Scholar 

  48. Colaianni, N. R. et al. A complex immune response to flagellin epitope variation in commensal communities. Cell Host Microbe 29, 635–649.e9 (2021).

    CAS  PubMed  Google Scholar 

  49. Meindl, T., Boller, T. & Felix, G. The bacterial elicitor flagellin activates its receptor in tomato cells according to the address–message concept. Plant Cell 12, 1783–1794 (2000).

    CAS  PubMed  PubMed Central  Google Scholar 

  50. Bauer, Z., Gómez-Gómez, L., Boller, T. & Felix, G. Sensitivity of different ecotypes and mutants of Arabidopsis thaliana toward the bacterial elicitor flagellin correlates with the presence of receptor-binding sites. J. Biol. Chem. 276, 45669–45676 (2001).

    CAS  PubMed  Google Scholar 

  51. Stevens, D. M. et al. Natural variation of immune epitopes reveals intrabacterial antagonism. Proc. Natl Acad. Sci. USA 121, e2319499121 (2024).

    CAS  PubMed  PubMed Central  Google Scholar 

  52. Hind, S. R. et al. Tomato receptor FLAGELLIN-SENSING 3 binds flgII-28 and activates the plant immune system. Nat. Plants 2, 1–8 (2016).

    Google Scholar 

  53. Katsuragi, Y. et al. CD2-1, the C-terminal region of flagellin, modulates the induction of immune responses in rice. Mol. Plant Microbe Interact. 28, 648–658 (2015).

    CAS  PubMed  Google Scholar 

  54. Zipfel, C. et al. Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation. Cell 125, 749–760 (2006).

    CAS  PubMed  Google Scholar 

  55. Furukawa, T., Inagaki, H., Takai, R., Hirai, H. & Che, F. S. Two distinct EF-Tu epitopes induce immune responses in rice and Arabidopsis. Mol. Plant Microbe Interact. 27, 113–124 (2014).

    CAS  PubMed  Google Scholar 

  56. Dodds, I., Chen, C., Buscaill, P. & van der Hoorn, R. A. L. Depletion of the NbCORE receptor drastically improves agroinfiltration productivity in older Nicotiana benthamiana plants. Plant Biotechnol. J. 21, 1103–1105 (2023).

    CAS  PubMed  PubMed Central  Google Scholar 

  57. Du, J. et al. Elicitin recognition confers enhanced resistance to Phytophthora infestans in potato. Nat. Plants 1, 1–5 (2015).

    Google Scholar 

  58. Van der Hoorn, R. A. L., Roth, R. & De Wit, P. J. G. M. Identification of distinct specificity determinants in resistance protein Cf-4 allows construction of a Cf-9 mutant that confers recognition of avirulence protein AVR4. Plant Cell 13, 273–285 (2001).

    PubMed  PubMed Central  Google Scholar 

  59. Van Der Hoorn, R. A. L. et al. Structure–function analysis of Cf-9, a receptor-like protein with extracytoplasmic leucine-rich repeats. Plant Cell 17, 1000–1015 (2005).

    PubMed  PubMed Central  Google Scholar 

  60. Wulff, B. B. H., Thomas, C. M., Smoker, M., Grant, M. & Jones, J. D. J. Domain swapping and gene shuffling identify sequences required for induction of an Avr-dependent hypersensitive response by the tomato Cf-4 and Cf-9 proteins. Plant Cell 13, 255–272 (2001).

    CAS  PubMed  PubMed Central  Google Scholar 

  61. Wulff, B. B. H. et al. The major specificity-determining amino acids of the tomato Cf-9 disease resistance protein are at hypervariable solvent-exposed positions in the central leucine-rich repeats. Mol. Plant Microbe Interact. 22, 1203–1213 (2009).

    CAS  PubMed  Google Scholar 

  62. Mueller, K. et al. Chimeric FLS2 receptors reveal the basis for differential flagellin perception in Arabidopsis and tomato. Plant Cell 24, 2213–2224 (2012).

    CAS  PubMed  PubMed Central  Google Scholar 

  63. Albert, M. et al. Arabidopsis thaliana pattern recognition receptors for bacterial elongation factor Tu and flagellin can be combined to form functional chimeric receptors. J. Biol. Chem. 285, 19035–19042 (2010).

    CAS  PubMed  PubMed Central  Google Scholar 

  64. Chakrabarti, A., Panter, S. N., Harrison, K., Jones, J. D. G. & Jones, D. A. Regions of the Cf-9B disease resistance protein able to cause spontaneous necrosis in Nicotiana benthamiana lie within the region controlling pathogen recognition in tomato. Mol. Plant Microbe Interact. 22, 1214–1226 (2009).

    CAS  PubMed  Google Scholar 

  65. Montoya, T. et al. Cloning the tomato Curl3 gene highlights the putative dual role of the leucine-rich repeat receptor kinase tBRI1/SR160 in plant steroid hormone and peptide hormone signaling. Plant Cell 14, 3163–3176 (2002).

    CAS  PubMed  PubMed Central  Google Scholar 

  66. Li, J. & Chory, J. A putative leucine-rich repeat receptor kinase involved in brassinosteroid signal transduction. Cell 90, 929–938 (1997).

    CAS  PubMed  Google Scholar 

  67. Hohmann, U., Lau, K. & Hothorn, M. The structural basis of ligand perception and signal activation by receptor kinases. Annu. Rev. Plant Biol. 68, 109–137 (2017).

    CAS  PubMed  Google Scholar 

  68. She, J. et al. Structural insight into brassinosteroid perception by BRI1. Nature 474, 472–476 (2011).

    CAS  PubMed  PubMed Central  Google Scholar 

  69. Sun, Y. et al. Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex. Science 342, 624–628 (2013).

    CAS  PubMed  Google Scholar 

  70. Lensink, M. F. et al. Impact of AlphaFold on structure prediction of protein complexes: the CASP15-CAPRI experiment. Proteins 91, 1658–1683 (2023).

    CAS  PubMed  PubMed Central  Google Scholar 

  71. Lacombe, S. et al. Interfamily transfer of a plant pattern-recognition receptor confers broad-spectrum bacterial resistance. Nat. Biotechnol. 28, 365–369 (2010). This paper reports the first successful transfer of EFR into a distantly related plant species.

    CAS  PubMed  Google Scholar 

  72. Boschi, F. et al. Enhanced bacterial wilt resistance in potato through expression of Arabidopsis EFR and introgression of quantitative resistance from Solanum commersonii. Front. Plant Sci. 8, 283733 (2017).

    Google Scholar 

  73. Pfeilmeier, S. et al. Expression of the Arabidopsis thaliana immune receptor EFR in Medicago truncatula reduces infection by a root pathogenic bacterium, but not nitrogen-fixing rhizobial symbiosis. Plant Biotechnol. J. 17, 569–579 (2019).

    CAS  PubMed  Google Scholar 

  74. Lu, F. et al. Enhancement of innate immune system in monocot rice by transferring the dicotyledonous elongation factor Tu receptor EFR. J. Integr. Plant Biol. 57, 641–652 (2015).

    CAS  PubMed  Google Scholar 

  75. Schwessinger, B. et al. Transgenic expression of the dicotyledonous pattern recognition receptor EFR in rice leads to ligand-dependent activation of defense responses. PLoS Pathog. 11, e1004809 (2015).

    PubMed  PubMed Central  Google Scholar 

  76. Schoonbeek, H. et al. Arabidopsis EF-Tu receptor enhances bacterial disease resistance in transgenic wheat. N. Phytol. 206, 606–613 (2015).

    CAS  Google Scholar 

  77. Adero, M., Tripathi, J. N., Oduor, R., Zipfel, C. & Tripathi, L. Transgenic expression of Arabidopsis ELONGATION FACTOR-TU RECEPTOR (AtEFR) gene in banana enhances resistance against Xanthomonas campestris pv. musacearum. PLoS ONE 18, e0290884 (2023).

    CAS  PubMed  PubMed Central  Google Scholar 

  78. Hao, G., Pitino, M., Duan, Y. & Stover, E. Reduced susceptibility to Xanthomonas citri in transgenic citrus expressing the FLS2 receptor from Nicotiana benthamiana. Mol. Plant Microbe Interact. 29, 132–142 (2016).

    CAS  PubMed  Google Scholar 

  79. Mitre, L. K. et al. The Arabidopsis immune receptor EFR increases resistance to the bacterial pathogens Xanthomonas and Xylella in transgenic sweet orange. Plant Biotechnol. J. 19, 1294–1296 (2021).

    CAS  PubMed  PubMed Central  Google Scholar 

  80. Piazza, S. et al. The Arabidopsis pattern recognition receptor EFR enhances fire blight resistance in apple. Hortic. Res. 8, 1–9 (2021).

    Google Scholar 

  81. Omar, A. A., Murata, M. M., El-Shamy, H. A., Graham, J. H. & Grosser, J. W. Enhanced resistance to citrus canker in transgenic mandarin expressing Xa21 from rice. Transgenic Res. 27, 179–191 (2018).

    CAS  PubMed  Google Scholar 

  82. Tripathi, J. N., Lorenzen, J., Bahar, O., Ronald, P. & Tripathi, L. Transgenic expression of the rice Xa21 pattern-recognition receptor in banana (Musa sp.) confers resistance to Xanthomonas campestris pv. musacearum. Plant Biotechnol. J. 12, 663–673 (2014).

    CAS  PubMed  Google Scholar 

  83. Albert, I. et al. An RLP23–SOBIR1–BAK1 complex mediates NLP-triggered immunity. Nat. Plants 1, 1–9 (2015).

    Google Scholar 

  84. Kouzai, Y., Kaku, H., Shibuya, N., Minami, E. & Nishizawa, Y. Expression of the chimeric receptor between the chitin elicitor receptor CEBiP and the receptor-like protein kinase Pi-d2 leads to enhanced responses to the chitin elicitor and disease resistance against Magnaporthe oryzae in rice. Plant Mol. Biol. 81, 287–295 (2013).

    CAS  PubMed  Google Scholar 

  85. Kishimoto, K. et al. Enhancement of MAMP signaling by chimeric receptors improves disease resistance in plants. Plant Signal. Behav. 6, 449–451 (2011).

    CAS  PubMed  PubMed Central  Google Scholar 

  86. Holton, N., Nekrasov, V., Ronald, P. C. & Zipfel, C. The phylogenetically-related pattern recognition receptors EFR and XA21 recruit similar immune signaling components in monocots and dicots. PLoS Pathog. 1, e1004602 (2015).

    Google Scholar 

  87. Jehle, A. K. et al. The receptor-like protein ReMAX of Arabidopsis detects the microbe-associated molecular pattern eMax from Xanthomonas. Plant Cell 25, 2330–2340 (2013).

    CAS  PubMed  PubMed Central  Google Scholar 

  88. Zdrzałek, R., Stone, C., De la Concepcion, J. C., Banfield, M. J. & Bentham, A. R. Pathways to engineering plant intracellular NLR immune receptors. Curr. Opin. Plant Biol. 74, 102380 (2023).

    PubMed  Google Scholar 

  89. Ghislain, M. et al. Stacking three late blight resistance genes from wild species directly into African highland potato varieties confers complete field resistance to local blight races. Plant Biotechnol. J. 17, 1119–1129 (2019).

    CAS  PubMed  Google Scholar 

  90. Paluchowska, P., Śliwka, J. & Yin, Z. Late blight resistance genes in potato breeding. Planta 255, 127 (2022).

    CAS  PubMed  PubMed Central  Google Scholar 

  91. Zhu, S., Li, Y., Vossen, J. H., Visser, R. G. F. & Jacobsen, E. Functional stacking of three resistance genes against Phytophthora infestans in potato. Transgenic Res. 21, 89–99 (2012).

    CAS  PubMed  Google Scholar 

  92. Luo, M. et al. A five-transgene cassette confers broad-spectrum resistance to a fungal rust pathogen in wheat. Nat. Biotechnol. 39, 561–566 (2021).

    CAS  PubMed  Google Scholar 

  93. Ascurra, Y. C. T., Wouters, D., Visser, R. G. F., Nürnberger, T. & Vleeshouwers, V. G. A. A. Stacking of PRRs in potato to achieve enhanced resistance against Phytophthora infestans. Preprint at bioRxiv https://doi.org/10.1101/2023.09.07.556738 (2023).

  94. Zhang, J., Li, X., Jiang, G., Xu, Y. & He, Y. Pyramiding of Xa7 and Xa21 for the improvement of disease resistance to bacterial blight in hybrid rice. Plant Breed. 125, 600–605 (2006).

    CAS  Google Scholar 

  95. Pradhan, S. K. et al. Pyramiding of three bacterial blight resistance genes for broad-spectrum resistance in deepwater rice variety, Jalmagna. Rice 8, 1–14 (2015).

    Google Scholar 

  96. Helft, L., Thompson, M. & Bent, A. F. Directed evolution of FLS2 towards novel flagellin peptide recognition. PLoS ONE 11, e0157155 (2016).

    PubMed  PubMed Central  Google Scholar 

  97. Homma, F., Huang, J. & Van Der Hoorn, R. A. L. AlphaFold-multimer predicts cross-kingdom interactions at the plant-pathogen interface. Nat. Commun. 14, 1–13 (2023).

    Google Scholar 

  98. Steinbrenner, A. D. et al. A receptor-like protein mediates plant immune responses to herbivore-associated molecular patterns. Proc. Natl Acad. Sci. USA 117, 31510–31518 (2020).

    CAS  PubMed  PubMed Central  Google Scholar 

  99. Hegenauer, V. et al. The tomato receptor CuRe1 senses a cell wall protein to identify Cuscuta as a pathogen. Nat. Commun. 11, 1–7 (2020).

    Google Scholar 

  100. Gomez-Gomez, L. & Boller, T. FLS2: an LRR receptor–like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis. Mol. Cell 5, 1003–1011 (2000).

    CAS  PubMed  Google Scholar 

  101. Liu, Z. et al. Phytocytokine signalling reopens stomata in plant immunity and water loss. Nature 605, 332–339 (2022).

    CAS  PubMed  PubMed Central  Google Scholar 

  102. Saur, I. M. L. et al. NbCSPR underlies age-dependent immune responses to bacterial cold shock protein in Nicotiana benthamiana. Proc. Natl Acad. Sci. USA 113, 3389–3394 (2016).

    CAS  PubMed  PubMed Central  Google Scholar 

  103. Yamaguchi, Y., Pearce, G. & Ryan, C. A. The cell surface leucine-rich repeat receptor for AtPep1, an endogenous peptide elicitor in Arabidopsis, is functional in transgenic tobacco cells. Proc. Natl Acad. Sci. USA 103, 10104–10109 (2006).

    CAS  PubMed  PubMed Central  Google Scholar 

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Acknowledgements

The authors thank members of the Zipfel laboratory for useful discussions. C.Z. is thankful for support from the Gatsby Charitable Foundation, the University of Zurich, the Zurich-Basel Plant Science Center, the European Research Council and the Swiss National Science Foundation. O.J. is the recipient of a Walter Benjamin Fellowship from the Deutsche Forschungsgemeinschaft (Fellowship ID: 537740606).

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  1. These authors contributed equally: Simon Snoeck, Oliver Johanndrees.

Authors and Affiliations

  1. Institute of Plant and Microbial Biology, Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland

    Simon Snoeck, Oliver Johanndrees & Cyril Zipfel

  2. Center of Plant Molecular Biology (ZMBP), University of Tübingen, Tübingen, Germany

    Thorsten Nürnberger

  3. The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK

    Cyril Zipfel

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S.S., O.J. and C.Z. substantially contributed to discussions of the content. S.S. and O.J. researched the literature and wrote the review. T.N. and C.Z. reviewed and/or edited the manuscript before submission.

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Correspondence to Cyril Zipfel.

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C.Z. is a member of the Scientific Advisory Board of the non-for-profit 2Blades foundation and has received funding from industry on the identification and engineering of plant PRRs. T.N. has received funding from industry for the identification of plant PRRs. The other authors declare no competing interests.

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Snoeck, S., Johanndrees, O., Nürnberger, T. et al. Plant pattern recognition receptors: from evolutionary insight to engineering. Nat Rev Genet 26, 268–278 (2025). https://doi.org/10.1038/s41576-024-00793-z

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