Molecular mimicry of a pathogen virulence target by a plant immune receptor.
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| Title: | Molecular mimicry of a pathogen virulence target by a plant immune receptor. |
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| Authors: | Gómez De La Cruz, Diana (AUTHOR), Ingram, Thomas (AUTHOR), Zdrzałek, Rafał (AUTHOR), Taylor, Jodie (AUTHOR), Wawryk-Khamdavong, Aleksandra (AUTHOR), Bachowska, Kinga (AUTHOR), Banfield, Mark J. (AUTHOR), Talbot, Nicholas J. (AUTHOR), Moscou, Matthew J. (AUTHOR) |
| Source: | Science. 6/4/2026, Vol. 392 Issue 6802, p1050-1055. 6p. |
| Subjects: | Molecular mimicry, Disease resistance of plants, Immune recognition, Microbial virulence, Plant immunology, Plant diseases, Immunologic receptors, Natural immunity |
| 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, how receptors evolve new recognition specificities remains poorly understood. We found that the plant NLR MLA3 (Mildew locus a 3) has evolved to recognize a pathogen effector by acting as a molecular mimic of an effector virulence target, thereby triggering an immune response. By introducing the mimic's binding interface into the wheat stem rust resistance protein SR50, we bioengineered a chimeric receptor with dual recognition activities that conferred resistance to two major cereal pathogens in barley transgenic lines. These results demonstrate that molecular mimicry by immune receptors can be harnessed to engineer multiple disease resistance. Editor's summary: Plant intracellular immune receptors detect effector proteins secreted by pathogens, but how these receptors evolve new detection capabilities is not well understood. Gómez De La Cruz et al. found that a barley receptor called MLA3 has evolved to resemble the very host protein that a blast fungus effector targets. Structural analysis confirmed that MLA3 and the original target share a similar binding interface with the effector. Using this insight, the authors engineered a chimeric rye immune receptor that detects effectors from both wheat stem rust and blast fungus, two major threats to cereal crops. —Unnati Sonawala and Madeleine Seale [ABSTRACT FROM AUTHOR] |
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| Database: | Psychology and Behavioral Sciences Collection |
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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, how receptors evolve new recognition specificities remains poorly understood. We found that the plant NLR MLA3 (Mildew locus a 3) has evolved to recognize a pathogen effector by acting as a molecular mimic of an effector virulence target, thereby triggering an immune response. By introducing the mimic's binding interface into the wheat stem rust resistance protein SR50, we bioengineered a chimeric receptor with dual recognition activities that conferred resistance to two major cereal pathogens in barley transgenic lines. These results demonstrate that molecular mimicry by immune receptors can be harnessed to engineer multiple disease resistance. Editor's summary: Plant intracellular immune receptors detect effector proteins secreted by pathogens, but how these receptors evolve new detection capabilities is not well understood. Gómez De La Cruz et al. found that a barley receptor called MLA3 has evolved to resemble the very host protein that a blast fungus effector targets. Structural analysis confirmed that MLA3 and the original target share a similar binding interface with the effector. Using this insight, the authors engineered a chimeric rye immune receptor that detects effectors from both wheat stem rust and blast fungus, two major threats to cereal crops. —Unnati Sonawala and Madeleine Seale [ABSTRACT FROM AUTHOR] |
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| ISSN: | 00368075 |
| DOI: | 10.1126/science.aef9946 |
