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.
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]
Copyright of Science is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Molecular mimicry of a pathogen virulence target by a plant immune receptor.
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  Data: <searchLink fieldCode="AR" term="%22Gómez+De+La+Cruz%2C+Diana%22">Gómez De La Cruz, Diana</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Ingram%2C+Thomas%22">Ingram, Thomas</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Zdrzałek%2C+Rafał%22">Zdrzałek, Rafał</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Taylor%2C+Jodie%22">Taylor, Jodie</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Wawryk-Khamdavong%2C+Aleksandra%22">Wawryk-Khamdavong, Aleksandra</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Bachowska%2C+Kinga%22">Bachowska, Kinga</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Banfield%2C+Mark+J%2E%22">Banfield, Mark J.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Talbot%2C+Nicholas+J%2E%22">Talbot, Nicholas J.</searchLink> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Moscou%2C+Matthew+J%2E%22">Moscou, Matthew J.</searchLink> (AUTHOR)
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  Data: <searchLink fieldCode="JN" term="%22Science%22">Science</searchLink>. 6/4/2026, Vol. 392 Issue 6802, p1050-1055. 6p.
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  Data: <searchLink fieldCode="DE" term="%22Molecular+mimicry%22">Molecular mimicry</searchLink><br /><searchLink fieldCode="DE" term="%22Disease+resistance+of+plants%22">Disease resistance of plants</searchLink><br /><searchLink fieldCode="DE" term="%22Immune+recognition%22">Immune recognition</searchLink><br /><searchLink fieldCode="DE" term="%22Microbial+virulence%22">Microbial virulence</searchLink><br /><searchLink fieldCode="DE" term="%22Plant+immunology%22">Plant immunology</searchLink><br /><searchLink fieldCode="DE" term="%22Plant+diseases%22">Plant diseases</searchLink><br /><searchLink fieldCode="DE" term="%22Immunologic+receptors%22">Immunologic receptors</searchLink><br /><searchLink fieldCode="DE" term="%22Natural+immunity%22">Natural immunity</searchLink>
– Name: Abstract
  Label: Abstract
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  Data: 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]
– Name: AbstractSuppliedCopyright
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  Data: <i>Copyright of Science is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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      – Type: doi
        Value: 10.1126/science.aef9946
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      – Code: eng
        Text: English
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        PageCount: 6
        StartPage: 1050
    Subjects:
      – SubjectFull: Molecular mimicry
        Type: general
      – SubjectFull: Disease resistance of plants
        Type: general
      – SubjectFull: Immune recognition
        Type: general
      – SubjectFull: Microbial virulence
        Type: general
      – SubjectFull: Plant immunology
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      – SubjectFull: Plant diseases
        Type: general
      – SubjectFull: Immunologic receptors
        Type: general
      – SubjectFull: Natural immunity
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      – TitleFull: Molecular mimicry of a pathogen virulence target by a plant immune receptor.
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              Text: 6/4/2026
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              Y: 2026
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