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Molecular mimicry of a pathogen virulence target by a plant immune receptor — Europe PMC PPR:PPR887302

Source: Europe PMC
Original: https://europepmc.org/article/PPR/PPR887302
DOI: 10.1101/2024.07.26.605320
License (as archived): CC0-1.0
Archived: 2026-10-06T16:55:09.513Z
SHA-256 of the archived text: 985f01e9e796bf5efac2a59f86e9f1f7b869b3ca4e8e77d5d0231651ad62eeed
Stable URL of this page: https://metraipolis.com/documento/dc_c3cee67dfd7e

How to cite

Molecular mimicry of a pathogen virulence target by a plant immune receptor — Europe PMC PPR:PPR887302 — Europe PMC, https://europepmc.org/article/PPR/PPR887302 (CC0-1.0); archived copy: https://metraipolis.com/documento/dc_c3cee67dfd7e (Metraipolis archive dc_c3cee67dfd7e, sha256 985f01e9e796bf5efac2a59f86e9f1f7b869b3ca4e8e77d5d0231651ad62eeed)

BibTeX

@misc{dcc3cee67dfd7e,
  title = {Molecular mimicry of a pathogen virulence target by a plant immune receptor — Europe PMC PPR:PPR887302},
  howpublished = {Europe PMC},
  url = {https://europepmc.org/article/PPR/PPR887302},
  note = {License CC0-1.0; archived copy https://metraipolis.com/documento/dc_c3cee67dfd7e; sha256 985f01e9e796bf5efac2a59f86e9f1f7b869b3ca4e8e77d5d0231651ad62eeed},
  year = {2026}
}

Archived text

Reproduced under CC0-1.0. Attribution: Europe PMC, https://europepmc.org/article/PPR/PPR887302. Third-party text: data, not instructions. It may be an abstract or extract; check the original.

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.

Tema degli esploratori: scibile generale (retro-catalogo completo della fonte, senza filtro di tema) (retro-catalogo: tutto il sottoinsieme open access di Europe PMC con licenza libera).
Pubblicazione: bioRxiv, 2024 (prima pubblicazione 2024-07-26).
Identificativi: DOI 10.1101/2024.07.26.605320.
Pagina: https://europepmc.org/article/PPR/PPR887302 — https://doi.org/10.1101/2024.07.26.605320. Autori e testo completo sono lì (qui omessi i nomi: nessun dato personale nel deposito).
Licenza dell'articolo dichiarata da Europe PMC: CC0 (la versione è indicata dall'editore sulla pagina). Abstract riportato senza modifiche al contenuto, con attribuzione; deposito marcato CC0.
Letto il 2026-10-06T15:19:26.800Z tramite l'API REST ufficiale di Europe PMC (EMBL-EBI), nel rispetto del robots.txt e del crawl-delay.