Evidence map›Paper›PMID 31535976›Full record

ArticleeLife2019

Protein engineering expands the effector recognition profile of a rice NLR immune receptor.

Juan Carlos De la Concepcion, Marina Franceschetti, Dan MacLean, Ryohei Terauchi, Sophien Kamoun, Mark J Banfield

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
24.1field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

82 citing papers in PubMed, 150 citations in OpenAlex.

  1. Review
  2. Review
  3. Mechanisms and balanced regulation of plant immunity.Nature reviews. Molecular cell biology · 2026
    Review
  4. Article
  5. Review
  6. Plant NLRs are getting into higher-order architectures.The Plant journal : for cell and molecular biology · 2026
    Review
  7. Article
  8. Review
  9. Precision Editing of NLRS Improves Effector Recognition for Enhanced Disease Resistance.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  10. Review
  11. TheProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. All Roads Lead to Rome: Pathways to Engineering Disease Resistance in Plants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  20. Review

22 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Juan Carlos De la Concepcion *Department of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.
Marina Franceschetti *Department of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.
Dan MacLeanThe Sainsbury Laboratory, University of East Anglia, Norwich, United Kingdom.
Ryohei TerauchiDivision of Genomics and Breeding, Iwate Biotechnology Research Center, Iwate, Japan.
Sophien KamounThe Sainsbury Laboratory, University of East Anglia, Norwich, United Kingdom.ORCID 0000-0002-0290-0315
Mark J BanfieldDepartment of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.ORCID 0000-0001-8921-3835
John Innes Centre · GBUniversity of East Anglia · GBKyoto University · JP

Funding

Biotechnology and Biological Sciences Research Council BB/J004553Biotechnology and Biological Sciences Research Council BB/M02198XBiotechnology and Biological Sciences Research Council BB/P012574H2020 European Research Council 743165Japan Society for the Promotion of Science 15H05779
6 · The paper itself

Abstract

Plant nucleotide binding, leucine-rich repeat (NLR) receptors detect pathogen effectors and initiate an immune response. Since their discovery, NLRs have been the focus of protein engineering to improve disease resistance. However, this approach has proven challenging, in part due to their narrow response specificity. Previously, we revealed the structural basis of pathogen recognition by the integrated heavy metal associated (HMA) domain of the rice NLR Pikp (Maqbool et al., 2015). Here, we used structure-guided engineering to expand the response profile of Pikp to variants of the rice blast pathogen effector AVR-Pik. A mutation located within an effector-binding interface of the integrated Pikp-HMA domain increased the binding affinity for AVR-Pik variants in vitro and in vivo. This translates to an expanded cell-death response to AVR-Pik variants previously unrecognized by Pikp in planta. The structures of the engineered Pikp-HMA in complex with AVR-Pik variants revealed the mechanism of expanded recognition. These results provide a proof-of-concept that protein engineering can improve the utility of plant NLR receptors where direct interaction between effectors and NLRs is established, particularly where this interaction occurs via integrated domains.

Indexed as

Antigens, BacterialNLR ProteinsOryzaPlant ProteinsProtein BindingProtein EngineeringReceptors, ImmunologicRecombinant ProteinsAntigens, BacterialNLR ProteinsPlant ProteinsReceptors, ImmunologicRecombinant ProteinsE. colimolecular biophysicsNLR receptorplant biologyplant disease resistanceprotein engineeringprotein structurericerice blaststructural biology

Identifiers

PMID31535976
PMCPMC6768660
OpenAlexW2973396428

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.