Evidence map›Paper›PMID 26304198›Full record

ArticleeLife2015

Structural basis of pathogen recognition by an integrated HMA domain in a plant NLR immune receptor.

A Maqbool, H Saitoh, M Franceschetti, C E M Stevenson, A Uemura, H Kanzaki, S Kamoun, R Terauchi, M J Banfield

Abstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers.

0numbers the graph read from it
0cells of the map it votes in
152citing papers in PubMed
–field-weighted citation impact
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

152 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
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  6. Article
  7. Structure-informed engineering of plant-microbe interactions.The Plant journal : for cell and molecular biology · 2026
    Review
  8. Article
  9. Article
  10. Plant NLRs are getting into higher-order architectures.The Plant journal : for cell and molecular biology · 2026
    Review
  11. Article
  12. Review
  13. Precision Editing of NLRS Improves Effector Recognition for Enhanced Disease Resistance.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

92 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

9 authors.

A MaqboolDepartment of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.
H SaitohIwate Biotechnology Research Center, Kitakami, Japan.
M FranceschettiDepartment of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.
C E M StevensonDepartment of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.
A UemuraIwate Biotechnology Research Center, Kitakami, Japan.
H KanzakiIwate Biotechnology Research Center, Kitakami, Japan.
S KamounThe Sainsbury Laboratory, Norwich, United Kingdom.ORCID http://orcid.org/0000-0002-0290-0315
R TerauchiIwate Biotechnology Research Center, Kitakami, Japan.
M J BanfieldDepartment of Biological Chemistry, John Innes Centre, Norwich, United Kingdom.ORCID http://orcid.org/0000-0001-8921-3835

Funding

Biotechnology and Biological Sciences Research Council BB/J00453Biotechnology and Biological Sciences Research Council BB/M02198XBiotechnology and Biological Sciences Research Council BBS/E/J/000C0624
6 · The paper itself

Abstract

Plants have evolved intracellular immune receptors to detect pathogen proteins known as effectors. How these immune receptors detect effectors remains poorly understood. Here we describe the structural basis for direct recognition of AVR-Pik, an effector from the rice blast pathogen, by the rice intracellular NLR immune receptor Pik. AVR-PikD binds a dimer of the Pikp-1 HMA integrated domain with nanomolar affinity. The crystal structure of the Pikp-HMA/AVR-PikD complex enabled design of mutations to alter protein interaction in yeast and in vitro, and perturb effector-mediated response both in a rice cultivar containing Pikp and upon expression of AVR-PikD and Pikp in the model plant Nicotiana benthamiana. These data reveal the molecular details of a recognition event, mediated by a novel integrated domain in an NLR, which initiates a plant immune response and resistance to rice blast disease. Such studies underpin novel opportunities for engineering disease resistance to plant pathogens in staple food crops.

Indexed as

Crystallography, X-RayModels, MolecularNicotianaOryzaPlant ProteinsProtein ConformationProtein Interaction MappingReceptors, ImmunologicPlant ProteinsReceptors, Immunologicbiophysicseffector proteinintegrated sensor domainplant biologyplant disease resistancericerice blast diseasestructural biology

Identifiers

PMID26304198
PMCPMC4547098

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.