Evidence map›Paper›PMID 28817232›Full record

ArticleMolecular plant pathology2018

Crystal structure of the Melampsora lini effector AvrP reveals insights into a possible nuclear function and recognition by the flax disease resistance protein P.

Xiaoxiao Zhang, Nadya Farah, Laura Rolston, Daniel J Ericsson, Ann-Maree Catanzariti, Maud Bernoux, Thomas Ve, Katerina Bendak, Chunhong Chen, Joel P Mackay and 7 more

Open access · greenAbstract read
In one paragraph

Article in Molecular plant pathology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
5.6field-weighted citation impact, top 5% 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

11 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structural polymorphisms within a common powdery mildew effector scaffold as a driver of coevolution with cereal immune receptors.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Evolution of Disease Defense Genes and Their Regulators in Plants.International journal of molecular sciences · 2019
    Review
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

17 authors at 8 institutions in 1 country.

Xiaoxiao ZhangSchool of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia.
Nadya FarahDivision of Plant Sciences, Research School of Biology, Australian National University, Acton, Australian Capital Territory 2601, Australia.
Laura RolstonDivision of Plant Sciences, Research School of Biology, Australian National University, Acton, Australian Capital Territory 2601, Australia.
Daniel J EricssonSchool of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia.
Ann-Maree CatanzaritiDivision of Plant Sciences, Research School of Biology, Australian National University, Acton, Australian Capital Territory 2601, Australia.
Maud BernouxCommonwealth Scientific and Industrial Research Organisation Agriculture and Food, Canberra, Australian Capital Territory 2601, Australia.
Thomas VeSchool of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia.
Katerina BendakSchool of Molecular Bioscience, University of Sydney, Sydney, New South Wales 2006, Australia.
Chunhong ChenCommonwealth Scientific and Industrial Research Organisation Agriculture and Food, Canberra, Australian Capital Territory 2601, Australia.
Joel P MackaySchool of Molecular Bioscience, University of Sydney, Sydney, New South Wales 2006, Australia.
Gregory J LawrenceCommonwealth Scientific and Industrial Research Organisation Agriculture and Food, Canberra, Australian Capital Territory 2601, Australia.
Adrienne HardhamDivision of Plant Sciences, Research School of Biology, Australian National University, Acton, Australian Capital Territory 2601, Australia.
Jeffrey G EllisCommonwealth Scientific and Industrial Research Organisation Agriculture and Food, Canberra, Australian Capital Territory 2601, Australia.
Simon J WilliamsSchool of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia.
Peter N DoddsCommonwealth Scientific and Industrial Research Organisation Agriculture and Food, Canberra, Australian Capital Territory 2601, Australia.
David A JonesDivision of Plant Sciences, Research School of Biology, Australian National University, Acton, Australian Capital Territory 2601, Australia.
Bostjan KobeSchool of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia.
Australian National University · AUAgriculture and Food · AUCommonwealth Scientific and Industrial Research Organisation · AUUniversity of Sydney · AUACT GovernmentAustralian Synchrotron · AUGriffith University · AUUniversity of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The effector protein AvrP is secreted by the flax rust fungal pathogen (Melampsora lini) and recognized specifically by the flax (Linum usitatissimum) P disease resistance protein, leading to effector-triggered immunity. To investigate the biological function of this effector and the mechanisms of specific recognition by the P resistance protein, we determined the crystal structure of AvrP. The structure reveals an elongated zinc-finger-like structure with a novel interleaved zinc-binding topology. The residues responsible for zinc binding are conserved in AvrP effector variants and mutations of these motifs result in a loss of P-mediated recognition. The first zinc-coordinating region of the structure displays a positively charged surface and shows some limited similarities to nucleic acid-binding and chromatin-associated proteins. We show that the majority of the AvrP protein accumulates in the plant nucleus when transiently expressed in Nicotiana benthamiana cells, suggesting a nuclear pathogenic function. Polymorphic residues in AvrP and its allelic variants map to the protein surface and could be associated with differences in recognition specificity. Several point mutations of residues on the non-conserved surface patch result in a loss of recognition by P, suggesting that these residues are required for recognition.

Indexed as

Disease ResistanceAgrobacteriumAmino Acid MotifsAmino Acid SequenceBasidiomycotaCell NucleusConserved SequenceCrystallography, X-RayFlaxFungal ProteinsModels, MolecularNicotianaPlant CellsPlant DiseasesPlant ProteinsProtein BindingFungal ProteinsPlant ProteinsZinccrystal structureeffector-triggered immunityflax rust (Melampsora lini) effectorNLR [nucleotide-binding and oligomerization domain (NOD)-like receptornuclear localizationnucleotide-binding/leucine-rich repeat receptor]plant disease resistancezinc finger

Identifiers

PMID28817232
PMCPMC6638141
OpenAlexW2747555641

What OpenQuestion holds

Textmetadata
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.