Evidence map›Paper›PMID 21082183›Full record

ArticlePlant cell reports2011

Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases.

Laura Carrillo, Manuel Martinez, Koreen Ramessar, Inés Cambra, Pedro Castañera, Felix Ortego, Isabel Díaz

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Article in Plant cell reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

40 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Plant Defenses AgainstPlants (Basel, Switzerland) · 2020
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The Beneficial Endophytic FungusFrontiers in plant science · 2018
    Article
  19. Article
  20. Article
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

7 authors.

Laura CarrilloDpto. Biología Medioambiental, Centro de Investigaciones Biológicas, CSIC, Ramiro de Maéztu 9, 28040 Madrid, Spain.
Manuel Martinez
Koreen Ramessar
Inés Cambra
Pedro Castañera
Felix Ortego
Isabel Díaz

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phytocystatins are inhibitors of cysteine-proteases from plants putatively involved in plant defence based on their capability of inhibit heterologous enzymes. We have previously characterised the whole cystatin gene family members from barley (HvCPI-1 to HvCPI-13). The aim of this study was to assess the effects of barley cystatins on two phytophagous spider mites, Tetranychus urticae and Brevipalpus chilensis. The determination of proteolytic activity profile in both mite species showed the presence of the cysteine-proteases, putative targets of cystatins, among other enzymatic activities. All barley cystatins, except HvCPI-1 and HvCPI-7, inhibited in vitro mite cathepsin L- and/or cathepsin B-like activities, HvCPI-6 being the strongest inhibitor for both mite species. Transgenic maize plants expressing HvCPI-6 protein were generated and the functional integrity of the cystatin transgene was confirmed by in vitro inhibitory effect observed against T. urticae and B. chilensis protein extracts. Feeding experiments impaired on transgenic lines performed with T. urticae impaired mite development and reproductive performance. Besides, a significant reduction of cathepsin L-like and/or cathepsin B-like activities was observed when the spider mite fed on maize plants expressing HvCPI-6 cystatin. These findings reveal the potential of barley cystatins as acaricide proteins to protect plants against two important mite pests.

Indexed as

AnimalsBase SequenceCrosses, GeneticCystatinsCysteine ProteasesElectrophoresis, Polyacrylamide GelFeeding BehaviorGenes, PlantHordeumImmunity, InnateMitesMolecular Sequence DataPlant DiseasesPlants, Genetically ModifiedProtein Processing, Post-TranslationalRecombinant ProteinsCystatinsCysteine ProteasesRecombinant Proteins

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Registered trials

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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.