Evidence map›Paper›PMID 11553720›Full record

ArticleMolecular biology of the cell2001

Mediation of elicitin activity on tobacco is assumed by elicitin-sterol complexes.

H Osman, S Vauthrin, V Mikes, M L Milat, F Panabières, A Marais, S Brunie, B Maume, M Ponchet, J P Blein

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Genomic and transcriptomic analyses ofFrontiers in microbiology · 2024
    Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Phytophthora cinnamomi.Molecular plant pathology · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Sterol biosynthesis in oomycete pathogens.Plant signaling & behavior · 2010
    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

10 authors.

H OsmanUnité Mixte de Recherche 692, Laboratoire de Phytopharmacie et de Biochimie des Interactions Cellulaires, Institut National de la Recherche Agronomique, 21065 Dijon-cedex, France.
S Vauthrin
V Mikes
M L Milat
F Panabières
A Marais
S Brunie
B Maume
M Ponchet
J P Blein

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Elicitins secreted by phytopathogenic Phytophthora spp. are proteinaceous elicitors of plant defense mechanisms and were demonstrated to load, carry, and transfer sterols between membranes. The link between elicitor and sterol-loading properties was assessed with the use of site-directed mutagenesis of the 47 and 87 cryptogein tyrosine residues, postulated to be involved in sterol binding. Mutated cryptogeins were tested for their ability to load sterols, bind to plasma membrane putative receptors, and trigger biological responses. For each mutated elicitin, the chemical characterization of the corresponding complexes with stigmasterol (1:1 stoichiometry) demonstrated their full functionality. However, these proteins were strongly altered in their sterol-loading efficiency, specific binding to high-affinity sites, and activities on tobacco cells. Ligand replacement experiments strongly suggest that the formation of a sterol-elicitin complex is a requisite step before elicitins fasten to specific binding sites. This was confirmed with the use of two sterol-preloaded elicitins. Both more rapidly displaced labeled cryptogein from its specific binding sites than the unloaded proteins. Moreover, the binding kinetics of elicitins are related to their biological effects, which constitutes the first evidence that binding sites could be the biological receptors. The first event involved in elicitin-mediated cell responses is proposed to be the protein loading with a sterol molecule.

Indexed as

Algal ProteinsBinding SitesCalciumCell MembraneCells, CulturedFungal ProteinsHost-Parasite InteractionsHydrogen-Ion ConcentrationModels, BiologicalModels, MolecularNicotianaPhytophthoraPlant DiseasesPlant ProteinsProtein BindingProtein ConformationAlgal ProteinsCalciumcryptogein protein, Phytophthora cryptogeaelicitin, PhytophthoraFungal ProteinsPlant ProteinsProtein IsoformsProteinsReceptors, Cell SurfaceSterolsTyrosine

Identifiers

PMID11553720
PMCPMC59716

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.