Evidence map›Paper›PMID 25976013›Full record

ArticleMolecular plant pathology2016

Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum.

Lucía Citores, Rosario Iglesias, Carolina Gay, José Miguel Ferreras

Open access · bronzeAbstract read
In one paragraph

Article in Molecular plant pathology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

12 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Deciphering Molecular Determinants UnderlyingInternational journal of molecular sciences · 2022
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Ribosome Inactivating Proteins from Rosaceae.Molecules (Basel, Switzerland) · 2016
    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

4 authors at 2 institutions in 2 countries.

Lucía CitoresDepartment of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, 47011, Valladolid, Spain.
Rosario IglesiasDepartment of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, 47011, Valladolid, Spain.
Carolina GayLaboratory of Research on Proteins, Faculty of Exact and Natural Sciences and Surveying, National University of the Northeast (UNNE), 3400, Corrientes, Argentina.
José Miguel FerrerasDepartment of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, 47011, Valladolid, Spain.
Universidad de Valladolid · ESNational University of the Northeast · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) leaves is an apoplastic protein induced by signalling compounds, such as hydrogen peroxide and salicylic acid, which has been reported to be involved in defence against viruses. Here, we report that, at a concentration much lower than that present in the apoplast, BE27 displays antifungal activity against the green mould Penicillium digitatum, a necrotrophic fungus that colonizes wounds and grows in the inter- and intracellular spaces of the tissues of several edible plants. BE27 is able to enter into the cytosol and kill fungal cells, thus arresting the growth of the fungus. The mechanism of action seems to involve ribosomal RNA (rRNA) N-glycosylase activity on the sarcin-ricin loop of the major rRNA which inactivates irreversibly the fungal ribosomes, thus inhibiting protein synthesis. We compared the C-terminus of the BE27 structure with antifungal plant defensins and hypothesize that a structural motif composed of an α-helix and a β-hairpin, similar to the γ-core motif of defensins, might contribute to the specific interaction with the fungal plasma membranes, allowing the protein to enter into the cell.

Indexed as

Amino Acid MotifsAmino Acid SequenceAntifungal AgentsBeta vulgarisComputer SimulationModels, MolecularMolecular Sequence DataPenicilliumPlant ProteinsRibosome Inactivating ProteinsRibosomesAntifungal AgentsPlant ProteinsRibosome Inactivating Proteinsapoplastdefensingreen mouldplant defencepokeweed antiviral protein (PAP)polynucleotide:adenosine glycosylaserRNA N-glycosylase

Identifiers

PMID25976013
PMCPMC6638414
OpenAlexW1844505697

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.