Evidence map›Paper›PMID 24623187›Full record

ArticleCurrent microbiology2014

A sunflower lectin with antifungal properties and putative medical mycology applications.

Mariana Regente, Gabriel B Taveira, Marcela Pinedo, Maria Mercedes Elizalde, Ana Julia Ticchi, Mariângela S S Diz, Andre O Carvalho, Laura de la Canal, Valdirene M Gomes

Abstract read
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In one paragraph

Article in Current microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 60 citations in OpenAlex.

  1. Jacalin-Related LectinPlants (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. 130 years of Plant Lectin Research.Glycoconjugate journal · 2020
    Review
  12. Article
  13. Article
  14. Anti-Neuroblastoma Properties of a Recombinant Sunflower Lectin.International journal of molecular sciences · 2017
    Article
  15. Article
  16. A Chitin-binding Protein Purified fromFrontiers in microbiology · 2017
    Article
  17. Lectins, Interconnecting Proteins with Biotechnological/Pharmacological and Therapeutic Applications.Evidence-based complementary and alternative medicine : eCAM · 2017
    Review
  18. Article
  19. Review
  20. 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

9 authors at 3 institutions in 2 countries.

Mariana RegenteInstituto de Investigaciones Biológicas, Universidad Nacional de Mar del Plata - CONICET, Funes 3250, 7600, Mar del Plata, Argentina.
Gabriel B Taveira
Marcela Pinedo
Maria Mercedes Elizalde
Ana Julia Ticchi
Mariângela S S Diz
Andre O Carvalho
Laura de la Canal
Valdirene M Gomes
State University of Norte Fluminense · BRConsejo Nacional de Investigaciones Científicas y Técnicas · ARNational University of Mar del Plata · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lectins are carbohydrate-binding proteins with a high specificity for a variety of glycoconjugate sugar motifs. The jacalin-related lectins (JRL) are considered to be a small sub-family composed of galactose- and mannose-specific members. Using a proteomics approach, we have detected a 16 kDa protein (Helja) in sunflower seedlings that were further purified by mannose-agarose affinity chromatography. The aim of this work was to characterize the biological activity of Helja and to explore potential applications for the antifungal activity of this plant lectin against medically important yeasts. To initially assess the agglutination properties of the lectin, Saccharomyces cerevisiae cells were incubated with increasing concentrations of the purified lectin. At a concentration of 120 μg/ml, Helja clearly agglutinated these cells. The ability of different sugars to inhibit S. cerevisiae cell agglutination determined its carbohydrate-specificity. Among the monosaccharides tested, D-mannose had the greatest inhibitory effect, with a minimal concentration of 1.5 mM required to prevent cell agglutination. The antifungal activity was evaluated using pathogenic fungi belonging to the Candida and Pichia genera. We demonstrate that 200 μg/ml of Helja inhibited the growth of all yeasts, and it induced morphological changes, particularly through pseudohyphae formation on Candida tropicalis. Helja alters the membrane permeability of the tested fungi and is also able to induce the production of reactive oxygen species in C. tropicalis cells. We concluded that Helja is a mannose-binding JRL with cell agglutination capabilities and antifungal activity against yeasts. The biological properties of Helja may have practical applications in the control of human pathogens.

Indexed as

AgglutinationAntifungal AgentsCandidaCell MembraneGalactoseHelianthusHumansLectinsMannoseMycosesNitric OxidePichiaPlant LectinsPlant ProteinsReactive Oxygen SpeciesSeedlingsAntifungal AgentsGalactosejacalinLectinsMannoseNitric OxidePlant LectinsPlant ProteinsReactive Oxygen Species

Identifiers

PMID24623187
OpenAlexW2068505206

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.