Evidence map›Paper›PMID 23133547›Full record

ArticlePloS one2012

Rubber elongation factor (REF), a major allergen component in Hevea brasiliensis latex has amyloid properties.

Karine Berthelot, Sophie Lecomte, Yannick Estevez, Bénédicte Coulary-Salin, Ahmed Bentaleb, Christophe Cullin, Alain Deffieux, Frédéric Peruch

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. 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
1.9field-weighted citation impact, top 15% 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

28 citing papers in PubMed, 90 citations in OpenAlex.

  1. The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
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  4. EMBER multidimensional spectral microscopy enables quantitative determination of disease- and cell-specific amyloid strains.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  14. Review
  15. Article
  16. Article
  17. Biosynthesis of Natural Rubber: Current State and Perspectives.International journal of molecular sciences · 2018
    Review
  18. Article
  19. Article
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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

8 authors at 6 institutions in 1 country.

Karine BerthelotCNRS, LCPO, UMR 5629, Pessac, France. kberthelot@enscbp.fr
Sophie Lecomte
Yannick Estevez
Bénédicte Coulary-Salin
Ahmed Bentaleb
Christophe Cullin
Alain Deffieux
Frédéric Peruch
Centre National de la Recherche Scientifique · FRLaboratoire de Chimie des Polymères Organiques · FRChimie et Biologie des Membranes et des Nanoobjects · FRÉcole Nationale Supérieure de Chimie, de Biologie et de Physique · FRInstitut de Biochimie et Génétique Cellulaires · FRPaul Pascal Research Center · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

REF (Hevb1) and SRPP (Hevb3) are two major components of Hevea brasiliensis latex, well known for their allergenic properties. They are obviously taking part in the biosynthesis of natural rubber, but their exact function is still unclear. They could be involved in defense/stress mechanisms after tapping or directly acting on the isoprenoid biosynthetic pathway. The structure of these two proteins is still not described. In this work, it was discovered that REF has amyloid properties, contrary to SRPP. We investigated their structure by CD, TEM, ATR-FTIR and WAXS and neatly showed the presence of β-sheet organized aggregates for REF, whereas SRPP mainly fold as a helical protein. Both proteins are highly hydrophobic but differ in their interaction with lipid monolayers used to mimic the monomembrane surrounding the rubber particles. Ellipsometry experiments showed that REF seems to penetrate deeply into the monolayer and SRPP only binds to the lipid surface. These results could therefore clarify the role of these two paralogous proteins in latex production, either in the coagulation of natural rubber or in stress-related responses. To our knowledge, this is the first report of an amyloid formed from a plant protein. This suggests also the presence of functional amyloid in the plant kingdom.

Indexed as

AllergensAmyloidCloning, MolecularEndopeptidase KFluorescent DyesHeveaLatexLipidsMicroscopy, Electron, TransmissionMolecular Sequence DataPeptide Elongation FactorsPhylogenyPolymersProtein BindingProtein Structure, SecondaryRubberAllergensAmyloidEndopeptidase KFluorescent DyesLatexLipidsPeptide Elongation FactorsPolymersRubber

Identifiers

PMID23133547
PMCPMC3485013
OpenAlexW1991577517

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.