Evidence map›Paper›PMID 27374416›Full record

ArticleMolecular nutrition & food research2016

Heat processing of peanut seed enhances the sensitization potential of the major peanut allergen Ara h 6.

Blanche Guillon, Hervé Bernard, Marie-Françoise Drumare, Stéphane Hazebrouck, Karine Adel-Patient

Abstract read
In one paragraph

Article in Molecular nutrition & food research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Variable IgE cross-reactivity between peanut 2S-albumins: The case for measuring IgE to both Ara h 2 and Ara h 6.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2019
    Trial
  2. Review
  3. Mouse Models of Food Allergies: Where Do They Take Us?Clinical reviews in allergy & immunology · 2026
    Review
  4. Review
  5. Review
  6. The Effector Function of Allergens.Frontiers in allergy · 2022
    Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Peanut allergens.Molecular immunology · 2018
    Review
  15. 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

5 authors.

Blanche GuillonUMR CEA-INRA Service de Pharmacologie et d'Immunoanalyse, Université Paris-Saclay, Gif-sur-Yvette, France.
Hervé BernardUMR CEA-INRA Service de Pharmacologie et d'Immunoanalyse, Université Paris-Saclay, Gif-sur-Yvette, France.
Marie-Françoise DrumareUMR CEA-INRA Service de Pharmacologie et d'Immunoanalyse, Université Paris-Saclay, Gif-sur-Yvette, France.
Stéphane HazebrouckUMR CEA-INRA Service de Pharmacologie et d'Immunoanalyse, Université Paris-Saclay, Gif-sur-Yvette, France.
Karine Adel-PatientUMR CEA-INRA Service de Pharmacologie et d'Immunoanalyse, Université Paris-Saclay, Gif-sur-Yvette, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

scopeProcessing of food has been shown to impact IgE binding and functionality of food allergens. In the present study, we investigated the impact of heat processing on the sensitization capacity of Ara h 6, a major peanut allergen and one of the most potent elicitors of the allergic reaction. METHODS AND

resultsPeanut extracts obtained from raw or heat-processed peanut and some fractions thereof were biochemically and immunochemically characterized. These extracts/fractions, purified Ara h 6, or recombinant Ara h 6 including Ara h 6 mutants lacking disulfide bridges were used in in vitro digestion tests and mouse models of experimental sensitization. Peanut roasting led to the formation of complexes of high molecular weight, notably between Ara h 6 and Ara h 1, which supported the induction of IgE specific to native Ara h 6. On the contrary, a fraction containing free monomeric 2S albumins or purified native Ara h 6 displayed no intrinsic allergenicity. In addition to complex formation, heat denaturation and/or partial destabilization enhanced Ara h 6 immunogenicity and increased its sensitivity to digestion.

conclusionThese results suggest that sensitization potency and IgE binding capacity can be supported by different structures, modified and/or produced during food processing in interaction with other food constituents.

Indexed as

Food HandlingHot Temperature2S Albumins, PlantAnimalsAntigens, PlantArachisDisease Models, AnimalFemaleMiceMice, Inbred BALB CPeanut HypersensitivitySeeds2S Albumins, PlantAntigens, PlantAra h 6 allergen, Arachis hypogaeaAllergenicity assessmentAra h 6Food processingIgE inductionin vitro digestion test

Identifiers

PMID27374416
PMCPMC5213772

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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.