Evidence map›Paper›PMID 24936296›Full record

ArticleFood science & nutrition2014

The role of N-glycosylation in kiwi allergy.

María Garrido-Arandia, Amaya Murua-García, Aranzazu Palacin, Leticia Tordesillas, Cristina Gómez-Casado, Natalia Blanca-Lopez, Tania Ramos, Gabriela Canto, Carlos Blanco, Javier Cuesta-Herranz and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Food science & nutrition, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

4 citing papers in PubMed, 21 citations in OpenAlex.

  1. Allergy to Thaumatin-like Proteins-What Do We Know?Foods (Basel, Switzerland) · 2025
    Review
  2. Article
  3. Article
  4. Carbohydrates as food allergens.Asia Pacific allergy · 2015
    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

13 authors at 5 institutions in 1 country.

María Garrido-ArandiaCentre for Plant Biotechnology and Genomics U.P.M. - I.N.I.A., Campus de Montegancedo Pozuelo de Alarcón, Madrid, Spain.
Amaya Murua-GarcíaCentre for Plant Biotechnology and Genomics U.P.M. - I.N.I.A., Campus de Montegancedo Pozuelo de Alarcón, Madrid, Spain.
Aranzazu PalacinCentre for Plant Biotechnology and Genomics U.P.M. - I.N.I.A., Campus de Montegancedo Pozuelo de Alarcón, Madrid, Spain.
Leticia TordesillasCentre for Plant Biotechnology and Genomics U.P.M. - I.N.I.A., Campus de Montegancedo Pozuelo de Alarcón, Madrid, Spain.
Cristina Gómez-CasadoCentre for Plant Biotechnology and Genomics U.P.M. - I.N.I.A., Campus de Montegancedo Pozuelo de Alarcón, Madrid, Spain.
Natalia Blanca-LopezAllergy Service, Hospital Infanta Leonor Madrid, Spain.
Tania RamosHealth Research Institute La Princesa (IP) Madrid, Spain.
Gabriela CantoAllergy Service, Hospital Infanta Leonor Madrid, Spain.
Carlos BlancoHealth Research Institute La Princesa (IP) Madrid, Spain.
Javier Cuesta-HerranzIIS-Allergy Service, Fundación Jiménez Díaz Madrid, Spain.
Rosa Sánchez-MongeCentre for Plant Biotechnology and Genomics U.P.M. - I.N.I.A., Campus de Montegancedo Pozuelo de Alarcón, Madrid, Spain.
Luis F PaciosCentre for Plant Biotechnology and Genomics U.P.M. - I.N.I.A., Campus de Montegancedo Pozuelo de Alarcón, Madrid, Spain ; Biotechnology Department, ETSI de Montes, Technical University Madrid, Spain.
Araceli Díaz PeralesCentre for Plant Biotechnology and Genomics U.P.M. - I.N.I.A., Campus de Montegancedo Pozuelo de Alarcón, Madrid, Spain.
Centre for Plant Biotechnology and Genomics · ESHospital Universitario de La Princesa · ESHospital Universitario Infanta Leonor · ESHospital Universitario Fundación Jiménez Díaz · ESUniversidad Politécnica de Madrid · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The physical, biochemical, and immunological characteristics of plant allergens have been widely studied, but no definite conclusion has been reached about what actually makes a protein an allergen. In this sense, N-glycosylation is an exclusive characteristic of plant allergens not present in mammals and it could be implied in allergenic sensitization. With this aim, we evaluated and compared the allergenic activity of the protein fraction and the N-glycan fraction of the thaumatin-like protein and the main kiwi allergen, Act d 2. The natural allergen, Act d 2, was deglycosylated by trifluoromethanesulfonic acid treatment; the N-glycan fraction was obtained by extended treatment with proteinase K. N-glycan- and protein- fractions were recognized by specific IgE of kiwi-allergic patients. By contrast, the sugar moiety showed a reduced capacity to activate basophils and T cells, but not dendritic cells derived from patients' monocytes. Related to this, the production of cytokines such as IL6 and IL10 was increased by the incubation of dendritic cells with sugar moiety. Thus, the sugar moiety plays a significant role in sensitization, inducing the activation of antigen-presenting cells, but it is the protein fraction that is responsible for the allergic reactions.

Indexed as

Act d 2allergen sensitizationcarbohydrate complex determinantN-glycosylationplant food allergythaumatin-like protein

Identifiers

PMID24936296
PMCPMC4048612
OpenAlexW2041411045

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.