Evidence map›Paper›PMID 22114713›Full record

ArticlePloS one2011

Allergenic lipid transfer proteins from plant-derived foods do not immunologically and clinically behave homogeneously: the kiwifruit LTP as a model.

Maria Livia Bernardi, Ivana Giangrieco, Laura Camardella, Rosetta Ferrara, Paola Palazzo, Maria Rosaria Panico, Roberta Crescenzo, Vito Carratore, Danila Zennaro, Marina Liso and 5 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. 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
3.6field-weighted citation impact, top 7% 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, 78 citations in OpenAlex.

  1. Trial
  2. IgE-mediated lipid transfer protein allergy in children.Pediatric allergy and immunology : official publication of the European Society of Pediatric Allergy and Immunology · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Epitope Mapping of Allergenic Lipid Transfer Proteins.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  13. Review
  14. Similar Allergenicity to DifferentMedicina (Kaunas, Lithuania) · 2019
    Article
  15. Component-Resolved Diagnosis in Food Allergies.Medicina (Kaunas, Lithuania) · 2019
    Review
  16. Article
  17. Plant-Made Bet v 1 for Molecular Diagnosis.Frontiers in plant science · 2019
    Article
  18. Anaphylactic reaction in patient allergic to mango.Allergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology · 2018
    Article
  19. Article
  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

15 authors at 2 institutions in 1 country.

Maria Livia BernardiCenter for Molecular Allergology, IDI-IRCCS, Rome, Italy.
Ivana Giangrieco
Laura Camardella
Rosetta Ferrara
Paola Palazzo
Maria Rosaria Panico
Roberta Crescenzo
Vito Carratore
Danila Zennaro
Marina Liso
Mario Santoro
Sara Zuzzi
Maurizio Tamburrini
Maria Antonietta Ciardiello
Adriano Mari
Istituti di Ricovero e Cura a Carattere Scientifico · ITInstitute of Protein Biochemistry · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundFood allergy is increasingly common worldwide. Tools for allergy diagnosis measuring IgE improved much since allergenic molecules and microarrays started to be used. IgE response toward allergens belonging to the same group of molecules has not been comprehensively explored using such approach yet.

objectiveUsing the model of lipid transfer proteins (LTPs) from plants as allergens, including two new structures, we sought to define how heterogeneous is the behavior of homologous proteins.

methodsTwo new allergenic LTPs, Act d 10 and Act c 10, have been identified in green (Actinidia deliciosa) and gold (Actinidia chinensis) kiwifruit (KF), respectively, using clinically characterized allergic patients, and their biochemical features comparatively evaluated by means of amino acid sequence alignments. Along with other five LTPs from peach, mulberry, hazelnut, peanut, mugwort, KF LTPs, preliminary tested positive for IgE, have been immobilized on a microarray, used for IgE testing 1,003 allergic subjects. Comparative analysis has been carried out.

resultsAlignment of Act d 10 primary structure with the other allergenic LTPs shows amino acid identities to be in a narrow range between 40 and 55%, with a number of substitutions making the sequences quite different from each other. Although peach LTP dominates the IgE immune response in terms of prevalence, epitope recognition driven by sequence heterogeneity has been recorded to be distributed in a wide range of behaviors. KF LTPs IgE positive results were obtained in a patient subset IgE positive for the peach LTP. Anyhow, the negative results on homologous molecules allowed us to reintroduce KF in patients' diet.

conclusionThe biochemical nature of allergenic molecule belonging to a group of homologous ones should not be taken as proof of immunological recognition as well. The availability of panels of homologous molecules to be tested using microarrays is valuable to address the therapeutic intervention.

Indexed as

ActinidiaAdolescentAdultAllergensAmino Acid SequenceAntigens, PlantBiomarkersCarrier ProteinsChromatography, High Pressure LiquidDouble-Blind MethodFemaleFood HypersensitivityFruitGene Expression ProfilingHumansImmunoglobulin EAllergensAntigens, PlantBiomarkersCarrier ProteinsImmunoglobulin Elipid transfer proteins, plantPlant Proteins

Identifiers

PMID22114713
PMCPMC3219694
OpenAlexW2002629927

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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.